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Conserved domains on  [gi|1394533390|ref|NP_001350768|]
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ankyrin repeat domain-containing protein 54 isoform 3 [Homo sapiens]

Protein Classification

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

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-96 2.77e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 2.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALD 86
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                          90
                  ....*....|
gi 1394533390  87 RAGRTPLHLA 96
Cdd:COG0666   184 NDGETPLHLA 193
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 34-180 4.59e-05

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 4.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  34 GNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSK-----LNILQE--- 105
Cdd:PLN03192  536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkiFRILYHfas 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390 106 -------GHAQCLEAVRLEVKqiihMLREYLeRLGQHEQRERLDDLcTRLQMTSTKEQVDEVTDLL---ASFTSLSL--Q 173
Cdd:PLN03192  616 isdphaaGDLLCTAAKRNDLT----AMKELL-KQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLImngADVDKANTddD 689


                  ....*..
gi 1394533390 174 MQSMEKR 180
Cdd:PLN03192  690 FSPTELR 696
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-96 2.77e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 2.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALD 86
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                          90
                  ....*....|
gi 1394533390  87 RAGRTPLHLA 96
Cdd:COG0666   184 NDGETPLHLA 193
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-96 2.52e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 2.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALH-FA-SCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAA--CTNHVPVITTLLRGGARVDA 84
Cdd:PHA03095  173 LIDAGADVYAVDDRFRSLLHhHLqSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINA 252

                          90
                  ....*....|..
gi 1394533390  85 LDRAGRTPLHLA 96
Cdd:PHA03095  253 RNRYGQTPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-86 2.93e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 2.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHgADPNQRDGlGNTPLHLAACTNHVPVITTLLRGGARVDALD 86
Cdd:pfam12796  14 KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 22-94 1.37e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 59.05  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGADPNQR------------DG--LGNTPLHLAACTNHVPVITTLLRG---GARVDA 84
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkkkkggPGfyFGELPLSLAACTNQLDIVKFLLENphsPADISA 172

                          90
                  ....*....|
gi 1394533390  85 LDRAGRTPLH 94
Cdd:cd22196   173 RDSMGNTVLH 182
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 22-97 2.16e-07

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: 49.69  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGADPNQR------------DGL--GNTPLHLAACTNHVPVITTLLRGGARVDALDR 87
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSFyhGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90
                  ....*....|
gi 1394533390  88 AGRTPLHLAK 97
Cdd:TIGR00870 207 LGNTLLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 22-50 1.28e-06

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: 42.96  E-value: 1.28e-06
                           10        20
                   ....*....|....*....|....*....
gi 1394533390   22 KGRTALHFASCNGNDQIVQLLLDHGADPN 50
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 34-180 4.59e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 4.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  34 GNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSK-----LNILQE--- 105
Cdd:PLN03192  536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkiFRILYHfas 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390 106 -------GHAQCLEAVRLEVKqiihMLREYLeRLGQHEQRERLDDLcTRLQMTSTKEQVDEVTDLL---ASFTSLSL--Q 173
Cdd:PLN03192  616 isdphaaGDLLCTAAKRNDLT----AMKELL-KQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLImngADVDKANTddD 689


                  ....*..
gi 1394533390 174 MQSMEKR 180
Cdd:PLN03192  690 FSPTELR 696
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-96 2.77e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 2.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALD 86
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                          90
                  ....*....|
gi 1394533390  87 RAGRTPLHLA 96
Cdd:COG0666   184 NDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-101 7.19e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 7.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALD 86
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                          90
                  ....*....|....*
gi 1394533390  87 RAGRTPLHLAKSKLN 101
Cdd:COG0666   217 NDGKTALDLAAENGN 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-96 8.03e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.64  E-value: 8.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRA 88
Cdd:COG0666    73 LLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND 152


