PHB2_CAEEL
ID PHB2_CAEEL Reviewed; 294 AA.
AC P50093;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Mitochondrial prohibitin complex protein 2;
DE Short=Prohibitin-2;
GN Name=phb-2; ORFNames=T24H7.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12794069; DOI=10.1074/jbc.m304877200;
RA Artal-Sanz M., Tsang W.Y., Willems E.M., Grivell L.A., Lemire B.D.,
RA van der Spek H., Nijtmans L.G., Sanz M.A.;
RT "The mitochondrial prohibitin complex is essential for embryonic viability
RT and germline function in Caenorhabditis elegans.";
RL J. Biol. Chem. 278:32091-32099(2003).
RN [3]
RP FUNCTION.
RX PubMed=28017329; DOI=10.1016/j.cell.2016.11.042;
RA Wei Y., Chiang W.C., Sumpter R. Jr., Mishra P., Levine B.;
RT "Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor.";
RL Cell 168:224.e10-238.e10(2017).
CC -!- FUNCTION: PHB proteins are essential during embryonic development and
CC are required for somatic and germline differentiation in the larval
CC gonad. A deficiency in PHB proteins results in altered mitochondrial
CC biogenesis in body wall muscle cells (PubMed:12794069). Required for
CC clearance of paternal mitochondria after embryonic fertilization
CC (PubMed:28017329). {ECO:0000269|PubMed:12794069,
CC ECO:0000269|PubMed:28017329}.
CC -!- SUBUNIT: High molecular weight complex that consist of phb-1 and phb-2.
CC {ECO:0000269|PubMed:12794069}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:12794069}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12794069}; Intermembrane side
CC {ECO:0000269|PubMed:12794069}.
CC -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
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DR EMBL; FO080720; CCD66149.1; -; Genomic_DNA.
DR PIR; H88175; H88175.
DR RefSeq; NP_495250.2; NM_062849.4.
DR AlphaFoldDB; P50093; -.
DR SMR; P50093; -.
DR BioGRID; 39374; 16.
DR ComplexPortal; CPX-4114; Prohibitin complex.
DR DIP; DIP-26193N; -.
DR STRING; 6239.T24H7.1; -.
DR EPD; P50093; -.
DR PaxDb; P50093; -.
DR PeptideAtlas; P50093; -.
DR EnsemblMetazoa; T24H7.1.1; T24H7.1.1; WBGene00004015.
DR GeneID; 174034; -.
DR KEGG; cel:CELE_T24H7.1; -.
DR UCSC; T24H7.1; c. elegans.
DR CTD; 174034; -.
DR WormBase; T24H7.1; CE40718; WBGene00004015; phb-2.
DR eggNOG; KOG3090; Eukaryota.
DR GeneTree; ENSGT00950000183070; -.
DR HOGENOM; CLU_047969_0_2_1; -.
DR InParanoid; P50093; -.
DR OMA; IKYTRLG; -.
DR OrthoDB; 1089994at2759; -.
DR PhylomeDB; P50093; -.
DR Reactome; R-CEL-8949664; Processing of SMDT1.
DR PRO; PR:P50093; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004015; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:WormBase.
DR GO; GO:0035632; C:mitochondrial prohibitin complex; IDA:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IC:ComplexPortal.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0008406; P:gonad development; IMP:WormBase.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:WormBase.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0000423; P:mitophagy; IDA:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IMP:WormBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:WormBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:WormBase.
DR CDD; cd03401; SPFH_prohibitin; 1.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR000163; Prohibitin.
DR PANTHER; PTHR23222; PTHR23222; 1.
DR Pfam; PF01145; Band_7; 1.
DR PRINTS; PR00679; PROHIBITIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..294
FT /note="Mitochondrial prohibitin complex protein 2"
FT /id="PRO_0000213887"
FT TRANSMEM 20..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT COILED 212..237
FT /evidence="ECO:0000255"
SQ SEQUENCE 294 AA; 32668 MW; 4780712A1E8773E7 CRC64;
MAKQGQEAMK KAIQNARGAG VGLGLVAAAG AAVYGVAQSM FTVEAGHRAI MFNRIGGLST
DLYKEGLHFR IPWFQYPIIY DIRARPNQIR SPTGSKDLQM VNIGLRVLSR PNPEHLVHIY
RTLGQNWEER VLPSICNEVL KGVVAKFNAS QLITQRQQVS MLVRKTLIER ALDFNIILDD
VSLTELAFSP QYSAAVEAKQ VAAQEAQRAT FYVERAKQQK QEKIVQAEGE AESAKLLGEA
MKNDPGFLKL RKIRAAQKIA RIVSESGNKT YLPTGGLMLN IADTDYLNVT DKRR
