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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2469478536   1 MDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPP 75
Cdd:cd08829    37 VDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAKLLEALDEATDPWGVKVTRVEIKDITPPE 111

prohibitin homologues; prohibitin homologues

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469478536    2 DPYKASYGVEDPEYAVT-QLAQTTMRSELGKLSLDKVFR-ERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKE 79
Cdd:smart00244  75 DPLRAVYRVLDADYAVIeQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKE 154

                   ....*.
gi 2469478536   80 SMQMQV 85
Cdd:smart00244 155 AMEAQQ 160

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2469478536   1 MDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPP 75
Cdd:cd08829    37 VDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAKLLEALDEATDPWGVKVTRVEIKDITPPE 111

C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal extension of the Band_7 family, pfam01145. It is found in proteins fro bacteria to fungi, plants and mammals.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2469478536 150 RILAGALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTVLLPSNPSDVTSMVAQAMGVYGALTK 212
Cdd:pfam16200   1 EKVAEAIKKPGGQEAVSLRVAEQYVEAFGKLAKESNTVILPANLGDVSSMVAQAMSIYKKVNK 63

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469478536   2 DPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESM 81
Cdd:cd13435    56 DPLNAVIQVANYSHSTRLLAATTLRNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAM 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2469478536  82 QMQVEAERRKRATVLESEGTRESainvAEGKKQAQILASEAEKAEQI 128
Cdd:cd13435   136 AAEAEAAREARAKVIAAEGEMKS----SRALKEASDIISASPSALQL 178

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2469478536   2 DPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVP 74
Cdd:cd13434    35 DPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQEILDEATDPWGIKVERVEIKDIILP 107

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 2469478536  10 VEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAER 89
Cdd:cd03403    64 VENADRSTRLLAQTTLRNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAR 143

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2469478536  90 RKRATVLESEGTResaiNVAEGKKQAQILASEAEKAEQI 128
Cdd:cd03403   144 EARAKVIAAEGEQ----NASRALKEAADVISESPAALQL 178

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 2469478536   2 DPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNANIVDAINQAADCW--GIRCLRYEIKDIHVPPRVK 78
Cdd:cd03404    94 DPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRYdlGIEIVQVQLQDADPPEEVQ 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2469478536  79 ESMQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 134
Cdd:cd03404   174 DAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGD 229

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469478536   2 DPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESM 81
Cdd:cd13438    72 DPVKAVETVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREIL 151

                          90
                  ....*....|..
gi 2469478536  82 QMQVEAERRKRA 93
Cdd:cd13438   152 NQVLEAEKRAQA 163

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 2469478536   4 YKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQM 83
Cdd:cd03407    75 YDAFYKLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNE 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469478536  84 QVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAeKAEQiNQAageasavlakakakaeairILAG------ALT 157
Cdd:cd03407   155 INAAQRLREAAEEKAEAEKILQVKAAEAEAEAKRLQGVG-IAEQ-RKA-------------------IVDGlresieDFQ 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2469478536 158 QHNGDAAAS----LTVAEQYVSAFSKLAKDS--NTVLLPSNPSDVTSMVAQ 202
Cdd:cd03407   214 EAVPGVSSKevmdLLLITQYFDTLKEVGKSSksSTVFLPHGPGGVSDISAQ 264

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2469478536   2 DPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHV 73
Cdd:cd13436    58 DPVLSVMAVQDLNTSTRTTAQTSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129