ATP8_PIG
ID ATP8_PIG Reviewed; 67 AA.
AC Q35914; O79877; O99387;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 134.
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 Sus scrofa (Pig).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9732457; DOI=10.1007/pl00006388;
RA Ursing B.M., Arnason U.;
RT "The complete mitochondrial DNA sequence of the pig (Sus scrofa).";
RL J. Mol. Evol. 47:302-306(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Peripheral blood;
RX PubMed=9734874; DOI=10.2527/1998.7682207x;
RA Tartaglia M., Saulle E.;
RT "Rapid communication: nucleotide sequence of porcine and ovine tRNA(Lys)
RT and ATPase8 mitochondrial genes.";
RL J. Anim. Sci. 76:2207-2208(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Landrace;
RX PubMed=10433971; DOI=10.1016/s0378-1119(99)00247-4;
RA Lin C.S., Sun Y.L., Liu C.Y., Yang P.C., Chang L.C., Cheng I.C.,
RA Mao S.J.T., Huang M.C.;
RT "Complete nucleotide sequence of pig (Sus scrofa) mitochondrial genome and
RT dating evolutionary divergence within artiodactyla.";
RL Gene 236:107-114(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-67.
RX PubMed=3017295; DOI=10.1007/bf00499094;
RA Watanabe T., Hayashi Y., Kimura J., Yasuda Y., Saitou N., Tomita T.,
RA Ogasawara N.;
RT "Pig mitochondrial DNA: polymorphism, restriction map orientation, and
RT sequence data.";
RL Biochem. Genet. 24:385-396(1986).
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; AJ002189; CAA05233.1; -; Genomic_DNA.
DR EMBL; AF039170; AAD05064.1; -; Genomic_DNA.
DR EMBL; AF034253; AAD34189.1; -; Genomic_DNA.
DR EMBL; M26139; AAA32030.1; -; Genomic_DNA.
DR PIR; T10976; T10976.
DR RefSeq; NP_008638.1; NC_000845.1.
DR PDB; 6J54; EM; 3.94 A; 8=5-34.
DR PDB; 6J5A; EM; 4.35 A; 8=5-34.
DR PDB; 6J5I; EM; 3.34 A; 8=1-67.
DR PDB; 6J5J; EM; 3.45 A; 8=1-67.
DR PDB; 6J5K; EM; 6.20 A; 8/A8/B8/C8=1-67.
DR PDB; 6ZMR; EM; 3.94 A; 8=1-67.
DR PDB; 6ZNA; EM; 6.20 A; 8/A8/B8/C8=1-67.
DR PDBsum; 6J54; -.
DR PDBsum; 6J5A; -.
DR PDBsum; 6J5I; -.
DR PDBsum; 6J5J; -.
DR PDBsum; 6J5K; -.
DR PDBsum; 6ZMR; -.
DR PDBsum; 6ZNA; -.
DR AlphaFoldDB; Q35914; -.
DR SMR; Q35914; -.
DR IntAct; Q35914; 1.
DR STRING; 9823.ENSSSCP00000019139; -.
DR PaxDb; Q35914; -.
DR PeptideAtlas; Q35914; -.
DR PRIDE; Q35914; -.
DR Ensembl; ENSSSCT00000019675; ENSSSCP00000019139; ENSSSCG00000018080.
DR Ensembl; ENSSSCT00070061677; ENSSSCP00070052582; ENSSSCG00070030640.
DR GeneID; 808505; -.
DR KEGG; ssc:808505; -.
DR CTD; 4509; -.
DR VGNC; VGNC:99789; MT-ATP8.
DR eggNOG; ENOG502T21P; Eukaryota.
DR GeneTree; ENSGT00390000008771; -.
DR HOGENOM; CLU_2811757_0_0_1; -.
DR InParanoid; Q35914; -.
DR OMA; LDTSTWF; -.
DR OrthoDB; 1621322at2759; -.
DR TreeFam; TF343854; -.
DR Reactome; R-SSC-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SSC-8949613; Cristae formation.
DR Proteomes; UP000008227; Mitochondrion.
DR Proteomes; UP000314985; Mitochondrion.
DR Bgee; ENSSSCG00000018080; Expressed in Ammon's horn and 45 other tissues.
DR ExpressionAtlas; Q35914; baseline and differential.
DR Genevisible; Q35914; SS.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; CF(0); Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..67
FT /note="ATP synthase protein 8"
FT /id="PRO_0000195570"
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 CONFLICT 40
FT /note="I -> T (in Ref. 2; AAD05064)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="Q -> S (in Ref. 4; AAA32030)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="L -> S (in Ref. 2; AAD05064)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="P -> L (in Ref. 2; AAD05064)"
FT /evidence="ECO:0000305"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:6J5I"
SQ SEQUENCE 67 AA; 7947 MW; 2890AA68B5CDD48E CRC64;
MPQLDTSTWF ITITSMIMTL FILFQLKISN YSYPASPESI ELKTQKHSTP WEMKWTKIYL
PLLLPPR