                  ....*...
gi 1394533390  89 GRTPLHLA 96
Cdd:COG0666   153 GNTPLHLA 160
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-109 1.88e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALD 86
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                          90       100
                  ....*....|....*....|...
gi 1394533390  87 RAGRTPLHLAKSKLNILQEGHAQ 109
Cdd:COG0666   250 KDGLTALLLAAAAGAALIVKLLL 272
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-96 2.52e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 2.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALH-FA-SCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAA--CTNHVPVITTLLRGGARVDA 84
Cdd:PHA03095  173 LIDAGADVYAVDDRFRSLLHhHLqSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINA 252

                          90
                  ....*....|..
gi 1394533390  85 LDRAGRTPLHLA 96
Cdd:PHA03095  253 RNRYGQTPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-86 2.93e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 2.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHgADPNQRDGlGNTPLHLAACTNHVPVITTLLRGGARVDALD 86
Cdd:pfam12796  14 KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 9-100 4.40e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.61  E-value: 4.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAAD-DKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDR 87
Cdd:PHA02878  153 LLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232

                          90
                  ....*....|...
gi 1394533390  88 AGRTPLHLAKSKL 100
Cdd:PHA02878  233 CGNTPLHISVGYC 245
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-124 2.05e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.83  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADPNQRDGLGNTPLHlAACTN---HVPVITTLLRGGARVDA 84
Cdd:PHA03095   69 LLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNA 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1394533390  85 LDRAGRTPLHlaksklnILQEGHAQCLEAVRLEVKQIIHM 124
Cdd:PHA03095  148 LDLYGMTPLA-------VLLKSRNANVELLRLLIDAGADV 180
Ank_2 pfam12796
Ankyrin repeats (3 copies);
27-112 9.15e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 9.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  27 LHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRgGARVDALDRaGRTPLHLAksklniLQEG 106
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYA------ARSG 72


                  ....*.
gi 1394533390 107 HAQCLE 112
Cdd:pfam12796  73 HLEIVK 78
PHA03095 PHA03095
ankyrin-like protein; Provisional
 8-102 3.92e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 3.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   8 QLLEDGADPCAADDKGRTALH-FASCNGND--QIVQLLLDHGADPNQRDGLGNTPLHLAACTNHV-PVITTLLRGGARVD 83
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLHlYLHYSSEKvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVN 111

                          90
                  ....*....|....*....
gi 1394533390  84 ALDRAGRTPLHLAKSKLNI 102
Cdd:PHA03095  112 AKDKVGRTPLHVYLSGFNI 130
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-96 4.57e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALH----FASCNgnDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDA 84
Cdd:PHA03095  208 LIRAGCDPAATDMLGNTPLHsmatGSSCK--RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285

                          90
                  ....*....|..
gi 1394533390  85 LDRAGRTPLHLA 96
Cdd:PHA03095  286 VSSDGNTPLSLM 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 9-87 4.02e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.23  E-value: 4.02e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDR 87
Cdd:PHA03100  178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 31-96 6.60e-13

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.69  E-value: 6.60e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533390  31 SCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 96
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-96 6.90e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 6.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   3 MMWKQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARV 82
Cdd:COG0666    34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                          90
                  ....*....|....
gi 1394533390  83 DALDRAGRTPLHLA 96
Cdd:COG0666   114 NARDKDGETPLHLA 127
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 8-103 1.66e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.70  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   8 QLLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADPNQRDGLGNTPLHLAACTN-HVPVITTLLRGGARVDAL 85
Cdd:PHA02876  292 KLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNAR 371

                          90
                  ....*....|....*...
gi 1394533390  86 DRAGRTPLHLAKSKLNIL 103
Cdd:PHA02876  372 DYCDKTPIHYAAVRNNVV 389
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 9-96 1.71e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRA 88
Cdd:PHA02874  110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189


                  ....*...
gi 1394533390  89 GRTPLHLA 96
Cdd:PHA02874  190 GESPLHNA 197
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 9-77 4.21e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.38  E-value: 4.21e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLR 77
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 9-104 7.08e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 7.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNG-----NDQIVQLLLDHGADPNQRDGLGNTPLHLAACT--NHVPVITTLLRGGAR 81
Cdd:PHA03100   54 LLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGAN 133

