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Conserved domains on  [gi|530365369|ref|XP_005245540|]
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podocin isoform X1 [Homo sapiens]

Protein Classification

SPFH domain-containing protein( domain architecture ID 139628)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_like super family cl19107
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 92-285 1.78e-118

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.


The actual alignment was detected with superfamily member cd08827:

Pssm-ID: 473137 [Multi-domain]  Cd Length: 223  Bit Score: 340.33  E-value: 1.78e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  92 GLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRS 171
Cdd:cd08827   30 GLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVCLSSFASISDAMQALVQTTVKRLLAHRA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 172 LTEILLERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAE 251
Cdd:cd08827  110 FTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAEAQRQAKVKVIAAEGEKAASEALKAAAE 189

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530365369 252 ILSGTPAAVQLRYLHTLQSLSTEKPSTVVLPLPF 285
Cdd:cd08827  190 SLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLPF 223
 
Name Accession Description Interval E-value
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 92-285 1.78e-118

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: 340.33  E-value: 1.78e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  92 GLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRS 171
Cdd:cd08827   30 GLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVCLSSFASISDAMQALVQTTVKRLLAHRA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 172 LTEILLERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAE 251
Cdd:cd08827  110 FTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAEAQRQAKVKVIAAEGEKAASEALKAAAE 189

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530365369 252 ILSGTPAAVQLRYLHTLQSLSTEKPSTVVLPLPF 285
Cdd:cd08827  190 SLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLPF 223
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 90-231 2.76e-28

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 110.31  E-value: 2.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  90 EEGLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAH 169
Cdd:COG0330   43 EPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGK 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530365369 170 RSLTEILLE-RKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSL--AVEAEAQRQAKV 231
Cdd:COG0330  123 MTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMedRMKAEREREAAI 187
PHB smart00244
prohibitin homologues; prohibitin homologues
 90-228 6.22e-22

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 90.41  E-value: 6.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369    90 EEGLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENAsllLSSLAHVS----KAVQFLVQTTMKR 165
Cdd:smart00244  25 GPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDP---LRAVYRVLdadyAVIEQLAQTTLRS 101

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530365369   166 LLAHRSLTEIL-LERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQhslavEAEAQRQ 228
Cdd:smart00244 102 VIGKRTLDELLtDQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK-----EAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 90-232 1.40e-21

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: 89.69  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369   90 EEGLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRM--ENASLLLSSLAHVSKAVQFL---VQTTMK 164
Cdd:pfam01145  22 EPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLVQNVFGSDDLQELLrrvLESALR 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  165 RLLAHRSLTEILLERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLA--VEAEAQRQAKVR 232
Cdd:pfam01145 102 EIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEakQTAEQEAEAEIA 171
 
Name Accession Description Interval E-value
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 92-285 1.78e-118

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: 340.33  E-value: 1.78e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  92 GLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRS 171
Cdd:cd08827   30 GLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVCLSSFASISDAMQALVQTTVKRLLAHRA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 172 LTEILLERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAE 251
Cdd:cd08827  110 FTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAEAQRQAKVKVIAAEGEKAASEALKAAAE 189

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530365369 252 ILSGTPAAVQLRYLHTLQSLSTEKPSTVVLPLPF 285
Cdd:cd08827  190 SLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLPF 223
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 92-286 6.14e-67

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: 208.56  E-value: 6.14e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  92 GLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRS 171
Cdd:cd03403    8 GLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGTKN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 172 LTEILLERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAE 251
Cdd:cd03403   88 LSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRALKEAAD 167

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530365369 252 ILSGTPAAVQLRYLHTLQSLSTEKPSTVVLPLPFD 286
Cdd:cd03403  168 VISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 92-288 4.39e-65

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: 204.15  E-value: 4.39e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  92 GLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRS 171
Cdd:cd13435    8 GVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGTRN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 172 LTEILLERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAE 251
Cdd:cd13435   88 LSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRALKEASD 167

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530365369 252 ILSGTPAAVQLRYLHTLQSLSTEKPSTVVLPLPFDLL 288
Cdd:cd13435  168 IISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELL 204
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 106-213 1.06e-46

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: 153.50  E-value: 1.06e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 106 VDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRSLTEILLERKSIAQD 185
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....*...
gi 530365369 186 AKVALDSVTCIWGIKVERIEIKDVRLPA 213
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDIILPQ 108
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 98-275 2.12e-42

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: 144.58  E-value: 2.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  98 PCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRSLTEILL 177
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 178 ERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAEILSGTP 257
Cdd:cd08826   81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160

                        170
                 ....*....|....*...
gi 530365369 258 AAVQLRYLHTLQSLSTEK 275
Cdd:cd08826  161 GALQLRYLQTLSEIASEK 178
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 92-234 6.98e-42

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: 142.48  E-value: 6.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  92 GLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRS 171
Cdd:cd08828    4 GLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGTQT 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530365369 172 LTEILLERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMI 234
Cdd:cd08828   84 LAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVV 146
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 92-286 2.52e-41

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: 143.14  E-value: 2.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  92 GLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRS 171
Cdd:cd13437   30 GLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRIDNVKQALIERTQTTLRSVIGERT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 172 LTEILLERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAE 251
Cdd:cd13437  110 LQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIGESKIISAKADVESAKLMREAAD 189

