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Conserved domains on  [gi|815890997|ref|NP_001295167|]
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ankyrin repeat domain-containing protein 29 isoform 2 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-232 8.75e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 8.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666   53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666  133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890997 172 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELLK 232
Cdd:COG0666  213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-232 8.75e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 8.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666   53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666  133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890997 172 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELLK 232
Cdd:COG0666  213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-141 1.51e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997   50 LMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEfrTKDGGTALLAASQYGHMQVVE 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 815890997  130 TLLKHGANIHDQ 141
Cdd:pfam12796  79 LLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 38-171 4.15e-21

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 92.62  E-value: 4.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTkdGGTALL 117
Cdd:PLN03192 550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLC 627

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 815890997 118 AASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 66-215 1.07e-11

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 64.65  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  66 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFgASTEFRTKD--GGTALLAASQYGHMQVVETLLKHG---AN--I 138
Cdd:cd22192    4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApelVNepM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 139 HDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADR 204
Cdd:cd22192   83 TSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162

                        170
                 ....*....|.
gi 815890997 205 DAARNDGTTAL 215
Cdd:cd22192  163 RAQDSLGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 71-220 8.84e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 8.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997   71 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTEFRTKDGGTALLAASQyGHMQVVETLLKHGANIH----------- 139
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  140 ---DQLYDGATALFLAAQGGYLDVIRLLLASGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 202
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 815890997  203 DRDAARNDGTTaLLKAAN 220
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 45-74 1.34e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.34e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 815890997    45 HGTTLLMVAAYAGHIDCVRELVLQGADINL 74
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-232 8.75e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 8.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666   53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666  133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890997 172 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELLK 232
Cdd:COG0666  213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-232 6.48e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.19  E-value: 6.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890997 172 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELLK 232
Cdd:COG0666  180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-215 1.19e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 1.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  15 AAFWAARRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDV 94
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  95 VRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQP 174
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 815890997 175 RQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTAL 215
Cdd:COG0666  249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-232 1.81e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 1.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALL 117
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 118 AASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVM 197
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 815890997 198 LLRGADRDAARNDGTTALLKAANKGYNDVIKELLK 232
Cdd:COG0666  173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-141 1.51e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997   50 LMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEfrTKDGGTALLAASQYGHMQVVE 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 815890997  130 TLLKHGANIHDQ 141
Cdd:pfam12796  79 LLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 38-171 4.15e-21

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 92.62  E-value: 4.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTkdGGTALL 117
Cdd:PLN03192 550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLC 627

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 815890997 118 AASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-173 8.74e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 8.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997   83 LFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANihDQLYDGATALFLAAQGGYLDVIR 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 815890997  163 LLLASGAKVNQ 173
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-203 2.24e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  116 LLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPrqDGTAPLWIASQMGHSEVVR 195
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*...
gi 815890997  196 VMLLRGAD 203
Cdd:pfam12796  79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
149-232 1.56e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  149 LFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVmLLRGADRDAaRNDGTTALLKAANKGYNDVIK 228
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL-LLEHADVNL-KDNGRTALHYAARSGHLEIVK 78


                  ....
gi 815890997  229 ELLK 232
Cdd:pfam12796  79 LLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
17-104 5.49e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 5.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997   17 FWAARRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVAAYAGHIDCVRELvLQGADINLQrESGTTALFFAAQQGHNDVVR 96
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLK-DNGRTALHYAARSGHLEIVK 78


                  ....*...
gi 815890997   97 FLFGFGAS 104
Cdd:pfam12796  79 LLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 38-236 7.81e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.46  E-value: 7.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHN-----DVVRFLFGFGASTEFRTKDG 112
Cdd:PHA03100  27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNG 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 113 GTALLAASQY--GHMQVVETLLKHGANIHDQLYDGATALFLAAQGGY--LDVIRLLLASGAKVNQ--------------- 173
Cdd:PHA03100 107 ITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAknrvnyllsygvpin 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815890997 174 -PRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELLKFSPT 236
Cdd:PHA03100 187 iKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 37-231 5.15e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 5.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  37 VDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL 116
Cdd:PHA02874 115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 117 LAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQggYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHS-EVVR 195
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDiDIID 272

