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prohibitin-like [Mus musculus]
prohibitin family protein( domain architecture ID 10130412)
prohibitin family protein similar to Homo sapiens prohibitin, a lipid raft-associated integral membrane protein that inhibits DNA synthesis and has a role in regulating proliferation
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
SPFH_prohibitin | cd03401 | Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
27-221 | 8.23e-92 | ||||
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: 269.38 E-value: 8.23e-92
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Name | Accession | Description | Interval | E-value | |||||
SPFH_prohibitin | cd03401 | Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
27-221 | 8.23e-92 | |||||
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: 269.38 E-value: 8.23e-92
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PHB | smart00244 | prohibitin homologues; prohibitin homologues |
26-187 | 4.36e-35 | |||||
prohibitin homologues; prohibitin homologues Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 123.54 E-value: 4.36e-35
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HflC | COG0330 | Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
12-263 | 1.55e-33 | |||||
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 123.03 E-value: 1.55e-33
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Band_7 | pfam01145 | SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
30-207 | 4.29e-33 | |||||
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: 118.96 E-value: 4.29e-33
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Name | Accession | Description | Interval | E-value | |||||
SPFH_prohibitin | cd03401 | Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
27-221 | 8.23e-92 | |||||
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: 269.38 E-value: 8.23e-92
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PHB | smart00244 | prohibitin homologues; prohibitin homologues |
26-187 | 4.36e-35 | |||||
prohibitin homologues; prohibitin homologues Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 123.54 E-value: 4.36e-35
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HflC | COG0330 | Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
12-263 | 1.55e-33 | |||||
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 123.03 E-value: 1.55e-33
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Band_7 | pfam01145 | SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
30-207 | 4.29e-33 | |||||
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: 118.96 E-value: 4.29e-33
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SPFH_HflC | cd03405 | High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ... |
26-231 | 4.08e-15 | |||||
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: 72.91 E-value: 4.08e-15
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SPFH_like | cd02106 | core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
77-177 | 3.31e-09 | |||||
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: 53.52 E-value: 3.31e-09
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SPFH_eoslipins_u2 | cd13438 | Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ... |
112-248 | 6.71e-09 | |||||
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial SLPs remain uncharacterized. Pssm-ID: 259816 [Multi-domain] Cd Length: 215 Bit Score: 54.46 E-value: 6.71e-09
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SPFH_SLP-4 | cd13435 | Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ... |
51-268 | 1.31e-08 | |||||
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: 53.93 E-value: 1.31e-08
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SPFH_like_u4 | cd03407 | Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
36-241 | 3.54e-08 | |||||
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome. Pssm-ID: 259805 [Multi-domain] Cd Length: 269 Bit Score: 52.97 E-value: 3.54e-08
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SPFH_alloslipin | cd13437 | Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ... |
28-261 | 6.56e-08 | |||||
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: 51.85 E-value: 6.56e-08
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SPFH_HflK | cd03404 | High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ... |
13-257 | 6.72e-06 | |||||
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: 46.35 E-value: 6.72e-06
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SPFH_eoslipins_u1 | cd08826 | Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ... |
59-248 | 5.25e-05 | |||||
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: 42.89 E-value: 5.25e-05
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YqiK | COG2268 | Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
127-222 | 1.80e-04 | |||||
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 1.80e-04
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Blast search parameters | ||||
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