ATP8_CANLU
ID ATP8_CANLU Reviewed; 67 AA.
AC Q3L6Z3; Q1HK99; Q1HKB2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 (Gray wolf).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9612;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15964215; DOI=10.1016/j.ympev.2005.04.025;
RA Delisle I., Strobeck C.;
RT "A phylogeny of the Caniformia (order Carnivora) based on 12 complete
RT protein-coding mitochondrial genes.";
RL Mol. Phylogenet. Evol. 37:192-201(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-41; THR-42 AND LYS-49.
RX PubMed=16809672; DOI=10.1101/gr.5117706;
RA Bjornerfeldt S., Webster M.T., Vila C.;
RT "Relaxation of selective constraint on dog mitochondrial DNA following
RT domestication.";
RL Genome Res. 16:990-994(2006).
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; AY598495; AAU00441.1; -; Genomic_DNA.
DR EMBL; DQ480503; ABE48159.1; -; Genomic_DNA.
DR EMBL; DQ480504; ABE48172.1; -; Genomic_DNA.
DR EMBL; DQ480505; ABE48185.1; -; Genomic_DNA.
DR EMBL; DQ480506; ABE48198.1; -; Genomic_DNA.
DR EMBL; DQ480507; ABE48211.1; -; Genomic_DNA.
DR EMBL; DQ480508; ABE48224.1; -; Genomic_DNA.
DR RefSeq; YP_626732.1; NC_008092.1.
DR AlphaFoldDB; Q3L6Z3; -.
DR SMR; Q3L6Z3; -.
DR GeneID; 4097768; -.
DR CTD; 4509; -.
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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..67
FT /note="ATP synthase protein 8"
FT /id="PRO_0000269707"
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"
FT VARIANT 41
FT /note="S -> P"
FT /evidence="ECO:0000269|PubMed:16809672"
FT VARIANT 42
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:16809672"
FT VARIANT 49
FT /note="N -> K"
FT /evidence="ECO:0000269|PubMed:16809672"
SQ SEQUENCE 67 AA; 7978 MW; 3B313377275A0AC6 CRC64;
MPQLDTSTWF IMIFSMFLTL FILFQLKISN HYYPENPMTK SAKIAGQHNP WENKWTKIYS
LLSLPPQ