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 815890997 196 VMLLRGADRDAARNDGTTAL---LKAANKgyNDVIKELL 231
Cdd:PHA02874 273 ILLYHKADISIKDNKGENPIdtaFKYINK--DPVIKDII 309
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 151-256 2.15e-12

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 66.85  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 151 LAAQGGYLDvIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKEL 230
Cdd:PTZ00322  89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                         90       100
                 ....*....|....*....|....*.
gi 815890997 231 LKFSPTLGILKANELPAELTKNERIL 256
Cdd:PTZ00322 168 SRHSQCHFELGANAKPDSFTGKPPSL 193
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 66-215 1.07e-11

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 64.65  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  66 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFgASTEFRTKD--GGTALLAASQYGHMQVVETLLKHG---AN--I 138
Cdd:cd22192    4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApelVNepM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 139 HDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADR 204
Cdd:cd22192   83 TSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162

                        170
                 ....*....|.
gi 815890997 205 DAARNDGTTAL 215
Cdd:cd22192  163 RAQDSLGNTVL 173
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-203 6.65e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 6.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  53 AAYAGHIDCVRELVLQGADIN-LQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETL 131
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815890997 132 LKHGA--NIHDQLydGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDG-TAPLWIASQMGHSEVVRVMLLRGAD 203
Cdd:PHA02875 155 IDHKAclDIEDCC--GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 5-206 7.73e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 7.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997   5 SFKKETPLanaaFWAARRGNLALLKLLLNSGRVDVDCRDS-HGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTAL 83
Cdd:PHA02876 304 NIKGETPL----YLMAKNGYDTENIRTLIMLGADVNAADRlYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPI 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  84 FFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL-LAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGG-YLDVI 161
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTALhFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVI 459

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 815890997 162 RLLLASGAKVNQPRQDGTAPLWIAsqMGHSEVVRVMLLRGAD-RDA 206
Cdd:PHA02876 460 EMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAElRDS 503
Ank_4 pfam13637
Ankyrin repeats (many copies);
46-98 1.57e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.57e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 815890997   46 GTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 98
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 62-223 2.36e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  62 VRELVLQGADINLQ-RESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHD 140
Cdd:PHA02878 150 TKLLLSYGADINMKdRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 141 QLYDGATALFLAAqgGYL---DVIRLLLASGAKVN-QPRQDGTAPLWIASqmgHSE-VVRVMLLRGADRDAARNDGTTAL 215
Cdd:PHA02878 230 RDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNaKSYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPL 304


                 ....*...
gi 815890997 216 LKAANKGY 223
Cdd:PHA02878 305 SSAVKQYL 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 47-231 2.86e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 2.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  47 TTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEF------------------- 107
Cdd:PHA02874  36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgi 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 108 ----RTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLW 183
Cdd:PHA02874 116 dvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 815890997 184 IASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANkgYNDVIKELL 231
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELL 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
 38-219 2.88e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  38 DVDCRDSHGTTLLMVAAYAGHIDC---VRELVLQGADINLQRESGTTALFFAAQQGHN-DVVRFLFGFGASTEFRTKDGG 113
Cdd:PHA03095  39 DVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGR 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 114 TALLA--ASQYGHMQVVETLLKHGANIHDQLYDGATAL--FLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMG 189
Cdd:PHA03095 119 TPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSF 198

                        170       180       190
                 ....*....|....*....|....*....|..
gi 815890997 190 HS--EVVRVMLLRGADRDAARNDGTTALLKAA 219
Cdd:PHA03095 199 KPraRIVRELIRAGCDPAATDMLGNTPLHSMA 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-231 4.44e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 4.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  59 IDCVRELVLQGADINLQRESGTTALffaAQQGHN------DVVRFLFGFGASTEFRTKDGGTALLAASQYGH-MQVVETL 131
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 132 LKHGANIHDQLYDGATAL--FLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPL--WIASQMGHSEVVRVMLLRGADRDAA 207
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAV 183

                        170       180
                 ....*....|....*....|....*.
gi 815890997 208 RNDGTTALLKAAN--KGYNDVIKELL 231
Cdd:PHA03095 184 DDRFRSLLHHHLQsfKPRARIVRELI 209
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 62-233 7.77e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.92  E-value: 7.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  62 VRELVLQ-GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHD 140
Cdd:PHA02876 160 IAEMLLEgGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 141 Q------------------LYDGA-----------TALFLAAQGGYLD-VIRLLLASGAKVNQPRQDGTAPLWIASQMGH 190
Cdd:PHA02876 240 NdlsllkairnedletsllLYDAGfsvnsiddcknTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGY 319

