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Conserved domains on  [gi|662033920|ref|NP_001284504|]
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podocin isoform 2 [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 ...
 122-276 4.17e-85

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: 255.20  E-value: 4.17e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 122 WFCVKVVQEYERVIIFRLGHLLPGRAKGPGLFFFLPCLDTYHKVDLRLQTLEIPFHE----------------------- 178
Cdd:cd08827    1 WFCVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMivtkdlvcteidaicyyrienas 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 179 ---------------------------------------------VALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVE 213
Cdd:cd08827   81 vclssfasisdamqalvqttvkrllahraftdillerksiaqeikVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 662033920 214 AEAQRQAKVRMIAAEAEKAASESLRMAAEILSGTPAAVQLRYLHTLQSLSTEKPSTVVLPLPF 276
Cdd:cd08827  161 AEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLPF 223
 
Name Accession Description Interval E-value
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 122-276 4.17e-85

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: 255.20  E-value: 4.17e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 122 WFCVKVVQEYERVIIFRLGHLLPGRAKGPGLFFFLPCLDTYHKVDLRLQTLEIPFHE----------------------- 178
Cdd:cd08827    1 WFCVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMivtkdlvcteidaicyyrienas 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 179 ---------------------------------------------VALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVE 213
Cdd:cd08827   81 vclssfasisdamqalvqttvkrllahraftdillerksiaqeikVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 662033920 214 AEAQRQAKVRMIAAEAEKAASESLRMAAEILSGTPAAVQLRYLHTLQSLSTEKPSTVVLPLPF 276
Cdd:cd08827  161 AEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLPF 223
PHB smart00244
prohibitin homologues; prohibitin homologues
 123-219 1.00e-12

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 64.99  E-value: 1.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920   123 FCVKVVQEYERVIIFRLGHLLpgRAKGPGLFFFLPCLDTYHKVDLRLQTLEIP-------------------FHEV---- 179
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPpqetitkdnvkvsvdavvyYRVLdplr 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920   180 -----------------------------------------------ALDSVTCIWGIKVERIEIKDVRLPAGLQhslav 212
Cdd:smart00244  79 avyrvldadyavieqlaqttlrsvigkrtldelltdqrekisenireELNEAAEAWGIKVEDVEIKDIRLPEEIK----- 153


                   ....*..
gi 662033920   213 EAEAQRQ 219
Cdd:smart00244 154 EAMEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 104-222 2.50e-12

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 66.02  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 104 LLVLISLLFIIMTfpfsIWFCVKVVQEYERVIIFRLGHLLpgRAKGPGLFFFLPCLDTYHKVDLRLQTLEIPFHEV---- 179
Cdd:COG0330    4 ILLLILLVLVLVL----LFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVltkd 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 180 -----------------------------------------------------------------ALDSVTCIWGIKVER 194
Cdd:COG0330   78 nnivdvdavvqyritdpakflynvenaeealrqlaesalrevigkmtldevlstgrdeinaeireELQEALDPYGIEVVD 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 662033920 195 IEIKDVRLPAGLQHSL--AVEAEAQRQAKV 222
Cdd:COG0330  158 VEIKDIDPPEEVQDAMedRMKAEREREAAI 187
PRK11029 PRK11029
protease modulator HflC;
109-174 8.30e-06

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 46.66  E-value: 8.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 662033920 109 SLLFIIMTFPFSIWFCVKVVQEYERVIIFRLGHLLPGRAK-----GPGLFFFLPCLDTYHKVDLRLQTLEI 174
Cdd:PRK11029   4 SVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDN 74
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 126-179 2.92e-05

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: 43.85  E-value: 2.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 662033920  126 KVVQEYERVIIFRLGhlLPGRAKGPGLFFFLPCLDTYHKVDLRLQTLEIPFHEV 179
Cdd:pfam01145   1 IIVPPGEVGVVTRFG--KLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTV 52
 
Name Accession Description Interval E-value
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 122-276 4.17e-85

