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Conserved domains on  [gi|255522836|ref|NP_081218|]
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stomatin-like protein 1 [Mus musculus]

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 2.60e-74

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: 227.28  E-value: 2.60e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  94 GRIRNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAVKDLNTATRMTAHNA 173
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255522836 174 MTKALLRRPLQEIQMEKLKIGDQLLLEINDVTRAWGLEVDRVELAVEAVLQ 224
Cdd:cd13436   81 LTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKVLK 131
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 312-396 1.37e-17

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: 77.30  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  312 GACYQFNVILPSGTqsiYFLDLTTGQGRVGHGePDGIPDVVVEMAEADLQALLSKELRPLGAYMSGRLKVKGDLAVVMKL 391
Cdd:pfam02036  20 GKVIRFDLTDLGLS---LTLDLKDGGGRVLAG-DEGKADVTLSASDSDLLALATGKLNPQKAFMQGKLKIEGDMELAQKL 95


                  ....*
gi 255522836  392 EAVLK 396
Cdd:pfam02036  96 EGLLK 100
 
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 2.60e-74

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: 227.28  E-value: 2.60e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  94 GRIRNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAVKDLNTATRMTAHNA 173
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255522836 174 MTKALLRRPLQEIQMEKLKIGDQLLLEINDVTRAWGLEVDRVELAVEAVLQ 224
Cdd:cd13436   81 LTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKVLK 131
PHB smart00244
prohibitin homologues; prohibitin homologues
 77-217 3.12e-38

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 135.10  E-value: 3.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836    77 FALKIVPTYERMIVFRLGRIRNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSV 156
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255522836   157 MAVKDLN-TATRMTAHNAMTKALLRRPLQEIQM-EKLKIGDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:smart00244  81 YRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEI 143
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 73-217 5.12e-26

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 105.69  E-value: 5.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  73 ISGWFALKIVPTYERMIVFRLGRIRNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDP 152
Cdd:COG0330   15 VLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDP 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255522836 153 VLSVMAVKDLNTATRMTAHNAMTKALLRRPLQEIQMEK-LKIGDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:COG0330   95 AKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTGrDEINAEIREELQEALDPYGIEVVDVEI 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 80-217 2.49e-18

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: 81.98  E-value: 2.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836   80 KIVPTYERMIVFRLGRIRNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIW--DP---VL 154
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPpklVQ 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255522836  155 SVMAVKDLNTATRMTAHNAMTKALLRRPLQEIQMEKLKIGDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:pfam01145  81 NVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQI 143
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 312-396 1.37e-17

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: 77.30  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  312 GACYQFNVILPSGTqsiYFLDLTTGQGRVGHGePDGIPDVVVEMAEADLQALLSKELRPLGAYMSGRLKVKGDLAVVMKL 391
Cdd:pfam02036  20 GKVIRFDLTDLGLS---LTLDLKDGGGRVLAG-DEGKADVTLSASDSDLLALATGKLNPQKAFMQGKLKIEGDMELAQKL 95


                  ....*
gi 255522836  392 EAVLK 396
Cdd:pfam02036  96 EGLLK 100
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
311-398 1.65e-17

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


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 77.25  E-value: 1.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 311 VGACYQFNVILPSGTQsiYFLDLTTGQGRVGHGEpDGIPDVVVEMAEADLQALLSKELRPLGAYMSGRLKVKGDLAVVMK 390
Cdd:COG3255   20 WDGVVQFVITGEGGGA--YYLVIDDGKCTVSEGD-DDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLAMK 96


                 ....*...
gi 255522836 391 LEAVLKAL 398
Cdd:COG3255   97 LMSLFKAL 104
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 86-228 6.70e-06

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: 47.01  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836   86 ERMIVFRLGRIRNPQGPGMVLLLPFIDSFQRVdlrtrafNVPPCKLASKDGAVLS-------VGADVQFRIWDPVLSVMA 158
Cdd:TIGR01933   8 ERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPV-------NVTAVRNLRKQGLMLTgdenivnVEMNVQYRITDPYKYLFS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255522836  159 VKDLNTATRMTAHNAMTKALLRRPLQEIQME-KLKIGDQLLLEINDVTRAWGLEVDRVELAVEAVLqPPQD 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 2.60e-74

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: 227.28  E-value: 2.60e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  94 GRIRNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAVKDLNTATRMTAHNA 173
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255522836 174 MTKALLRRPLQEIQMEKLKIGDQLLLEINDVTRAWGLEVDRVELAVEAVLQ 224
Cdd:cd13436   81 LTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKVLK 131
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 117-224 6.44e-40