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 815890997 191 -SEVVRVMLLRGADRDAARNDGTTALLKAAN-KGYNDVIKELLKF 233
Cdd:PHA02876 320 dTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLEL 364
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 112-231 8.97e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 8.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 112 GGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASgAKVNQPRQDGTApLWIASQMGHS 191
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDL 635

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 815890997 192 EVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELL 231
Cdd:PLN03192 636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 90-239 1.07e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  90 GHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGA 169
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890997 170 KVNQP-RQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELLKFSPTLGI 239
Cdd:PHA02875  93 FADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-165 1.35e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.35e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 815890997  112 GGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 165
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 38-185 1.86e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 1.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  38 DVDCRDSH-GTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL 116
Cdd:PHA02878 159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890997 117 -LAASQYGHMQVVETLLKHGANIHDQLY-DGATALFLAAQGGylDVIRLLLASGAKVNQPRQDGTAPLWIA 185
Cdd:PHA02878 239 hISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 19-172 2.06e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  19 AARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 98
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815890997  99 FGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDG-ATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:PHA02875 155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 110-232 8.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 8.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 110 KDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMG 189
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 815890997 190 HSEVVRVMLLRGADRD-AARNDGTTALLKAANKGYNDVIKELLK 232
Cdd:PHA02875 180 DIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIK 223
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 9-193 1.12e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.40  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997   9 ETPLanaaFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGH-------IDCVRELVLQGADINLQResGTT 81
Cdd:cd22192   18 ESPL----LLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNleaavvlMEAAPELVNEPMTSDLYQ--GET 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  82 ALFFAAQQGHNDVVRFLFGFGAS--------TEFRTkdGGTALL---------AASQyGHMQVVETLLKHGANIHDQLYD 144
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGADvvspratgTFFRP--GPKNLIyygehplsfAACV-GNEEIVRLLIEHGADIRAQDSL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 815890997 145 GATAL-FLAAQGGYL---DVIRLLLASGAKVNQ------PRQDGTAPLWIASQMGHSEV 193
Cdd:cd22192  169 GNTVLhILVLQPNKTfacQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVM 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 34-100 7.48e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 7.48e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815890997  34 SGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFG 100
Cdd:PTZ00322 103 TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-86 7.98e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 7.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 815890997   35 GRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFA 86
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
182-233 9.74e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 9.74e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 815890997  182 LWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELLKF 233
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 62-151 1.09e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  62 VRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKH------- 134
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfel 177

                         90
                 ....*....|....*..
gi 815890997 135 GANIHDQLYDGATALFL 151
Cdd:PTZ00322 178 GANAKPDSFTGKPPSLE 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
79-132 1.27e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.27e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 815890997   79 GTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLL 132
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 126-259 1.95e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 126 QVVETLLKHGA--NIHDQlYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAD 203
Cdd:PHA02878 148 EITKLLLSYGAdiNMKDR-HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890997 204 RDAARNDGTTALLKAANKGYN-DVIKELLKFSPTLG----ILKANELPAELtKNERILRLL 259
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNaksyILGLTALHSSI-KSERKLKLL 286
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 117-198 3.32e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 117 LAASqyGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRV 196
Cdd:PTZ00322  89 LAAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 ..
gi 815890997 197 ML 198
Cdd:PTZ00322 167 LS 168
PHA03095 PHA03095
ankyrin-like protein; Provisional
 38-235 3.36e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  38 DVDCRDSHGTT-LLMVAAYAGHIDCVRELVLQGADINLQRESGTTAL--FFAAQQGHNDVVRFLFGFGASTEFRTKDGGT 114
Cdd:PHA03095  75 DVNAPERCGFTpLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMT 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 115 AL--LAASQYGHMQVVETLLKHGANIHD-----------------------------------QLYDGATALFLAAQGGY 157
Cdd:PHA03095 155 PLavLLKSRNANVELLRLLIDAGADVYAvddrfrsllhhhlqsfkprarivreliragcdpaaTDMLGNTPLHSMATGSS 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 158 LD--VIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELLKFSP 235
Cdd:PHA03095 235 CKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNP 314
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-172 4.06e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  37 VDVDCRDSHGTTLLMVAAYA--GHIDCVRELVLQGADINLQRESGTTALFFAAQQGHND--VVRFLF------------- 99
Cdd:PHA03100  97 ANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIdkgvdinaknrvn 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815890997 100 ---GFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:PHA03100 177 yllSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 18-233 5.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 5.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  18 WAARRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINlqreSGTTALFFAAQQGHNDVVRF 97
Cdd:PHA02876 184 YAAERGNAKMVNLLLSYG-ADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLETSLL 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  98 LFGFGASTEFRTKDGGTALLAASQYGHM-QVVETLLKHGANIHDQLYDGATALFLAAQGGY-LDVIRLLLASGAKVNQPR 175
Cdd:PHA02876 259 LYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAAD 338

