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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  74 PGGARGPGLFFVVPCIDSYKKIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNATISVINIEDAARSTKLLAQTTLR 153
Cdd:cd03403   1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459 154 NILGTKTLTEMLSDRDVISLQMQATLDETTIPWGVKVERVEMKDVRLPYQLQRVMAAEAEATRDAMAKIIAAEGEKNAST 233
Cdd:cd03403  81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17570459 234 ALAEAADVISMSPCAIQLRYLQTLNSISSEKNNTIVFPFPME 275
Cdd:cd03403 161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  74 PGGARGPGLFFVVPCIDSYKKIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNATISVINIEDAARSTKLLAQTTLR 153
Cdd:cd03403   1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459 154 NILGTKTLTEMLSDRDVISLQMQATLDETTIPWGVKVERVEMKDVRLPYQLQRVMAAEAEATRDAMAKIIAAEGEKNAST 233
Cdd:cd03403  81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17570459 234 ALAEAADVISMSPCAIQLRYLQTLNSISSEKNNTIVFPFPME 275
Cdd:cd03403 161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202

prohibitin homologues; prohibitin homologues

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459     54 CVKVAQEYERAVIFRLGRVKpgGARGPGLFFVVPCIDSYKKIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNATIS 133
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459    134 VINIEDAA-RSTKLLAQTTLRNILGTKTLTEMLSD-RDVISLQMQATLDETTIPWGVKVERVEMKDVRLPYQLQRVMAAE 211
Cdd:smart00244  80 VYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159

                   .
gi 17570459    212 A 212
Cdd:smart00244 160 Q 160

protease modulator HflC;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17570459   37 IFSYILAVLTLPISVFlcvkVAQEYERAVIFRLGRV------KPGgARGPGLFFVVPCIDSYKKIDLR 98
Cdd:PRK11029   6 IAIIIIVLVVLYMSVF----VVKEGERGIVLRFGKVlrdddnKPL-VYAPGLHFKIPFIETVKMLDAR 68

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  74 PGGARGPGLFFVVPCIDSYKKIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNATISVINIEDAARSTKLLAQTTLR 153
Cdd:cd03403   1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459 154 NILGTKTLTEMLSDRDVISLQMQATLDETTIPWGVKVERVEMKDVRLPYQLQRVMAAEAEATRDAMAKIIAAEGEKNAST 233
Cdd:cd03403  81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17570459 234 ALAEAADVISMSPCAIQLRYLQTLNSISSEKNNTIVFPFPME 275
Cdd:cd03403 161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  52 FLCVKVAQEYERAVIFRLGRVKPGGARGPGLFFVVPCIDSYKKIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNAT 131
Cdd:cd08827   1 WFCVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459 132 ISVINIEDAARSTKLLAQTTLRNILGTKTLTEMLSDRDVISLQMQATLDETTIPWGVKVERVEMKDVRLPYQLQRVMAAE 211
Cdd:cd08827  81 VCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17570459 212 AEATRDAMAKIIAAEGEKNASTALAEAADVISMSPCAIQLRYLQTLNSISSEKNNTIVFPFP 273
Cdd:cd08827 161 AEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLP 222

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  78 RGPGLFFVVPCIDSYKKIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNATISVINIEDAARSTKLLAQTTLRNILG 157
Cdd:cd08828   1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17570459 158 TKTLTEMLSDRDVISLQMQATLDETTIPWGVKVERVEMKDVRLPYQLQRVMAAEAEATRDAMAKIIAAEGEKNA 231
Cdd:cd08828  81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  80 PGLFFVVPCIDSYKKIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNATISVINIEDAARSTKLLAQTTLRNILGTK 159
Cdd:cd13437  29 PGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRIDNVKQALIERTQTTLRSVIGER 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459 160 TLTEMLSDRDVISLQMQATLDETTIPWGVKVERVEMKDVRLPYQLQRVMAAEAEATRDAMAKIIAAEGEKNASTALAEAA 239
Cdd:cd13437 109 TLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIGESKIISAKADVESAKLMREAA 188

                       170       180       190
                ....*....|....*....|....*....|.
gi 17570459 240 DVISmSPCAIQLRYLQTLNSISSEKNNTIVF 270
Cdd:cd13437 189 DILD-SKAAMQIRYLETLQAIAKSANSKVIF 218

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  95 IDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNATISVINIEDAARSTKLLAQTTLRNILGTKTLTEMLSDRDVISLQ 174
Cdd:cd13775   1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459 175 MQATLDETTIPWGVKVERVEMKDVRLPYQLQRVMAAEAEATRDAMAKIIAAEGEKNASTALAEAADVISMSPCAIQLRYL 254
Cdd:cd13775  81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160

