ID   ATPK_CAEEL              Reviewed;         153 AA.
AC   Q22021;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Putative ATP synthase subunit f, mitochondrial;
GN   ORFNames=R53.4 {ECO:0000312|WormBase:R53.4};
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).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC       Complex V) produces ATP from ADP in the presence of a proton gradient
CC       across the membrane which is generated by electron transport complexes
CC       of the respiratory chain. F-type ATPases consist of two structural
CC       domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC       - containing the membrane proton channel, linked together by a central
CC       stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC       catalytic domain of F(1) is coupled via a rotary mechanism of the
CC       central stalk subunits to proton translocation. Part of the complex
CC       F(0) domain. Minor subunit located with subunit a in the membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Subunit of the F-type ATPase which has 2 components, CF(1)
CC       - the catalytic core - and CF(0) - the membrane proton channel.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase F chain family. {ECO:0000305}.
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DR   EMBL; BX284602; CAA91350.1; -; Genomic_DNA.
DR   PIR; T24247; T24247.
DR   RefSeq; NP_496152.1; NM_063751.6.
DR   AlphaFoldDB; Q22021; -.
DR   SMR; Q22021; -.
DR   BioGRID; 39874; 10.
DR   IntAct; Q22021; 2.
DR   MINT; Q22021; -.
DR   STRING; 6239.R53.4; -.
DR   EPD; Q22021; -.
DR   PaxDb; Q22021; -.
DR   PeptideAtlas; Q22021; -.
DR   EnsemblMetazoa; R53.4.1; R53.4.1; WBGene00011273.
DR   GeneID; 174554; -.
DR   KEGG; cel:CELE_R53.4; -.
DR   UCSC; R53.4.1; c. elegans.
DR   CTD; 174554; -.
DR   WormBase; R53.4; CE03574; WBGene00011273; -.
DR   eggNOG; KOG4092; Eukaryota.
DR   GeneTree; ENSGT00940000175005; -.
DR   HOGENOM; CLU_1612248_0_0_1; -.
DR   InParanoid; Q22021; -.
DR   OMA; HRYLDFQ; -.
DR   OrthoDB; 1479342at2759; -.
DR   PhylomeDB; Q22021; -.
DR   Reactome; R-CEL-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-CEL-8949613; Cristae formation.
DR   PRO; PR:Q22021; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00011273; Expressed in embryo and 4 other tissues.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR   InterPro; IPR019344; F1F0-ATPsyn_F_prd.
DR   PANTHER; PTHR13080; PTHR13080; 1.
DR   Pfam; PF10206; WRW; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Reference proteome; Transport.
FT   CHAIN           1..153
FT                   /note="Putative ATP synthase subunit f, mitochondrial"
FT                   /id="PRO_0000194828"
SQ   SEQUENCE   153 AA;  18750 MW;  A983B58DA4A701E2 CRC64;
     MAWFRPPPPH TQLRPWVPDA IFIPISRAVE RVGVFFYNRV LNKTEVGLFD KRWNKNVHGP
     YCHWRYYGKL DTKFMDVKLG DLPAWMARRE KTPSAFYNEF MRNIWRVHNL YYSGPVYNNT
     VKVIFRFIFA YSFLNWLVKS HRYVDFQKTM YHW