ATP6_PIG
ID ATP6_PIG Reviewed; 226 AA.
AC Q35915; O79878;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
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 [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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
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. Key component of the
CC proton channel; it may play a direct role in the translocation of
CC protons across the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ (By similarity). Interacts with DNAJC30; interaction is direct
CC (By similarity). {ECO:0000250|UniProtKB:P00846,
CC ECO:0000250|UniProtKB:P00847}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR EMBL; AJ002189; CAA05234.1; -; Genomic_DNA.
DR EMBL; AF034253; AAD34190.1; -; Genomic_DNA.
DR EMBL; M26139; AAA32031.1; -; Genomic_DNA.
DR PIR; T10977; T10977.
DR RefSeq; NP_008639.1; NC_000845.1.
DR PDB; 6J54; EM; 3.94 A; a=1-226.
DR PDB; 6J5A; EM; 4.35 A; a=1-226.
DR PDB; 6J5I; EM; 3.34 A; a=1-226.
DR PDB; 6J5J; EM; 3.45 A; a=1-226.
DR PDB; 6J5K; EM; 6.20 A; Aa/Ba/Ca/a=1-226.
DR PDB; 6ZMR; EM; 3.94 A; a=1-226.
DR PDB; 6ZNA; EM; 6.20 A; Aa/Ba/Ca/a=1-226.
DR PDBsum; 6J54; -.
DR PDBsum; 6J5A; -.
DR PDBsum; 6J5I; -.
DR PDBsum; 6J5J; -.
DR PDBsum; 6J5K; -.
DR PDBsum; 6ZMR; -.
DR PDBsum; 6ZNA; -.
DR AlphaFoldDB; Q35915; -.
DR SMR; Q35915; -.
DR IntAct; Q35915; 2.
DR STRING; 9823.ENSSSCP00000019140; -.
DR PaxDb; Q35915; -.
DR PeptideAtlas; Q35915; -.
DR Ensembl; ENSSSCT00000019676; ENSSSCP00000019140; ENSSSCG00000018081.
DR Ensembl; ENSSSCT00070061678; ENSSSCP00070052583; ENSSSCG00070030641.
DR GeneID; 808506; -.
DR KEGG; ssc:808506; -.
DR CTD; 4508; -.
DR VGNC; VGNC:108745; MT-ATP6.
DR eggNOG; KOG4665; Eukaryota.
DR GeneTree; ENSGT00390000005568; -.
DR HOGENOM; CLU_041018_0_2_1; -.
DR InParanoid; Q35915; -.
DR OMA; FFDQFMS; -.
DR OrthoDB; 1095315at2759; -.
DR TreeFam; TF343395; -.
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; ENSSSCG00000018081; Expressed in prefrontal cortex and 44 other tissues.
DR ExpressionAtlas; Q35915; baseline and differential.
DR Genevisible; Q35915; 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:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.20.120.220; -; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..226
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082154"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 30..37
FT /note="LFPTPKRL -> SLYLHDNT (in Ref. 3; AAA32031)"
FT /evidence="ECO:0000305"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 57..61
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 139..150
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 151..179
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 207..221
FT /evidence="ECO:0007829|PDB:6J5I"
SQ SEQUENCE 226 AA; 25039 MW; BE197F3B086FEEA2 CRC64;
MNENLFASFI APTMMGLPIV TLIIMFPSLL FPTPKRLINN RTISIQQWLI QLTSKQMMAI
HNQKGQTWSL MLMSLIMFIG STNILGLLPH SFTPTTQLSM NLGMAIPLWS ATVFTGFRYK
TKTSLAHFLP QGTPALLIPM LVIIETISLF IQPVALAVRL TANITAGHLL IHLIGGATLA
LLNINTMTAF ITFTILILLT ILEFAVALIQ AYVFTLLVSL YLHDNT
