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Conserved domains on  [gi|375493507|ref|NP_001243604|]
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stomatin-like protein 1 isoform 5 [Homo sapiens]

Protein Classification

SPFH_SLP-1 and SCP2 domain-containing protein( domain architecture ID 10194182)

SPFH_SLP-1 and SCP2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 94-224 3.42e-76

Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in animals. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


:

Pssm-ID: 259814 [Multi-domain]  Cd Length: 131  Bit Score: 229.59  E-value: 3.42e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  94 GRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNA 173
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 375493507 174 MTKALLKRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVELAVEAVLQ 224
Cdd:cd13436   81 LTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKVLK 131
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
264-326 3.39e-13

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


:

Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 64.93  E-value: 3.39e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493507 264 GRGRVGHGvPDGIPDVVVEMAEADLRALLCRELRPLGAYMSGRLKVKGDLAMAMKLEAVLRAL 326
Cdd:COG3255   43 GKCTVSEG-DDDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLAMKLMSLFKAL 104
 
Name Accession Description Interval E-value
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 94-224 3.42e-76

Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in animals. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259814 [Multi-domain]  Cd Length: 131  Bit Score: 229.59  E-value: 3.42e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  94 GRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNA 173
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 375493507 174 MTKALLKRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVELAVEAVLQ 224
Cdd:cd13436   81 LTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKVLK 131
PHB smart00244
prohibitin homologues; prohibitin homologues
 77-217 1.07e-40

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 139.72  E-value: 1.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507    77 FALKIVPTYERMIVFRLGRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSV 156
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493507   157 MTVKDLN-TATRMTAQNAMTKALLKRPLREIQM-EKLKISDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:smart00244  81 YRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEI 143
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 57-217 5.25e-30

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 115.32  E-value: 5.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  57 GLISFLGFLLLLVTFPISGWFalkIVPTYERMIVFRLGRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDG 136
Cdd:COG0330    2 KLILLLILLVLVLVLLFSSVY---IVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507 137 AVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEK-LKISDQLLLEINDVTRAWGLEVDRV 215
Cdd:COG0330   79 NIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTGrDEINAEIREELQEALDPYGIEVVDV 158


                 ..
gi 375493507 216 EL 217
Cdd:COG0330  159 EI 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 80-217 1.48e-19

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 84.30  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507   80 KIVPTYERMIVFRLGRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIW--DP---VL 154
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPpklVQ 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493507  155 SVMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:pfam01145  81 NVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQI 143
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
264-326 3.39e-13

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 64.93  E-value: 3.39e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493507 264 GRGRVGHGvPDGIPDVVVEMAEADLRALLCRELRPLGAYMSGRLKVKGDLAMAMKLEAVLRAL 326
Cdd:COG3255   43 GKCTVSEG-DDDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLAMKLMSLFKAL 104
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 264-324 4.83e-12

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 61.50  E-value: 4.83e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375493507  264 GRGRVGHGvPDGIPDVVVEMAEADLRALLCRELRPLGAYMSGRLKVKGDLAMAMKLEAVLR 324
Cdd:pfam02036  41 GGGRVLAG-DEGKADVTLSASDSDLLALATGKLNPQKAFMQGKLKIEGDMELAQKLEGLLK 100
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 86-228 7.37e-07

HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 49.71  E-value: 7.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507   86 ERMIVFRLGRIRTPQGPGMVLLLPFIDSFQRVdlrtrafNVPPCKLASKDGAVLS-------VGADVQFRIWDPVLSVMT 158
Cdd:TIGR01933   8 ERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPV-------NVTAVRNLRKQGLMLTgdenivnVEMNVQYRITDPYKYLFS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375493507  159 VKDLNTATRMTAQNAMTKALLKRPLREIQME-KLKISDQLLLEINDVTRAWGLEVDRVELAVEAVLqPPQD 228
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYDLGITVTDVNFQSAR-PPEE 150
 
Name Accession Description Interval E-value
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 94-224 3.42e-76

Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in animals. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259814 [Multi-domain]  Cd Length: 131  Bit Score: 229.59  E-value: 3.42e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  94 GRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNA 173
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 375493507 174 MTKALLKRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVELAVEAVLQ 224
Cdd:cd13436   81 LTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKVLK 131
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 117-224 6.43e-44

Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, podocin, and other members of the stomatin-like protein family (SLPs or slipins). The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome. Bacterial and archaebacterial SLPs and many of the eukaryotic family members remain uncharacterized.


Pssm-ID: 259812 [Multi-domain]  Cd Length: 108  Bit Score: 146.18  E-value: 6.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507 117 VDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEKLKISDQ 196
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....*...
gi 375493507 197 LLLEINDVTRAWGLEVDRVELAVEAVLQ 224
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDIILPQ 108
PHB smart00244
prohibitin homologues; prohibitin homologues
 77-217 1.07e-40

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 139.72  E-value: 1.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507    77 FALKIVPTYERMIVFRLGRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSV 156
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493507   157 MTVKDLN-TATRMTAQNAMTKALLKRPLREIQM-EKLKISDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:smart00244  81 YRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEI 143
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 57-217 5.25e-30

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 115.32  E-value: 5.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  57 GLISFLGFLLLLVTFPISGWFalkIVPTYERMIVFRLGRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDG 136
Cdd:COG0330    2 KLILLLILLVLVLVLLFSSVY---IVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507 137 AVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEK-LKISDQLLLEINDVTRAWGLEVDRV 215
Cdd:COG0330   79 NIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTGrDEINAEIREELQEALDPYGIEVVDV 158


                 ..
gi 375493507 216 EL 217
Cdd:COG0330  159 EI 160
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 100-217 1.21e-29

Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch.


