ATP8_SALSA
ID ATP8_SALSA Reviewed; 55 AA.
AC P68529; P48179;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=ATP synthase protein 8;
DE AltName: Full=A6L;
DE AltName: Full=F-ATPase subunit 8;
GN Name=mt-atp8; Synonyms=atp8, atpase8, mtatp8;
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.
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: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase protein 8 family. {ECO:0000305}.
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DR EMBL; U12143; AAD04737.1; -; Genomic_DNA.
DR EMBL; AF133701; AAF61382.1; -; Genomic_DNA.
DR PIR; T09951; T09951.
DR RefSeq; NP_008449.1; NC_001960.1.
DR AlphaFoldDB; P68529; -.
DR SMR; P68529; -.
DR STRING; 8030.ENSSSAP00000000006; -.
DR GeneID; 808310; -.
DR KEGG; sasa:808310; -.
DR CTD; 4509; -.
DR OMA; MPQLNPN; -.
DR OrthoDB; 1621322at2759; -.
DR Proteomes; UP000087266; Mitochondrion MT.
DR Bgee; ENSSSAG00000000022; Expressed in zone of skin and 16 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
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 InterPro; IPR001421; ATP8_metazoa.
DR Pfam; PF00895; ATP-synt_8; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..55
FT /note="ATP synthase protein 8"
FT /id="PRO_0000195584"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 55 AA; 6413 MW; D02920C3E346925F CRC64;
MPQLNPAPWF AILVFSWLVF LTVIPPKVLG HTFTNEPTSQ STEKAKPEPW NWPWH