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530365369 252 ILSgTPAAVQLRYLHTLQSLSTEKPSTVVLpLPFD 286
Cdd:cd13437  190 ILD-SKAAMQIRYLETLQAIAKSANSKVIF-LPLD 222
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 90-231 2.76e-28

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 110.31  E-value: 2.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  90 EEGLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAH 169
Cdd:COG0330   43 EPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGK 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530365369 170 RSLTEILLE-RKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSL--AVEAEAQRQAKV 231
Cdd:COG0330  123 MTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMedRMKAEREREAAI 187
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 106-282 2.40e-25

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: 100.01  E-value: 2.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 106 VDLRLQTleIPFH--EIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRSLTEILLERKSIA 183
Cdd:cd13775    1 VDQRIRT--TPFSaeQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 184 QDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAEILSGTPAAVQLR 263
Cdd:cd13775   79 EELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLR 158

                        170
                 ....*....|....*....
gi 530365369 264 YLHTLQSLSTEKPSTVVLP 282
Cdd:cd13775  159 AMNMLYEGLKEKGSMVVVP 177
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 92-211 2.59e-22

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: 90.54  E-value: 2.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  92 GLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRS 171
Cdd:cd13436   10 GIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTSLTNSLSKKT 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530365369 172 LTEILLERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRL 211
Cdd:cd13436   90 VREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 104-213 4.09e-22

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: 89.07  E-value: 4.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 104 HKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRSLTEILLERKSIA 183
Cdd:cd08829    2 YKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEIN 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 530365369 184 QDAKVALDSVTCIWGIKVERIEIKDVRLPA 213
Cdd:cd08829   82 AKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 90-228 6.22e-22

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 90.41  E-value: 6.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369    90 EEGLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENAsllLSSLAHVS----KAVQFLVQTTMKR 165
Cdd:smart00244  25 GPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDP---LRAVYRVLdadyAVIEQLAQTTLRS 101

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530365369   166 LLAHRSLTEIL-LERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQhslavEAEAQRQ 228
Cdd:smart00244 102 VIGKRTLDELLtDQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK-----EAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 90-232 1.40e-21

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: 89.69  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369   90 EEGLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRM--ENASLLLSSLAHVSKAVQFL---VQTTMK 164
Cdd:pfam01145  22 EPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLVQNVFGSDDLQELLrrvLESALR 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  165 RLLAHRSLTEILLERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLA--VEAEAQRQAKVR 232
Cdd:pfam01145 102 EIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEakQTAEQEAEAEIA 171
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 105-284 1.28e-14

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: 71.41  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 105 KVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMKRLLAHRSLTEILLERKSIAQ 184
Cdd:cd13438   37 LVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 185 DAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAEILSGTPAAVQLRY 264
Cdd:cd13438  117 FLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKRAQANLIRAREETAATRSLLNAAKLMEENPALLRLRE 196

                        170       180
                 ....*....|....*....|
gi 530365369 265 LHTLqslstEKPSTVVLPLP 284
Cdd:cd13438  197 LEAL-----EKIAEKVGHIS 211
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 90-230 2.27e-11

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: 62.89  E-value: 2.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  90 EEGLFFFLPCLDTYHKVDLRLQTLEIPFHEIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFL---VQTTMKRL 166
Cdd:cd03405   25 EPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRFYQSVGGEEGAESRLddiVDSALRNE 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530365369 167 LAHRSLTEIL-LERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHSL--AVEAEAQRQAK 230
Cdd:cd03405  105 IGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVyeRMRAERERIAA 171
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 90-233 2.20e-10

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: 59.06  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  90 EEGLFFFLPCLDTYHKVDLRLQTLEIPFhEIVTKDMFIMEIDAICYYRM--ENASLLLSSL--AHVSKAVQFLVQTTMKR 165
Cdd:cd03401   25 GEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRPdpEKLPELYQNLgpDYEERVLPPIVREVLKA 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530365369 166 LLAHRSLTEILLERKSIAQDAKVALDSVTCIWGIKVERIEIKDVRLPAGLQHslAVEA-EAQRQAKVRM 233
Cdd:cd03401  104 VVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEK--AIEAkQVAEQEAERA 170
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 92-234 1.39e-08

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: 54.83  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369  92 GLFFFLPC-LDTYHKVDL-RLQTLEIPFH-----EIVTKDMFIMEIDAICYYRMENASLLLSSLAHVSKAVQFLVQTTMK 164
Cdd:cd03404   39 GLHWKLPFpIEVVEKVNVtQVRSVEIGFRvpeesLMLTGDENIVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALR 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530365369 165 RLLAHRSLTEILLERKS-IAQDAKVA----LDSVTCiwGIKVERIEIKDVRLPAGLQHSLAvEAEAQRQAKVRMI 234
Cdd:cd03404  119 EVVGSRTLDDVLTEGRAeIAADVRELlqeiLDRYDL--GIEIVQVQLQDADPPEEVQDAFD-DVNAARQDKERLI 190
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 109-212 1.50e-05

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: 43.51  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365369 109 RLQTLEIPFHEIVTKDMFIMEIDAICYYRM--ENASLLLSSLAHVSKAVQFLVQT---TMKRLLAHRSLTEILLERKSIA 183
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRItdYNALPAFYLVDFVKDIKADIRRKiadVLRAAIGRMTLDQIISGRDEIA 80

                         90       100
                 ....*....|....*....|....*....
gi 530365369 184 QDAKVALDSVTCIWGIKVERIEIKDVRLP 212
Cdd:cd02106   81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
 
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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