                          90       100
                  ....*....|....*....|....*..
gi 1394533390  82 VDALDRAGRTPLHLA----KSKLNILQ 104
Cdd:PHA03100  134 VNIKNSDGENLLHLYlesnKIDLKILK 160
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 7-96 1.11e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASC-NGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDAL 85
Cdd:PHA02876  325 RTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404

                          90
                  ....*....|.
gi 1394533390  86 DRAGRTPLHLA 96
Cdd:PHA02876  405 SQKIGTALHFA 415
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 9-96 2.48e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALH-FASCNGND-QIVQLLLDHGADPNQ----------------RDGLGNTPLHLAACTNHVP 70
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHlYLESNKIDlKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPE 206

                          90       100
                  ....*....|....*....|....*.
gi 1394533390  71 VITTLLRGGARVDALDRAGRTPLHLA 96
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIA 232
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 7-108 3.48e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPL----------------HLAA------ 64
Cdd:PLN03192  542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyHFASisdpha 621

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1394533390  65 -----CT----NHVPVITTLLRGGARVDALDRAGRTPLHLAksklniLQEGHA 108
Cdd:PLN03192  622 agdllCTaakrNDLTAMKELLKQGLNVDSEDHQGATALQVA------MAEDHV 668
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-93 1.07e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRA 88
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284


                  ....*
gi 1394533390  89 GRTPL 93
Cdd:COG0666   285 LLTLL 289
PHA02946 PHA02946
ankyin-like protein; Provisional
 7-93 1.16e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 59.30  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNH--VPVITTLLRGGARV-D 83
Cdd:PHA02946   56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInN 135

                          90
                  ....*....|
gi 1394533390  84 ALDRAGRTPL 93
Cdd:PHA02946  136 SVDEEGCGPL 145
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 22-94 1.37e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 59.05  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGADPNQR------------DG--LGNTPLHLAACTNHVPVITTLLRG---GARVDA 84
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkkkkggPGfyFGELPLSLAACTNQLDIVKFLLENphsPADISA 172

                          90
                  ....*....|
gi 1394533390  85 LDRAGRTPLH 94
Cdd:cd22196   173 RDSMGNTVLH 182
Ank_4 pfam13637
Ankyrin repeats (many copies);
23-76 1.71e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 1.71e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533390  23 GRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLL 76
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 27-102 1.94e-10

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: 58.49  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  27 LHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLH-LAACTNHVPV------ITTLLRGG--ARVDAL-DRAGRTPLHLA 96
Cdd:cd22192   140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQPNKTFAcqmydlILSYDKEDdlQPLDLVpNNQGLTPFKLA 219


                  ....*.
gi 1394533390  97 KSKLNI 102
Cdd:cd22192   220 AKEGNI 225
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 22-95 9.25e-10

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: 56.56  E-value: 9.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGADPNQ-----------RDGL---GNTPLHLAACTNHVPVITTLLRGGARVDALDR 87
Cdd:cd22192    88 QGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167


                  ....*...
gi 1394533390  88 AGRTPLHL 95
Cdd:cd22192   168 LGNTVLHI 175
PHA03095 PHA03095
ankyrin-like protein; Provisional
 38-95 1.07e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.19  E-value: 1.07e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533390  38 IVQLLLDHGADPNQRDGLGNTPLHLAACTNHVP---VITTLLRGGARVDALDRAGRTPLHL 95
Cdd:PHA03095   29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHL 89
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 9-103 1.59e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQI-VQLLLDHGADPNQRDGLGNTPLHLAACTNHVP-VITTLLRGGARVDALD 86
Cdd:PHA02876  394 LLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAIN 473

                          90       100
                  ....*....|....*....|
gi 1394533390  87 RAGRTPLHLA---KSKLNIL 103
Cdd:PHA02876  474 IQNQYPLLIAleyHGIVNIL 493
Ank_5 pfam13857
Ankyrin repeats (many copies);
9-63 1.68e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533390   9 LLEDG-ADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLA 63
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 9-96 1.91e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRA 88
Cdd:PHA02874  143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN 222