                       170
                ....*....|....*..
gi 17570459 255 QTLNSISSEKNNTIVFP 271
Cdd:cd13775 161 NMLYEGLKEKGSMVVVP 177

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  70 GRVKPggARGPGLFFVVPCIDSYKKIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNATISVINIEDAARSTKLLAQ 149
Cdd:cd13436   1 GRLQK--PRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQ 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17570459 150 TTLRNILGTKTLTEMLSDRDVISLQMQATLDETTIPWGVKVERVEMKDVRL 200
Cdd:cd13436  79 TSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  94 KIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNATISVINIEDAARSTKLLAQTTLRNILGTKTLTEMLSDRDVISL 173
Cdd:cd08829   3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                        90       100
                ....*....|....*....|....*...
gi 17570459 174 QMQATLDETTIPWGVKVERVEMKDVRLP 201
Cdd:cd08829  83 KLLEALDEATDPWGVKVTRVEIKDITPP 110

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  54 CVKVAQEYERAVIFRLGRVKpGGARGPGLFFVVPCIDSYKKIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNAT-- 131
Cdd:cd03405   1 SVFIVDETEQAVVLQFGKPV-RVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLrf 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459 132 -ISVINIEDAARstkLLAQ---TTLRNILGTKTLTEMLSD-RDVISLQMQATLDETTIPWGVKVERVEMKDVRLPYQ-LQ 205
Cdd:cd03405  80 yQSVGGEEGAES---RLDDivdSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEvSE 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17570459 206 RV---MAAEaeatRDAMAKIIAAEGEKNASTALAEA 238
Cdd:cd03405 157 SVyerMRAE----RERIAAEYRAEGEEEAEKIRAEA 188

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  41 ILAVLTLPISVFLCVKVAQEYERAVIFRLGRVKpgGARGPGLFFVVPC-IDSYKKID---LRTLS--FEVPPQEL-LSKD 113
Cdd:cd03404   1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKYV--RTVGPGLHWKLPFpIEVVEKVNvtqVRSVEigFRVPEESLmLTGD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459 114 AVTVAVDAVVFFRISNATISVINIEDAARSTKLLAQTTLRNILGTKTLTEMLS-DRDVISLQ----MQATLDETTIpwGV 188
Cdd:cd03404  79 ENIVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADvrelLQEILDRYDL--GI 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17570459 189 KVERVEMKDVRLPYQLQR----VMAAE-------AEATRDAMAKIIAAEGEKNA--STALAEAADVIS 243
Cdd:cd03404 157 EIVQVQLQDADPPEEVQDafddVNAARqdkerliNEAQAYANEVIPRARGEAARiiQEAEAYKAEVVA 224

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17570459 133 SVINIEDAARSTkllAQTTLRNILGTKTLTEMLSDRDVISLQMQATLDETTIPWGVKVERVEMKDVRLP 201
Cdd:cd02106  44 FVKDIKADIRRK---IADVLRAAIGRMTLDQIISGRDEIAKAVKEDLEEDLENFGVVISDVDITSIEPP 109

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  62 ERAVIFRLGRVKpGGARGPGLFFVVPCIdSYKKIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNATISVINIEDAA 141
Cdd:cd03402  17 EAAVLTLFGRYR-GTVRRPGLRWVNPFY-RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWRVVDTAKAVFDVDDYE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459 142 RSTKLLAQTTLRNIL----------GTKTLTemlSDRDVISLQMQATLDETTIPWGVKVerVEMKDVRLPY-------QL 204
Cdd:cd03402  95 EFVSIQSEAALRRVAsrypydsfedGEPSLR---GNSDEVSEELRRELQERLAVAGVEV--IEARITHLAYapeiaqaML 169

                       170
                ....*....|....*...
gi 17570459 205 QRVmaaEAEATRDAMAKI 222
Cdd:cd03402 170 QRQ---QASAIIAARQTI 184

Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; The flotillin (reggie) like proteins are lipid raft-associated. Individual proteins of this SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. In addition, microdomains formed from flotillin proteins may be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and interact with a variety of proteins. They may play a role 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570459  84 FVVPCIDSYKKIDLRTLSFEVPPQELLSKDAVTVAVDAVVFFRISNATISVINiedAARstKLLAQTT------------ 151
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAA---AAE--RFLGKSTeeirelvketle 75

                        90       100
                ....*....|....*....|
gi 17570459 152 --LRNILGTKTLTEMLSDRD 169
Cdd:cd03399  76 ghLRAIVGTMTVEEIYQDRE 95