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 112.26  E-value: 1.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507 100 QGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALL 179
Cdd:cd03403    5 KGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLG 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 375493507 180 KRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:cd03403   85 TKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEI 122
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 100-217 1.33e-26

Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in arthropods. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this divergent slipin subgroup remain largely uncharacterized. It contains Drosophila Mec2, the gene for which was identified in a screen for genes required for nephrocyte function; it may function together with Sns in maintaining nephrocyte diaphragm.


Pssm-ID: 259813 [Multi-domain]  Cd Length: 208  Bit Score: 104.39  E-value: 1.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507 100 QGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALL 179
Cdd:cd13435    5 RGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLG 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 375493507 180 KRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:cd13435   85 TRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEI 122
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 76-227 1.67e-25

Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Podocin is expressed in the kidney and mutations in the gene have been linked to familial idiopathic nephrotic syndrome. Podocin interacts with the TRP ion channel TRPV-6 and may function as a scaffolding protein in the organization of lipid-protein domains.


Pssm-ID: 259809 [Multi-domain]  Cd Length: 223  Bit Score: 101.89  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  76 WFALKIVPTYERMIVFRLGRI--RTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPV 153
Cdd:cd08827    1 WFCVKVVREYERAVIFRLGHLlqGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375493507 154 LSVMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVElaVEAVLQPPQ 227
Cdd:cd08827   81 VCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAE--IKDVNLPPE 152
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 100-217 7.44e-22

Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this slipin subgroup remain uncharacterized, except for Caenorhabditis elegans UNC-1. Mutations in the unc-1 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259810 [Multi-domain]  Cd Length: 154  Bit Score: 90.09  E-value: 7.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507 100 QGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALL 179
Cdd:cd08828    1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 375493507 180 KRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:cd08828   81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEI 118
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 80-217 1.48e-19

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 84.30  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507   80 KIVPTYERMIVFRLGRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIW--DP---VL 154
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPpklVQ 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493507  155 SVMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:pfam01145  81 NVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQI 143
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 109-217 5.58e-19

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized. This subgroup contains PH1511 from the hyperthermophilic archaeon Pyrococcus horikoshi.


Pssm-ID: 259808 [Multi-domain]  Cd Length: 178  Bit Score: 82.95  E-value: 5.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507 109 PFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALLKRPLREIQM 188
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                         90       100
                 ....*....|....*....|....*....
gi 375493507 189 EKLKISDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:cd08826   81 EREEINKRIQEIIDEQTEPWGIKVTAVEI 109
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 116-217 2.17e-16

Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in all three kingdoms of life. The conserved domain common to these families has also been referred to as the Band 7 domain. Individual proteins of the SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This subgroup of the SLPs remains largely uncharacterized. It includes human SLP-2 which is upregulated and involved in the progression and development in several types of cancer, including esophageal squamous cell carcinoma, endometrial adenocarcinoma, breast cancer, and glioma.


Pssm-ID: 259811 [Multi-domain]  Cd Length: 111  Bit Score: 73.66  E-value: 2.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507 116 RVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEKLKISD 195
Cdd:cd08829    3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                         90       100
                 ....*....|....*....|..
gi 375493507 196 QLLLEINDVTRAWGLEVDRVEL 217
Cdd:cd08829   83 KLLEALDEATDPWGVKVTRVEI 104
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 81-224 5.46e-14

High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259803 [Multi-domain]  Cd Length: 249  Bit Score: 70.59  E-value: 5.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  81 IVPTYERMIVFRLGRI-RTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTV 159
Cdd:cd03405    4 IVDETEQAVVLQFGKPvRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRFYQSV 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375493507 160 KDLNTA-TRMTAQ--NAMTKALLKRPLRE-IQMEKLKISDQLLLEINDVTRAWGLEVD-----RVELaVEAVLQ 224
Cdd:cd03405   84 GGEEGAeSRLDDIvdSALRNEIGKRTLAEvVSGGRDELMEEILEQANEEAKEYGIEVVdvrikRIDL-PEEVSE 156
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
264-326 3.39e-13

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 64.93  E-value: 3.39e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493507 264 GRGRVGHGvPDGIPDVVVEMAEADLRALLCRELRPLGAYMSGRLKVKGDLAMAMKLEAVLRAL 326
Cdd:COG3255   43 GKCTVSEG-DDDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLAMKLMSLFKAL 104
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 264-324 4.83e-12