                  ....*...
gi 1394533390  89 GRTPLHLA 96
Cdd:PHA02874  223 GFTPLHNA 230
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 22-94 2.17e-08

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: 52.57  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGAD-----------PNQRDGL--GNTPLHLAACTNHVPVITTLLRGGARVDAL--- 85
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADvsaratgrffrKSPGNLFyfGELPLSLAACTNQEEIVRLLLENGAQPAALeaq 151


                  ....*....
gi 1394533390  86 DRAGRTPLH 94
Cdd:cd21882   152 DSLGNTVLH 160
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 22-102 2.78e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLN 101
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180


                  .
gi 1394533390 102 I 102
Cdd:PHA02875  181 I 181
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 37-101 3.20e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 3.20e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533390  37 QIVQLLLDHGADPNQRD-GLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLN 101
Cdd:PHA02878  148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN 213
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 9-102 5.98e-08

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: 51.42  E-value: 5.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGAD-------------PCAADDKGRTALHFASCNGNDQIVQLLLDHGADP---NQRDGLGNTPLH-LAACTNHVPV 71
Cdd:cd21882    92 LVENGADvsaratgrffrksPGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHaLVLQADNTPE 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1394533390  72 ITT--------LLRGGARVDAL-------DRAGRTPLHLAKSKLNI 102
Cdd:cd21882   172 NSAfvcqmynlLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGKI 217
PHA03095 PHA03095
ankyrin-like protein; Provisional
 7-88 8.58e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 8.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALD 86
Cdd:PHA03095  241 LPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320


                  ..
gi 1394533390  87 RA 88
Cdd:PHA03095  321 AT 322
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 22-94 9.91e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all 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.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 50.56  E-value: 9.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGADPN------------QRDG--LGNTPLHLAACTNHVPVITTLLRGG---ARVDA 84
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHahakgrffqpkyQGEGfyFGELPLSLAACTNQPDIVQYLLENEhqpADIEA 154

                          90
                  ....*....|
gi 1394533390  85 LDRAGRTPLH 94
Cdd:cd22193   155 QDSRGNTVLH 164
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-89 1.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRA 88
Cdd:PHA02875  121 LIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN 200


                  .
gi 1394533390  89 G 89
Cdd:PHA02875  201 G 201
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 22-94 1.77e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all 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.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 50.14  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGADPN------------QRDG--LGNTPLHLAACTNHVPVITTLL-RGGARVDALD 86
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpkyKHEGfyFGETPLALAACTNQPEIVQLLMeKESTDITSQD 219


                  ....*...
gi 1394533390  87 RAGRTPLH 94
Cdd:cd22194   220 SRGNTVLH 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 22-53 1.91e-07

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: 45.36  E-value: 1.91e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1394533390  22 KGRTALHFASC-NGNDQIVQLLLDHGADPNQRD 53
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 9-96 2.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVitTLLRGGARVDALDRA 88
Cdd:PHA02874  176 LLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDID 253


                  ....*...
gi 1394533390  89 GRTPLHLA 96
Cdd:PHA02874  254 GSTPLHHA 261
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 38-99 2.06e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 2.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533390  38 IVQLLLDHGADPNQRDGLGNTPLHLAACTNHV-----PVITTLLRGGARVDALDRAGRTPLHLAKSK 99
Cdd:PHA03100   50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 22-97 2.16e-07

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: 49.69  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGADPNQR------------DGL--GNTPLHLAACTNHVPVITTLLRGGARVDALDR 87
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSFyhGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90
                  ....*....|
gi 1394533390  88 AGRTPLHLAK 97
Cdd:TIGR00870 207 LGNTLLHLLV 216
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 9-96 2.69e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.49  E-value: 2.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADPNQRDG-LGNTPLHLAActnHVP-VITTLLRGGARVDAL 85
Cdd:PHA02878  220 LLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSI---KSErKLKLLLEYGADINSL 296