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: 137.71  E-value: 6.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 117 VDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAVKDLNTATRMTAHNAMTKALLRRPLQEIQMEKLKIGDQ 196
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....*...
gi 255522836 197 LLLEINDVTRAWGLEVDRVELAVEAVLQ 224
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDIILPQ 108
PHB smart00244
prohibitin homologues; prohibitin homologues
 77-217 3.12e-38

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 135.10  E-value: 3.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836    77 FALKIVPTYERMIVFRLGRIRNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSV 156
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255522836   157 MAVKDLN-TATRMTAHNAMTKALLRRPLQEIQM-EKLKIGDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:smart00244  81 YRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEI 143
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 100-217 1.15e-26

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: 105.71  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 100 QGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAVKDLNTATRMTAHNAMTKALL 179
Cdd:cd03403    5 KGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLG 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 255522836 180 RRPLQEIQMEKLKIGDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:cd03403   85 TKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEI 122
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 73-217 5.12e-26

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 105.69  E-value: 5.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  73 ISGWFALKIVPTYERMIVFRLGRIRNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDP 152
Cdd:COG0330   15 VLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDP 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255522836 153 VLSVMAVKDLNTATRMTAHNAMTKALLRRPLQEIQMEK-LKIGDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:COG0330   95 AKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTGrDEINAEIREELQEALDPYGIEVVDVEI 160
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 100-217 2.35e-25

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: 102.46  E-value: 2.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 100 QGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAVKDLNTATRMTAHNAMTKALL 179
Cdd:cd13435    5 RGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLG 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 255522836 180 RRPLQEIQMEKLKIGDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:cd13435   85 TRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEI 122
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 76-232 9.92e-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: 101.12  E-value: 9.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  76 WFALKIVPTYERMIVFRLGRI--RNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPV 153
Cdd:cd08827    1 WFCVKVVREYERAVIFRLGHLlqGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 154 LSVMAVKDLNTATRMTAHNAMTKALLRRPLQEIQMEKLKIGDQLLLEINDVTRAWGLEVDRVElaVEAVLQPP--QDSLT 231
Cdd:cd08827   81 VCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAE--IKDVNLPPelQHSFA 158


                 .
gi 255522836 232 V 232
Cdd:cd08827  159 V 159
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 100-217 2.95e-20

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: 86.62  E-value: 2.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 100 QGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAVKDLNTATRMTAHNAMTKALL 179
Cdd:cd08828    1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 255522836 180 RRPLQEIQMEKLKIGDQLLLEINDVTRAWGLEVDRVEL 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 2.49e-18

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: 81.98  E-value: 2.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836   80 KIVPTYERMIVFRLGRIRNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIW--DP---VL 154
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPpklVQ 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255522836  155 SVMAVKDLNTATRMTAHNAMTKALLRRPLQEIQMEKLKIGDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:pfam01145  81 NVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQI 143
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 109-217 8.71e-18

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: 80.25  E-value: 8.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 109 PFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAVKDLNTATRMTAHNAMTKALLRRPLQEIQM 188
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                         90       100
                 ....*....|....*....|....*....
gi 255522836 189 EKLKIGDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:cd08826   81 EREEINKRIQEIIDEQTEPWGIKVTAVEI 109
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 312-396 1.37e-17

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: 77.30  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  312 GACYQFNVILPSGTqsiYFLDLTTGQGRVGHGePDGIPDVVVEMAEADLQALLSKELRPLGAYMSGRLKVKGDLAVVMKL 391
Cdd:pfam02036  20 GKVIRFDLTDLGLS---LTLDLKDGGGRVLAG-DEGKADVTLSASDSDLLALATGKLNPQKAFMQGKLKIEGDMELAQKL 95


                  ....*
gi 255522836  392 EAVLK 396
Cdd:pfam02036  96 EGLLK 100
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
311-398 1.65e-17

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


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 77.25  E-value: 1.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 311 VGACYQFNVILPSGTQsiYFLDLTTGQGRVGHGEpDGIPDVVVEMAEADLQALLSKELRPLGAYMSGRLKVKGDLAVVMK 390
Cdd:COG3255   20 WDGVVQFVITGEGGGA--YYLVIDDGKCTVSEGD-DDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLAMK 96


                 ....*...
gi 255522836 391 LEAVLKAL 398
Cdd:COG3255   97 LMSLFKAL 104
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 116-217 1.53e-14

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: 69.43  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 116 RVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAVKDLNTATRMTAHNAMTKALLRRPLQEIQMEKLKIGD 195
Cdd:cd08829    3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                         90       100
                 ....*....|....*....|..
gi 255522836 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 6.73e-13