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 61.50  E-value: 4.83e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375493507  264 GRGRVGHGvPDGIPDVVVEMAEADLRALLCRELRPLGAYMSGRLKVKGDLAMAMKLEAVLR 324
Cdd:pfam02036  41 GGGRVLAG-DEGKADVTLSASDSDLLALATGKLNPQKAFMQGKLKIEGDMELAQKLEGLLK 100
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 62-228 2.11e-11

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 63.30  E-value: 2.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  62 LGFLLLLVTFPISGWFalkIVPTYERMIVFRLGRIRTPQGPGMVLLLPF-IDSFQRVDL-RTRAFNVPPCKLAS-----K 134
Cdd:cd03404    1 LILLLLLLVWLLSGFY---TVDPGERGVVLRFGKYVRTVGPGLHWKLPFpIEVVEKVNVtQVRSVEIGFRVPEEslmltG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507 135 DGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALLKRPLREI-QMEKLKISDQLLLEINDVTRAW--GLE 211
Cdd:cd03404   78 DENIVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVlTEGRAEIAADVRELLQEILDRYdlGIE 157

                        170
                 ....*....|....*..
gi 375493507 212 VDRVELavEAVlQPPQD 228
Cdd:cd03404  158 IVQVQL--QDA-DPPEE 171
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 89-215 2.19e-11

Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in some eukaryotes and viruses. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This diverse subgroup of the SLPs remains largely uncharacterized.


Pssm-ID: 259815 [Multi-domain]  Cd Length: 222  Bit Score: 62.63  E-value: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  89 IVFRLGRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRM 168
Cdd:cd13437   16 LVERFGKFYKTVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRIDNVKQALIE 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 375493507 169 TAQNAMTKALLKRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRV 215
Cdd:cd13437   96 RTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESI 142
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 82-217 4.23e-10

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial SLPs remain uncharacterized.


Pssm-ID: 259816 [Multi-domain]  Cd Length: 215  Bit Score: 58.70  E-value: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  82 VPTYERMIVFRLGRIRTPQGPGMVLLLPFIDSFQ--RVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTV 159
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTLEPGRYAFWKFGRKVQveLVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 375493507 160 KDLNTATRMTAQNAMTKALLKRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:cd13438   81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGV 138
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 79-149 1.97e-07

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 50.59  E-value: 1.97e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493507  79 LKIVPTYERMIVFRLGRIRTPQ--GPGMVLLLPFIDSFQRVDLRTRAFNVPPcKLASKDGAVLSVGADVQFRI 149
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEvlGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRP 72
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 117-216 4.39e-07

Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of the SPFH family (stomatin, prohibitin, flotillin, and HflK/C); This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized.


Pssm-ID: 259817 [Multi-domain]  Cd Length: 177  Bit Score: 49.16  E-value: 4.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507 117 VDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEKLKISDQ 196
Cdd:cd13775    1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                         90       100
                 ....*....|....*....|
gi 375493507 197 LLLEINDVTRAWGLEVDRVE 216
Cdd:cd13775   81 LQDIIDEKTTPWGITVQSVE 100
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 86-228 7.37e-07

HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 49.71  E-value: 7.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507   86 ERMIVFRLGRIRTPQGPGMVLLLPFIDSFQRVdlrtrafNVPPCKLASKDGAVLS-------VGADVQFRIWDPVLSVMT 158
Cdd:TIGR01933   8 ERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPV-------NVTAVRNLRKQGLMLTgdenivnVEMNVQYRITDPYKYLFS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375493507  159 VKDLNTATRMTAQNAMTKALLKRPLREIQME-KLKISDQLLLEINDVTRAWGLEVDRVELAVEAVLqPPQD 228
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYDLGITVTDVNFQSAR-PPEE 150
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 71-217 5.00e-04

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259800  Cd Length: 231  Bit Score: 41.00  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  71 FPISGWFalkIVPTYERMIVFRLGR-IRTPQGPGMVLLLPFIdSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRI 149
Cdd:cd03402    5 ILLGGFF---VVQPNEAAVLTLFGRyRGTVRRPGLRWVNPFY-RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWRV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375493507 150 WDPVLSVMTVKDLNTATRMTAQNAMTKALLKRP----------LREiqmEKLKISDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:cd03402   81 VDTAKAVFDVDDYEEFVSIQSEAALRRVASRYPydsfedgepsLRG---NSDEVSEELRRELQERLAVAGVEVIEARI 155
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 120-216 6.23e-04

core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259797 [Multi-domain]  Cd Length: 110  Bit Score: 38.88  E-value: 6.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507 120 RTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLS-----VMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEKLKIS 194
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                         90       100
                 ....*....|....*....|..
gi 375493507 195 DQLLLEINDVTRAWGLEVDRVE 216
Cdd:cd02106   81 KAVKEDLEEDLENFGVVISDVD 102
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 81-149 6.99e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 37.56  E-value: 6.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493507  81 IVPTYERMIVFRLGRIRTPQGPGMVLLLPFIDS-FQRVDLRTRAFNVpPCKLASKDGAVLSVGADVQFRI 149
Cdd:cd03407    1 CVSQSTVAIVERFGKFSRIAEPGLHFIIPPIESvAGRVSLRVQQLDV-RVETKTKDNVFVTLVVSVQYRV 69
 
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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