                          90
                  ....*....|.
gi 1394533390  86 DRAGRTPLHLA 96
Cdd:PHA02878  297 NSYKLTPLSSA 307
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 40-110 3.52e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 47.56  E-value: 3.52e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533390  40 QLLLDHGADPNQRDGL-GNTPLHLAACTNHVPVITTLLRG-GARVDALDRAGRTPLHLAKSK-----LNILQEGHAQC 110
Cdd:PHA02736   75 KLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERhdakmMNILRAKGAQC 152
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 9-98 4.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGN-DQIVQLLLDHGADPNQRDGLGNTPLHLAACTNH-VPVITTLLRGGARVDALD 86
Cdd:PHA02876  259 LYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAAD 338

                          90
                  ....*....|..
gi 1394533390  87 RAGRTPLHLAKS 98
Cdd:PHA02876  339 RLYITPLHQAST 350
PHA02946 PHA02946
ankyin-like protein; Provisional
 35-94 4.49e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.90  E-value: 4.49e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  35 NDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLH 94
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY 110
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 20-93 5.03e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 48.75  E-value: 5.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  20 DDKGRTALH--FASCNGNDQIVQLLLDHGADPNQRDGLGNTPLH-----------LAACTNH---VPVITTLLRGGARVD 83
Cdd:PHA02716  314 DSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvniLDPETDNdirLDVIQCLISLGADIT 393

                          90
                  ....*....|
gi 1394533390  84 ALDRAGRTPL 93
Cdd:PHA02716  394 AVNCLGYTPL 403
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 22-94 6.30e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 48.31  E-value: 6.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGADPNQRDG-------------LGNTPLHLAACTNHVPVITTLLRGG---ARVDAL 85
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYLLENPhqpASLQAQ 172


                  ....*....
gi 1394533390  86 DRAGRTPLH 94
Cdd:cd22197   173 DSLGNTVLH 181
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 6-82 1.15e-06

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: 47.70  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   6 KQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDhgADP---NQRDG----LGNTPLHLAACTNHVPVITTLLRG 78
Cdd:cd22192    34 KKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPelvNEPMTsdlyQGETALHIAVVNQNLNLVRELIAR 111


                  ....
gi 1394533390  79 GARV 82
Cdd:cd22192   112 GADV 115
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 22-50 1.28e-06

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: 42.96  E-value: 1.28e-06
                           10        20
                   ....*....|....*....|....*....
gi 1394533390   22 KGRTALHFASCNGNDQIVQLLLDHGADPN 50
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
42-96 1.34e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533390  42 LLDHG-ADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 96
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 7-86 8.06e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 8.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   7 QQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPN--QRDGLgnTPLHLAACTNHVPVITTLLRGGARVDA 84
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiiALDDL--SVLECAVDSKNIDTIKAIIDNRSNINK 239


                  ..
gi 1394533390  85 LD 86
Cdd:PHA02876  240 ND 241
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 22-50 1.85e-05

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: 39.93  E-value: 1.85e-05
                          10        20
                  ....*....|....*....|....*....
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGADPN 50
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 23-102 2.03e-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: 43.92  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  23 GRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITT---------LLRGGARVDA-------LD 86
Cdd:TIGR00870 175 GESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEYEelscqmynfALSLLDKLRDskeleviLN 254

                          90
                  ....*....|....*.
gi 1394533390  87 RAGRTPLHLAKSKLNI 102
Cdd:TIGR00870 255 HQGLTPLKLAAKEGRI 270
Ank_4 pfam13637
Ankyrin repeats (many copies);
9-43 3.28e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 3.28e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQIVQLLL 43
Cdd:pfam13637  20 LLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 34-180 4.59e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 4.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  34 GNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSK-----LNILQE--- 105
Cdd:PLN03192  536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkiFRILYHfas 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390 106 -------GHAQCLEAVRLEVKqiihMLREYLeRLGQHEQRERLDDLcTRLQMTSTKEQVDEVTDLL---ASFTSLSL--Q 173
Cdd:PLN03192  616 isdphaaGDLLCTAAKRNDLT----AMKELL-KQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLImngADVDKANTddD 689