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 815890997 176 QDGTAPLWIASQMG-HSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELLKF 233
Cdd:PHA02876 339 RLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 95-165 1.49e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.49e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890997  95 VRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 165
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-75 2.21e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 2.21e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815890997   14 NAAFWAARRGNLALLKLLLNSGRVDVDCrdsHGTTLLMVAAYAGHIDCVRELVLQGADINLQ 75
Cdd:pfam12796  32 TALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-198 4.40e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 4.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 815890997  147 TALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVML 198
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 93-240 5.26e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 5.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  93 DVVRFLFGFGASTEFRTKDGG-TALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890997 172 NQPRQDGTAPLWIA-SQMGHSEVVRVMLLRGADRDAARN-DGTTALLKAANKgyNDVIKELLKFSPTLGIL 240
Cdd:PHA02878 228 DARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSL 296
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 55-232 2.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  55 YAGHIDCVRELV-LQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLK 133
Cdd:PHA02874  10 YSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 134 HGANIHdqlydgatalFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTT 213
Cdd:PHA02874  90 NGVDTS----------ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159

                        170
                 ....*....|....*....
gi 815890997 214 ALLKAANKGYNDVIKELLK 232
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLE 178
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-107 2.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 2.71e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890997  37 VDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEF 107
Cdd:PHA03100 183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02798 PHA02798
ankyrin-like protein; Provisional
 125-232 5.18e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 5.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 125 MQVVETLLKHGANIHDQLYDGATAL--FLAAQGGY---LDVIRLLLASGAKVNQPRQDGTAPLWIA---SQMGHSEVVRV 196
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLctILSNIKDYkhmLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLF 130

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 815890997 197 MLLRGADRDAARNDGTTAL---LKAANKGYNDVIKELLK 232
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLqvyLQSNHHIDIEIIKLLLE 169
PHA02798 PHA02798
ankyrin-like protein; Provisional
 59-173 5.42e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  59 IDCVRELVLQGADIN-LQRESGT---TALFFAAQQGHN-DVVRFLFGFGASTEFRTKDGGT---ALLAASQYGHMQVVET 130
Cdd:PHA02798  51 TDIVKLFINLGANVNgLDNEYSTplcTILSNIKDYKHMlDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 815890997 131 LLKHGANIHDQLYDGATALFLAAQGGY---LDVIRLLLASGAKVNQ 173
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINT 176
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 71-220 8.84e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 8.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997   71 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTEFRTKDGGTALLAASQyGHMQVVETLLKHGANIH----------- 139
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  140 ---DQLYDGATALFLAAQGGYLDVIRLLLASGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 202
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 815890997  203 DRDAARNDGTTaLLKAAN 220
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 112-221 1.15e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 112 GGTALLAASQYGHMQVVETL------------LKHGAN--IHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVnQPRQD 177
Cdd:cd21882   26 GKTCLHKAALNLNDGVNEAImllleaapdsgnPKELVNapCTDEFYQGQTALHIAIENRNLNLVRLLVENGADV-SARAT 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815890997 178 GTA--------------PLWIASQMGHSEVVRVMLLRGAD------RDAARNDGTTALLKAANK 221
Cdd:cd21882  105 GRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaleaQDSLGNTVLHALVLQADN 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 45-74 1.34e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.34e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 815890997    45 HGTTLLMVAAYAGHIDCVRELVLQGADINL 74
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
70-116 1.42e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 1.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 815890997   70 ADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL 116
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 111-141 1.60e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 1.60e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 815890997  111 DGGTAL-LAASQYGHMQVVETLLKHGANIHDQ 141
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-166 2.96e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997   41 CRDSHGTTLLMVAAYAGHIDCVRELVLQGADINL-------QRESGTTALF-------FAAQQGHNDVVRFLFGFGASte 106
Cdd:TIGR00870 123 SEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFYhgesplnAAACLGSPSIVALLSEDPAD-- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  107 frtkdggtaLLAASQYG----HMQVVET----------------LLKHGANIHDQL-------YDGATALFLAAQGGYLD 159
Cdd:TIGR00870 201 ---------ILTADSLGntllHLLVMENefkaeyeelscqmynfALSLLDKLRDSKelevilnHQGLTPLKLAAKEGRIV 271


