ID   ATPL2_CAEEL             Reviewed;         131 AA.
AC   Q18803;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Probable ATP synthase subunit g 2, mitochondrial;
DE            Short=ATPase subunit g 2;
GN   Name=asg-2 {ECO:0000312|WormBase:C53B7.4};
GN   ORFNames=C53B7.4 {ECO:0000312|WormBase:C53B7.4};
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
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. Part of the complex
CC       F(0) domain. Minor subunit located with subunit a in the membrane.
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 g subunit family. {ECO:0000305}.
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DR   EMBL; BX284606; CCD67887.1; -; Genomic_DNA.
DR   PIR; T28801; T28801.
DR   RefSeq; NP_509152.1; NM_076751.4.
DR   AlphaFoldDB; Q18803; -.
DR   SMR; Q18803; -.
DR   BioGRID; 45884; 38.
DR   STRING; 6239.C53B7.4; -.
DR   EPD; Q18803; -.
DR   PaxDb; Q18803; -.
DR   PeptideAtlas; Q18803; -.
DR   EnsemblMetazoa; C53B7.4.1; C53B7.4.1; WBGene00000210.
DR   GeneID; 180956; -.
DR   KEGG; cel:CELE_C53B7.4; -.
DR   UCSC; C53B7.4; c. elegans.
DR   CTD; 180956; -.
DR   WormBase; C53B7.4; CE06974; WBGene00000210; asg-2.
DR   eggNOG; KOG4103; Eukaryota.
DR   GeneTree; ENSGT00390000009724; -.
DR   HOGENOM; CLU_152793_1_0_1; -.
DR   InParanoid; Q18803; -.
DR   OMA; PPRQADW; -.
DR   OrthoDB; 1461139at2759; -.
DR   PhylomeDB; Q18803; -.
DR   Reactome; R-CEL-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-CEL-8949613; Cristae formation.
DR   PRO; PR:Q18803; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00000210; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR   GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR   InterPro; IPR006808; ATP_synth_F0_gsu_mt.
DR   PANTHER; PTHR12386; PTHR12386; 1.
DR   Pfam; PF04718; ATP-synt_G; 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..131
FT                   /note="Probable ATP synthase subunit g 2, mitochondrial"
FT                   /id="PRO_0000071694"
SQ   SEQUENCE   131 AA;  14834 MW;  466C770E311DD3DC CRC64;
     MAAPKLGFFE KIANLTGALY RHQHAQFPRR FAILKAVGKH ELAPPRQADW PAIKADWAKV
     QSFIQTGGYK NLSIREGLVY TAVTLEVVFW FFVGEMIGRR YIFGYLVPAD YVSKSTKKTV
     KEQEALAALE N