ID   PHB1_CAEEL              Reviewed;         275 AA.
AC   Q9BKU4;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Mitochondrial prohibitin complex protein 1;
DE            Short=Prohibitin-1;
GN   Name=phb-1; ORFNames=Y37E3.9;
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).
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. {ECO:0000269|PubMed:12794069}.
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}.
CC   -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
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DR   EMBL; FO081769; CCD73430.1; -; Genomic_DNA.
DR   RefSeq; NP_490929.1; NM_058528.4.
DR   AlphaFoldDB; Q9BKU4; -.
DR   SMR; Q9BKU4; -.
DR   BioGRID; 37255; 15.
DR   ComplexPortal; CPX-4114; Prohibitin complex.
DR   IntAct; Q9BKU4; 1.
DR   STRING; 6239.Y37E3.9; -.
DR   EPD; Q9BKU4; -.
DR   PaxDb; Q9BKU4; -.
DR   PeptideAtlas; Q9BKU4; -.
DR   EnsemblMetazoa; Y37E3.9.1; Y37E3.9.1; WBGene00004014.
DR   GeneID; 171768; -.
DR   KEGG; cel:CELE_Y37E3.9; -.
DR   UCSC; Y37E3.9; c. elegans.
DR   CTD; 171768; -.
DR   WormBase; Y37E3.9; CE26775; WBGene00004014; phb-1.
DR   eggNOG; KOG3083; Eukaryota.
DR   GeneTree; ENSGT00950000183070; -.
DR   HOGENOM; CLU_047969_0_0_1; -.
DR   InParanoid; Q9BKU4; -.
DR   OMA; QKMQFVL; -.
DR   OrthoDB; 1089994at2759; -.
DR   PhylomeDB; Q9BKU4; -.
DR   Reactome; R-CEL-5673000; RAF activation.
DR   Reactome; R-CEL-8949664; Processing of SMDT1.
DR   PRO; PR:Q9BKU4; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00004014; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
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; IBA:GO_Central.
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: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.
FT   CHAIN           1..275
FT                   /note="Mitochondrial prohibitin complex protein 1"
FT                   /id="PRO_0000213882"
FT   COILED          180..213
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   275 AA;  29988 MW;  2C0440785DDBD072 CRC64;
     MAASAQKLLG RLGTVGVGLS IAGGIAQTAL YNVDGGQRAV IFDRFSGVKN EVVGEGTHFL
     IPWVQKPIIF DIRSTPRAVT TITGSKDLQN VNITLRILHR PSPDRLPNIY LNIGLDYAER
     VLPSITNEVL KAVVAQFDAH EMITQREVVS QRASVALRER AAQFGLLLDD IAITHLNFGR
     EFTEAVEMKQ VAQQEAEKAR YLVEKAEQMK IAAVTTAEGD AQAAKLLAKA FASAGDGLVE
     LRKIEAAEEI AERMAKNKNV TYLPGNQQTL LNLQS