                  ....*..
gi 815890997  160 VIRLLLA 166
Cdd:TIGR00870 272 LFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 144-172 5.56e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 5.56e-04
                           10        20
                   ....*....|....*....|....*....
gi 815890997   144 DGATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 45-75 5.60e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 5.60e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 815890997   45 HGTTLLMVAAY-AGHIDCVRELVLQGADINLQ 75
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
Ank_4 pfam13637
Ankyrin repeats (many copies);
178-231 6.43e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 6.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 815890997  178 GTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELL 231
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 125-259 8.41e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.39  E-value: 8.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 125 MQVVETLLKHGANIHdqlYDGA---TAL--FLAAQGG-YLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSE-VVRVM 197
Cdd:PHA03095  27 VEEVRRLLAAGADVN---FRGEygkTPLhlYLHYSSEkVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLL 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 198 LLRGADRDAARNDGTTAL-LKAANKGYN-DVIKELLKFSPTLGILKANELP--AELTKNER----ILRLL 259
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLhVYLSGFNINpKVIRLLLRKGADVNALDLYGMTplAVLLKSRNanveLLRLL 173
PHA03095 PHA03095
ankyrin-like protein; Provisional
 37-96 1.17e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 1.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  37 VDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVR 96
Cdd:PHA03095 248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 111-140 1.78e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 1.78e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 815890997   111 DGGTALLAASQYGHMQVVETLLKHGANIHD 140
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 37-133 1.97e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  37 VDVDCRDSHGTTLLMVAAYagHIDCVRELVLQ----GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDG 112
Cdd:PHA03095 213 CDPAATDMLGNTPLHSMAT--GSSCKRSLVLPlliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290

                         90       100
                 ....*....|....*....|.
gi 815890997 113 GTALLAASQYGHMQVVETLLK 133
Cdd:PHA03095 291 NTPLSLMVRNNNGRAVRAALA 311
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 114-223 2.77e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 38.84  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 114 TALLAASQYGHMQVVETLLK-HGANIHDQLYDGATALFLAAQGGYLDVIRLLL-ASGAKVNQPRQ----DGTAPLWIASQ 187
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeAAPELVNEPMTsdlyQGETALHIAVV 98

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 815890997 188 MGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGY 223
Cdd:cd22192   99 NQNLNLVRELIARGADVVSPRATGTFFRPGPKNLIY 134
PHA02795 PHA02795
ankyrin-like protein; Provisional
 38-90 2.87e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 38.82  E-value: 2.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 815890997  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQG 90
Cdd:PHA02795 213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
PHA02798 PHA02798
ankyrin-like protein; Provisional
 47-139 4.06e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.28  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997  47 TTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH---NDVVRFLFGFGASTEFRTKDGGTALLAASQYG 123
Cdd:PHA02798  77 TILSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSN 156

                         90
                 ....*....|....*....
gi 815890997 124 H---MQVVETLLKHGANIH 139
Cdd:PHA02798 157 HhidIEIIKLLLEKGVDIN 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 114-243 5.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.64  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890997 114 TALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKvnqprqdgTAPLWIASQmgHSEV 193
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD--------TSILPIPCI--EKDM 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 815890997 194 VRVMLLRGADRDAARNDGTTALLKAANKGYNDVIKELLKFSPTLGILKAN 243
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN 156
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-73 9.47e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.00  E-value: 9.47e-03
                          10        20
                  ....*....|....*....|....*.
gi 815890997   48 TLLMVAAYAGHIDCVRELVLQGADIN 73
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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