ATPL1_CAEEL
ID ATPL1_CAEEL Reviewed; 131 AA.
AC P90921;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable ATP synthase subunit g 1, mitochondrial;
DE Short=ATPase subunit g 1;
GN Name=asg-1 {ECO:0000312|WormBase:K07A12.3};
GN ORFNames=K07A12.3 {ECO:0000312|WormBase:K07A12.3};
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 (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 g subunit family. {ECO:0000305}.
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DR EMBL; BX284601; CAB03179.1; -; Genomic_DNA.
DR PIR; T23392; T23392.
DR RefSeq; NP_492352.1; NM_059951.5.
DR AlphaFoldDB; P90921; -.
DR SMR; P90921; -.
DR BioGRID; 38106; 43.
DR STRING; 6239.K07A12.3; -.
DR EPD; P90921; -.
DR PaxDb; P90921; -.
DR PeptideAtlas; P90921; -.
DR EnsemblMetazoa; K07A12.3.1; K07A12.3.1; WBGene00000209.
DR GeneID; 172673; -.
DR KEGG; cel:CELE_K07A12.3; -.
DR UCSC; K07A12.3.1; c. elegans.
DR CTD; 172673; -.
DR WormBase; K07A12.3; CE11868; WBGene00000209; asg-1.
DR eggNOG; KOG4103; Eukaryota.
DR GeneTree; ENSGT00390000009724; -.
DR HOGENOM; CLU_152793_1_0_1; -.
DR InParanoid; P90921; -.
DR OMA; CWHKELK; -.
DR OrthoDB; 1461139at2759; -.
DR PhylomeDB; P90921; -.
DR PRO; PR:P90921; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000209; Expressed in germ line (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: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 InterPro; IPR016702; ATP_synth_su_G_mt_met.
DR PANTHER; PTHR12386; PTHR12386; 1.
DR Pfam; PF04718; ATP-synt_G; 1.
DR PIRSF; PIRSF017835; ATP-synth_g_mitoch_animal; 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 1, mitochondrial"
FT /id="PRO_0000071695"
SQ SEQUENCE 131 AA; 14920 MW; E50872543A258383 CRC64;
MATHKLSFFE KLANTFGALY RHQAQQFPRR LAILKAVGKH ELAPPRSADI PAIKADWAKL
QKFIETKQYV NLSIKESLVY SAVALEVVFW FFVGEMIGRR YIFGYIVPAN YVSKDTKAKV
AEKKRLAALE A