ID   ATPD_CAEEL              Reviewed;         163 AA.
AC   Q09544;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=ATP synthase subunit delta, mitochondrial;
DE   AltName: Full=F-ATPase delta subunit;
DE   Flags: Precursor;
GN   ORFNames=F58F12.1 {ECO:0000312|WormBase:F58F12.1};
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   PROTEIN SEQUENCE OF 19-36.
RC   STRAIN=Bristol N2;
RX   PubMed=9150941; DOI=10.1002/elps.1150180337;
RA   Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R.;
RT   "Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates
RT   and identification of protein spots by microsequencing.";
RL   Electrophoresis 18:557-562(1997).
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 turnover in
CC       the 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(1) domain and of the central stalk which is part of the complex
CC       rotary element (Probable). {ECO:0000305}.
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. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR   EMBL; BX284602; CCD72069.1; -; Genomic_DNA.
DR   PIR; T16501; T16501.
DR   RefSeq; NP_495286.1; NM_062885.5.
DR   AlphaFoldDB; Q09544; -.
DR   SMR; Q09544; -.
DR   BioGRID; 39399; 47.
DR   DIP; DIP-27343N; -.
DR   IntAct; Q09544; 1.
DR   STRING; 6239.F58F12.1; -.
DR   EPD; Q09544; -.
DR   PaxDb; Q09544; -.
DR   PeptideAtlas; Q09544; -.
DR   EnsemblMetazoa; F58F12.1.1; F58F12.1.1; WBGene00019061.
DR   GeneID; 174059; -.
DR   KEGG; cel:CELE_F58F12.1; -.
DR   UCSC; F58F12.1.1; c. elegans.
DR   CTD; 174059; -.
DR   WormBase; F58F12.1; CE01976; WBGene00019061; -.
DR   eggNOG; KOG1758; Eukaryota.
DR   GeneTree; ENSGT00390000017576; -.
DR   HOGENOM; CLU_084338_0_1_1; -.
DR   InParanoid; Q09544; -.
DR   OMA; TLPHQTI; -.
DR   OrthoDB; 1286602at2759; -.
DR   PhylomeDB; Q09544; -.
DR   Reactome; R-CEL-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-CEL-8949613; Cristae formation.
DR   PRO; PR:Q09544; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00019061; Expressed in larva and 4 other tissues.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR   CDD; cd12152; F1-ATPase_delta; 1.
DR   Gene3D; 2.60.15.10; -; 1.
DR   HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR   InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   PANTHER; PTHR13822; PTHR13822; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; SSF51344; 1.
DR   TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..18
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:9150941"
FT   CHAIN           19..163
FT                   /note="ATP synthase subunit delta, mitochondrial"
FT                   /id="PRO_0000002665"
SQ   SEQUENCE   163 AA;  16927 MW;  9969F2D763139CA7 CRC64;
     MLARTIQRFS VVAKRGYAAA APAANANPEE LRLTFASPDT AVFSNAVVKQ VDVPTLAGMV
     GVLANHVPTI GVLKPGVVSV TTNEGTVQRL FVSSGTLSVN IDGSCQVLAE EVLKVEEIDE
     SAARAELDAA QRASGEGSEV ARAEAQIRAE VAEALIKAAT NQQ