                  ....*..
gi 1394533390 174 MQSMEKR 180
Cdd:PLN03192  690 FSPTELR 696
Ank_4 pfam13637
Ankyrin repeats (many copies);
56-112 5.30e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 5.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533390  56 GNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAksklniLQEGHAQCLE 112
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA------ASNGNVEVLK 51
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 35-96 5.64e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 5.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533390  35 NDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 96
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 22-94 1.30e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). 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.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 41.76  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  22 KGRTALHFASCNGNDQIVQLLLDHGAD-----------PNQRDG---LGNTPLHLAACTNHVPVITTLLRGGARVDAL-- 85
Cdd:cd22195   136 RGQTALHIAIERRCKHYVELLVEKGADvhaqargrffqPKDEGGyfyFGELPLSLAACTNQPDIVHYLTENAHKKADLrr 215

                          90
                  ....*....|
gi 1394533390  86 -DRAGRTPLH 94
Cdd:cd22195   216 qDSRGNTVLH 225
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 56-87 1.35e-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: 37.65  E-value: 1.35e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1394533390  56 GNTPLHLAAC-TNHVPVITTLLRGGARVDALDR 87
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 9-94 3.73e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.42  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGAD-PCAADDKGRTALH-FASCNGN--DQIVQLLLDHGADPNQRDGLGNTPLH--LAACTNHVPVITTLLRGGARV 82
Cdd:PHA02859   72 LIENGADvNFKTRDNNLSALHhYLSFNKNvePEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSF 151

                          90
                  ....*....|..
gi 1394533390  83 DALDRAGRTPLH 94
Cdd:PHA02859  152 LNKDFDNNNILY 163
PHA02791 PHA02791
ankyrin-like protein; Provisional
 5-102 9.87e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.48  E-value: 9.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   5 WKQQLLED---GADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDglGNTPLHLAACTNHVPVITTLLRGGAR 81
Cdd:PHA02791    9 WKSKQLKSflsSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMD 86

                          90       100
                  ....*....|....*....|.
gi 1394533390  82 VDALDRAGRTPLHLAKSKLNI 102
Cdd:PHA02791   87 DSQFDDKGNTALYYAVDSGNM 107
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-102 1.26e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.43  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARV-DALDR 87
Cdd:PHA02875   21 LLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYK 100

                          90
                  ....*....|....*
gi 1394533390  88 AGRTPLHLAKSKLNI 102
Cdd:PHA02875  101 DGMTPLHLATILKKL 115
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 9-45 1.33e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.73  E-value: 1.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1394533390   9 LLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDH 45
Cdd:PTZ00322  134 LLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 56-84 1.51e-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: 34.87  E-value: 1.51e-03
                           10        20
                   ....*....|....*....|....*....
gi 1394533390   56 GNTPLHLAACTNHVPVITTLLRGGARVDA 84
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-102 1.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.12  E-value: 1.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533390  38 IVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLNI 102
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 30-102 1.79e-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: 38.07  E-value: 1.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533390  30 ASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALD-----RAGRTPLHLAKSKLNI 102
Cdd:cd22192    25 AKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPmtsdlYQGETALHIAVVNQNL 102
PHA02798 PHA02798
ankyrin-like protein; Provisional
 38-116 2.17e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.89  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533390  38 IVQLLLDHGADPNQRDGLGNTPLHLA---ACTNHVPVITTLLRGGARVDALDRAGRTPLHLaksklnILQEGHAQCLEAV 114
Cdd:PHA02798   91 IVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQV------YLQSNHHIDIEII 164


                  ..
gi 1394533390 115 RL 116
Cdd:PHA02798  165 KL 166
PHA02798 PHA02798
ankyrin-like protein; Provisional
 38-104 6.12e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 36.35  E-value: 6.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533390  38 IVQLLLDHGADPNQRDGLGNTPLhlaaCT--------NH-VPVITTLLRGGARVDALDRAGRTPLH--LAKSKLNILQ 104
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPL----CTilsnikdyKHmLDIVKILIENGADINKKNSDGETPLYclLSNGYINNLE 126
 
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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