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: 255.20  E-value: 4.17e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 122 WFCVKVVQEYERVIIFRLGHLLPGRAKGPGLFFFLPCLDTYHKVDLRLQTLEIPFHE----------------------- 178
Cdd:cd08827    1 WFCVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMivtkdlvcteidaicyyrienas 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 179 ---------------------------------------------VALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVE 213
Cdd:cd08827   81 vclssfasisdamqalvqttvkrllahraftdillerksiaqeikVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 662033920 214 AEAQRQAKVRMIAAEAEKAASESLRMAAEILSGTPAAVQLRYLHTLQSLSTEKPSTVVLPLPF 276
Cdd:cd08827  161 AEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLPF 223
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 144-277 3.10e-42

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: 144.62  E-value: 3.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 144 PGRAKGPGLFFFLPCLDTYHKVDLRLQTLEIPFHEV-------------------------------------------- 179
Cdd:cd03403    1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEIltkdsvtvavdavvyyrvqnatiavtnvenadrstrllaqttlr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 180 ------------------------ALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASE 235
Cdd:cd03403   81 nvlgtknlseilsdretishqmqsTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 662033920 236 SLRMAAEILSGTPAAVQLRYLHTLQSLSTEKPSTVVLPLPFD 277
Cdd:cd03403  161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 145-279 1.46e-41

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: 143.29  E-value: 1.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 145 GRAKGPGLFFFLPCLDTYHKVDLRLQTLEIPFHEV--------------------------------------------- 179
Cdd:cd13435    2 GGARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVltkdsvtvtvdavvyyrisdplnaviqvanyshstrllaattlrn 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 180 -----------------------ALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASES 236
Cdd:cd13435   82 vlgtrnlsellteretishsmqvTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 662033920 237 LRMAAEILSGTPAAVQLRYLHTLQSLSTEKPSTVVLPLPFDLL 279
Cdd:cd13435  162 LKEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELL 204
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 181-266 2.62e-22

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: 91.81  E-value: 2.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 181 LDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAEILSGTPAAVQLRYLHTLQ 260
Cdd:cd08826   93 IDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSPGALQLRYLQTLS 172


                 ....*.
gi 662033920 261 SLSTEK 266
Cdd:cd08826  173 EIASEK 178
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 146-277 1.68e-19

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: 85.36  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 146 RAKGPGLFFFLPCLDTYHKVDLRLQTLEIPFHE--------VALDSV---------------------------TCI--- 187
Cdd:cd13437   25 KTVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSvmtkdnvsVTIDSVvyyriidpykaiyridnvkqaliertqTTLrsv 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 188 ------------------------------WGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESL 237
Cdd:cd13437  105 igertlqdllekreeiadeieeiveevakeWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIGESKIISAKADVESAKLM 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 662033920 238 RMAAEILSgTPAAVQLRYLHTLQSLSTEKPSTVVLpLPFD 277
Cdd:cd13437  185 REAADILD-SKAAMQIRYLETLQAIAKSANSKVIF-LPLD 222
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 148-225 4.36e-17

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: 76.99  E-value: 4.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 148 KGPGLFFFLPCLDTYHKVDLRLQTLEIPFHEV------------------------------------------------ 179
Cdd:cd08828    1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEIltkdsvttqvdgvvyyriqsavkavanvnnvhiatfllaqttlrnvlg 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 662033920 180 --------------------ALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMI 225
Cdd:cd08828   81 tqtlaqilagreeiahsiqsILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVV 146
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 178-273 3.43e-13

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: 66.50  E-value: 3.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 178 EVALDSVTCIWGIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAEILSGTPAAVQLRYLH 257
Cdd:cd13775   82 QDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAMN 161

                         90
                 ....*....|....*.
gi 662033920 258 TLQSLSTEKPSTVVLP 273
Cdd:cd13775  162 MLYEGLKEKGSMVVVP 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 123-219 1.00e-12

