ATP8_SALFO
ID ATP8_SALFO Reviewed; 55 AA.
AC Q9XN35;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 Salvelinus fontinalis (Brook trout) (Salmo fontinalis).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salvelinus.
OX NCBI_TaxID=8038;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Doiron S., Blier P.U., Bernatchez L.;
RT "A comparative analysis of complete sequence of mitochondrial genome
RT between brook char (Salvelinus fontinalis) and arctic char (S. alpinus).";
RL Submitted (MAY-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF154850; AAD41376.1; -; Genomic_DNA.
DR RefSeq; NP_008664.1; NC_000860.1.
DR AlphaFoldDB; Q9XN35; -.
DR SMR; Q9XN35; -.
DR GeneID; 808533; -.
DR CTD; 4509; -.
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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..55
FT /note="ATP synthase protein 8"
FT /id="PRO_0000195583"
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; 6443 MW; D02930C2E346925F CRC64;
MPQLNPAPWF AILVFSWLVF LTVIPPKVLG HTFTNEPTSQ STEKTKPEPW NWPWH