ATP6_SALSA
ID ATP6_SALSA Reviewed; 227 AA.
AC Q35920;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 3.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=mt-atp6; Synonyms=atp6, atpase6, mtatp6;
OS Salmo salar (Atlantic salmon).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=10548724; DOI=10.1016/s0378-1119(99)00425-4;
RA Hurst C.D., Bartlett S.E., Davidson W.S., Bruce I.J.;
RT "The complete mitochondrial DNA sequence of the Atlantic salmon, Salmo
RT salar.";
RL Gene 239:237-242(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Arnason U., Johnsson E., Rasmussen A.S.;
RT "The complete mitochondrial genome sequence of a teleost, Salmo salar, and
RT comparisons with other salmoniformes.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-98.
RX PubMed=2744446; DOI=10.1139/g89-451;
RA Davidson W.S., Birt T.P., Green J.M.;
RT "Organisation of the mitochondrial genome from Atlantic salmon (Salmo
RT salar).";
RL Genome 32:340-342(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-227.
RX PubMed=9007022; DOI=10.1006/mpev.1996.0373;
RA Oohara I., Sawano K., Okazaki T.;
RT "Mitochondrial DNA sequence analysis of the masu salmon -- phylogeny in the
RT genus Oncorhynchus.";
RL Mol. Phylogenet. Evol. 7:71-78(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 220-227.
RC TISSUE=Liver;
RX PubMed=8000479;
RA Hardiman G., Byrnes L., Peden J., Wolff J., Gannon F.;
RT "Cloning and sequencing of the Atlantic salmon (Salmo salar) cytochrome c
RT oxidase subunit III gene (coxIII) and analysis of coxIII expression during
RT parr-smolt transformation.";
RL Mol. Mar. Biol. Biotechnol. 3:210-216(1994).
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. Key component of the
CC proton channel; it may play a direct role in the translocation of
CC protons across the membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR EMBL; U12143; AAD04738.1; -; Genomic_DNA.
DR EMBL; AF133701; AAF61383.1; -; Genomic_DNA.
DR EMBL; D84148; BAA20157.1; -; Genomic_DNA.
DR EMBL; L04502; AAA62408.1; -; Genomic_DNA.
DR PIR; T09952; T09952.
DR RefSeq; NP_008450.1; NC_001960.1.
DR AlphaFoldDB; Q35920; -.
DR SMR; Q35920; -.
DR STRING; 8030.ENSSSAP00000000007; -.
DR GeneID; 808313; -.
DR KEGG; sasa:808313; -.
DR CTD; 4508; -.
DR OMA; FFDQFMS; -.
DR OrthoDB; 1095315at2759; -.
DR Proteomes; UP000087266; Mitochondrion MT.
DR Bgee; ENSSSAG00000000023; Expressed in mesonephros and 16 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR Gene3D; 1.20.120.220; -; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..227
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082167"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 8
FT /note="Q -> E (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 73..86
FT /note="LTSLMLFLITLNML -> QLPNMFFITSNNLM (in Ref. 3; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="Y -> H (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 96..98
FT /note="TTQ -> HTL (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25108 MW; C6664DA82423EB26 CRC64;
MTLSFFDQFM SPTYLGIPLI AVALTLPWIL FPTPSTRWLN NRLITLQGWF INRFTQQLLL
PLNLGGHKWA VLLTSLMLFL ITLNMLGLLP YTFTPTTQLS LNMGLAVPLW LATVIIGMRN
QPTAALGHLL PEGTPVPLIP VLIIIETISL FIRPLALGVR LTANLTAGHL LIQLIATAAF
VLMPIMPTVA ILTSIVLFLL TLLEIAVAMI QAYVFVLLLS LYLQENV