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: 67.90  E-value: 6.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  81 IVPTYERMIVFRLGRI-RNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAV 159
Cdd:cd03405    4 IVDETEQAVVLQFGKPvRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRFYQSV 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255522836 160 KDLNTA-TRMTA--HNAMTKALLRRPLQE-IQMEKLKIGDQLLLEINDVTRAWGLEVD-----RVELaVEAVLQ 224
Cdd:cd03405   84 GGEEGAeSRLDDivDSALRNEIGKRTLAEvVSGGRDELMEEILEQANEEAKEYGIEVVdvrikRIDL-PEEVSE 156
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 89-215 1.66e-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: 63.40  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  89 IVFRLGRIRNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAVKDLNTATRm 168
Cdd:cd13437   16 LVERFGKFYKTVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRIDNVKQALI- 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 255522836 169 tahnAMTKALLR-----RPLQEIQMEKLKIGDQLLLEINDVTRAWGLEVDRV 215
Cdd:cd13437   95 ----ERTQTTLRsvigeRTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESI 142
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 73-228 4.34e-10

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: 59.83  E-value: 4.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  73 ISGWFalkIVPTYERMIVFRLGRIRNPQGPGMVLLLPF-IDSFQRVDL-RTRAFNVPPCKLAS-----KDGAVLSVGADV 145
Cdd:cd03404   12 LSGFY---TVDPGERGVVLRFGKYVRTVGPGLHWKLPFpIEVVEKVNVtQVRSVEIGFRVPEEslmltGDENIVDVDFVV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 146 QFRIWDPVLSVMAVKDLNTATRMTAHNAMTKALLRRPLQEI-QMEKLKIGDQLLLEINDVTRAW--GLEVDRVELavEAV 222
Cdd:cd03404   89 QYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVlTEGRAEIAADVRELLQEILDRYdlGIEIVQVQL--QDA 166


                 ....*.
gi 255522836 223 lQPPQD 228
Cdd:cd03404  167 -DPPEE 171
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 82-217 1.50e-08

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: 54.46  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  82 VPTYERMIVFRLGRIRNPQGPGMVLLLPFIDSFQ--RVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAV 159
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTLEPGRYAFWKFGRKVQveLVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255522836 160 KDLNTATRMTAHNAMTKALLRRPLQEIQMEKLKIGDQLLLEINDVTRAWGLEVDRVEL 217
Cdd:cd13438   81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGV 138
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 79-149 2.87e-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: 2.87e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255522836  79 LKIVPTYERMIVFRLGRI--RNPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPcKLASKDGAVLSVGADVQFRI 149
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGvkDEVLGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRP 72
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 117-230 8.68e-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: 48.78  E-value: 8.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 117 VDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMAVKDLNTATRMTAHNAMTKALLRRPLQEIQMEKLKIGDQ 196
Cdd:cd13775    1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 255522836 197 LLLEINDVTRAWGLEVDRVElaVEAVLQPP--QDSL 230
Cdd:cd13775   81 LQDIIDEKTTPWGITVQSVE--IRDIIIPKelQDAM 114
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 86-228 6.70e-06

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: 47.01  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836   86 ERMIVFRLGRIRNPQGPGMVLLLPFIDSFQRVdlrtrafNVPPCKLASKDGAVLS-------VGADVQFRIWDPVLSVMA 158
Cdd:TIGR01933   8 ERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPV-------NVTAVRNLRKQGLMLTgdenivnVEMNVQYRITDPYKYLFS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255522836  159 VKDLNTATRMTAHNAMTKALLRRPLQEIQME-KLKIGDQLLLEINDVTRAWGLEVDRVELAVEAVLqPPQD 228
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYDLGITVTDVNFQSAR-PPEE 150
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 120-216 4.40e-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: 39.65  E-value: 4.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836 120 RTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLS-----VMAVKDLNTATRMTAHNAMTKALLRRPLQEIQMEKLKIG 194
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                         90       100
                 ....*....|....*....|..
gi 255522836 195 DQLLLEINDVTRAWGLEVDRVE 216
Cdd:cd02106   81 KAVKEDLEEDLENFGVVISDVD 102
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 343-397 4.05e-03

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 39.44  E-value: 4.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255522836 343 GEPDGIPDVVVEMAEADLQALLSKELRPLGAYMSGRLKVKGDLAVVMKLEAVLKA 397
Cdd:COG2015  567 GPQADDADATLTLTRADLLALLLGKTTLDDLVASGGAKVEGDAAALARLLGLLDP 621
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 71-164 8.56e-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: 259800  Cd Length: 231  Bit Score: 37.53  E-value: 8.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522836  71 FPISGWFalkIVPTYERMIVFRLGR----IRNPqgpGMVLLLPFIdSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQ 146
Cdd:cd03402    5 ILLGGFF---VVQPNEAAVLTLFGRyrgtVRRP---GLRWVNPFY-RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVV 77

                         90
                 ....*....|....*...
gi 255522836 147 FRIWDPVLSVMAVKDLNT 164
Cdd:cd03402   78 WRVVDTAKAVFDVDDYEE 95
 
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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