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 64.99  E-value: 1.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920   123 FCVKVVQEYERVIIFRLGHLLpgRAKGPGLFFFLPCLDTYHKVDLRLQTLEIP-------------------FHEV---- 179
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPpqetitkdnvkvsvdavvyYRVLdplr 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920   180 -----------------------------------------------ALDSVTCIWGIKVERIEIKDVRLPAGLQhslav 212
Cdd:smart00244  79 avyrvldadyavieqlaqttlrsvigkrtldelltdqrekisenireELNEAAEAWGIKVEDVEIKDIRLPEEIK----- 153


                   ....*..
gi 662033920   213 EAEAQRQ 219
Cdd:smart00244 154 EAMEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 104-222 2.50e-12

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 66.02  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 104 LLVLISLLFIIMTfpfsIWFCVKVVQEYERVIIFRLGHLLpgRAKGPGLFFFLPCLDTYHKVDLRLQTLEIPFHEV---- 179
Cdd:COG0330    4 ILLLILLVLVLVL----LFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVltkd 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 180 -----------------------------------------------------------------ALDSVTCIWGIKVER 194
Cdd:COG0330   78 nnivdvdavvqyritdpakflynvenaeealrqlaesalrevigkmtldevlstgrdeinaeireELQEALDPYGIEVVD 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 662033920 195 IEIKDVRLPAGLQHSL--AVEAEAQRQAKV 222
Cdd:COG0330  158 VEIKDIDPPEEVQDAMedRMKAEREREAAI 187
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 178-204 1.00e-08

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: 52.19  E-value: 1.00e-08
                         10        20
                 ....*....|....*....|....*..
gi 662033920 178 EVALDSVTCIWGIKVERIEIKDVRLPA 204
Cdd:cd13434   82 QEILDEATDPWGIKVERVEIKDIILPQ 108
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 124-179 2.19e-06

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: 47.87  E-value: 2.19e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 662033920 124 CVKVVQEYERVIIFRLGHLLpGRAKGPGLFFFLPCLDTYHKVDLRLQTLEIPFHEV 179
Cdd:cd03405    1 SVFIVDETEQAVVLQFGKPV-RVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEV 55
PRK11029 PRK11029
protease modulator HflC;
109-174 8.30e-06

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 46.66  E-value: 8.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 662033920 109 SLLFIIMTFPFSIWFCVKVVQEYERVIIFRLGHLLPGRAK-----GPGLFFFLPCLDTYHKVDLRLQTLEI 174
Cdd:PRK11029   4 SVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDN 74
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 126-179 2.92e-05

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: 43.85  E-value: 2.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 662033920  126 KVVQEYERVIIFRLGhlLPGRAKGPGLFFFLPCLDTYHKVDLRLQTLEIPFHEV 179
Cdd:pfam01145   1 IIVPPGEVGVVTRFG--KLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTV 52
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 145-175 7.49e-05

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: 42.00  E-value: 7.49e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 662033920 145 GRA---KGPGLFFFLPCLDTYHKVDLRLQTLEIP 175
Cdd:cd13436    1 GRLqkpRGPGIVLILPCIDNFTRVDMRTRAFNVP 34
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 125-176 1.05e-04

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: 42.50  E-value: 1.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 662033920 125 VKVVQEYERVIIFRLGHLLPGRAKGPGLFFFLPCLDTYHKVDLRLQTLEIPF 176
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITL 52
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 180-204 1.96e-04

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: 40.15  E-value: 1.96e-04
                         10        20
                 ....*....|....*....|....*
gi 662033920 180 ALDSVTCIWGIKVERIEIKDVRLPA 204
Cdd:cd08829   87 ALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 189-275 5.34e-03

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: 37.51  E-value: 5.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662033920 189 GIKVERIEIKDVRLPAGLQHSLAVEAEAQRQAKVRMIAAEAEKAASESLRMAAEILSGTPAAVQLRYLHTLqslstEKPS 268
Cdd:cd13438  130 GVEVLSVGVKDIILPGEIREILNQVLEAEKRAQANLIRAREETAATRSLLNAAKLMEENPALLRLRELEAL-----EKIA 204


                 ....*..
gi 662033920 269 TVVLPLP 275
Cdd:cd13438  205 EKVGHIS 211
 
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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