ATP8_CANLF
ID ATP8_CANLF Reviewed; 67 AA.
AC Q9ZZ63;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 127.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Boxer {ECO:0000312|Proteomes:UP000002254};
RX PubMed=9878232; DOI=10.1006/mpev.1998.0513;
RA Kim K.S., Lee S.E., Jeong H.W., Ha J.H.;
RT "The complete nucleotide sequence of the domestic dog (Canis familiaris)
RT mitochondrial genome.";
RL Mol. Phylogenet. Evol. 10:210-220(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Beagle;
RA Zhu S., Xu Q., Chang H.;
RT "The complete mitochondrial DNA sequence of the Beagle dog (Canis
RT familiaris).";
RL Submitted (AUG-2004) 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. Component of an ATP synthase
CC complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF,
CC ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO,
CC ATP5MG, ATP5MK and ATP5MJ (By similarity). Interacts with PRICKLE3 (By
CC similarity). {ECO:0000250|UniProtKB:P03928}.
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; U96639; AAD04767.1; -; Genomic_DNA.
DR EMBL; AY729880; AAU12160.1; -; Genomic_DNA.
DR PIR; T11497; T11497.
DR RefSeq; NP_008475.1; NC_002008.4.
DR AlphaFoldDB; Q9ZZ63; -.
DR SMR; Q9ZZ63; -.
DR STRING; 9612.ENSCAFP00000030313; -.
DR PaxDb; Q9ZZ63; -.
DR PRIDE; Q9ZZ63; -.
DR GeneID; 804487; -.
DR KEGG; cfa:804487; -.
DR CTD; 4509; -.
DR eggNOG; ENOG502T21P; Eukaryota.
DR HOGENOM; CLU_2811757_0_0_1; -.
DR InParanoid; Q9ZZ63; -.
DR OMA; LDTSTWF; -.
DR OrthoDB; 1621322at2759; -.
DR TreeFam; TF343854; -.
DR Reactome; R-CFA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-CFA-8949613; Cristae formation.
DR Proteomes; UP000002254; Mitochondrion.
DR Bgee; ENSCAFG00000022728; Expressed in adrenal cortex and 44 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
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; IPR039017; ATP8_mammal.
DR InterPro; IPR001421; ATP8_metazoa.
DR PANTHER; PTHR13722; PTHR13722; 1.
DR Pfam; PF00895; ATP-synt_8; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP synthesis; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..67
FT /note="ATP synthase protein 8"
FT /id="PRO_0000195499"
FT TRANSMEM 8..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 54
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P03930"
FT MOD_RES 54
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P03930"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P03930"
SQ SEQUENCE 67 AA; 7978 MW; 3B313377275A0AC6 CRC64;
MPQLDTSTWF IMIFSMFLTL FILFQLKISN HYYPENPMTK SAKIAGQHNP WENKWTKIYS
LLSLPPQ
