ATP5J_BOVIN
ID ATP5J_BOVIN Reviewed; 108 AA.
AC P02721; Q3ZBD6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=ATP synthase-coupling factor 6, mitochondrial {ECO:0000305};
DE Short=ATPase subunit F6;
DE AltName: Full=ATP synthase peripheral stalk subunit F6 {ECO:0000305};
DE Flags: Precursor;
GN Name=ATP5PF {ECO:0000250|UniProtKB:P18859}; Synonyms=ATP5J;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2894843; DOI=10.1021/bi00400a018;
RA Walker J.E., Gay N.J., Powell S.J., Kostina M., Dyer M.R.;
RT "ATP synthase from bovine mitochondria: sequences of imported precursors of
RT oligomycin sensitivity conferral protein, factor 6, and
RT adenosinetriphosphatase inhibitor protein.";
RL Biochemistry 26:8613-8619(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 33-108.
RX PubMed=6149548; DOI=10.1073/pnas.81.21.6603;
RA Fang J.-K., Jacobs J.W., Kanner B.I., Racker R., Bradshaw R.A.;
RT "Amino acid sequence of bovine heart coupling factor 6.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6603-6607(1984).
RN [4]
RP PROTEIN SEQUENCE OF 33-37.
RC TISSUE=Heart;
RX PubMed=1827992; DOI=10.1021/bi00236a007;
RA Walker J.E., Lutter R., Dupuis A., Runswick M.J.;
RT "Identification of the subunits of F1F0-ATPase from bovine heart
RT mitochondria.";
RL Biochemistry 30:5369-5378(1991).
RN [5]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=25851905; DOI=10.1074/jbc.m115.645283;
RA Lee J., Ding S., Walpole T.B., Holding A.N., Montgomery M.G.,
RA Fearnley I.M., Walker J.E.;
RT "Organization of Subunits in the Membrane Domain of the Bovine F-ATPase
RT Revealed by Covalent Cross-linking.";
RL J. Biol. Chem. 290:13308-13320(2015).
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 and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements. Also involved in the restoration of
CC oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(0) seems to have nine
CC subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP
CC synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
CC ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
CC ATP5PO, ATP5MG, ATP5MK and ATP5MJ. {ECO:0000269|PubMed:17570365,
CC ECO:0000269|PubMed:25851905}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase subunit F6 family.
CC {ECO:0000305}.
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DR EMBL; M19217; AAA30511.1; -; mRNA.
DR EMBL; BC103429; AAI03430.1; -; mRNA.
DR PIR; B27382; JLBO6.
DR RefSeq; NP_777142.1; NM_174717.3.
DR RefSeq; XP_005201201.1; XM_005201144.3.
DR RefSeq; XP_005201202.1; XM_005201145.3.
DR RefSeq; XP_005201203.1; XM_005201146.3.
DR RefSeq; XP_010799229.1; XM_010800927.1.
DR PDB; 1VZS; NMR; -; A=33-108.
DR PDB; 2CLY; X-ray; 2.80 A; C/F=32-108.
DR PDB; 2WSS; X-ray; 3.20 A; V/Z=33-108.
DR PDB; 4B2Q; EM; 37.00 A; V/v=36-101.
DR PDB; 5ARA; EM; 6.70 A; V=32-108.
DR PDB; 5ARE; EM; 7.40 A; V=32-108.
DR PDB; 5ARH; EM; 7.20 A; V=32-108.
DR PDB; 5ARI; EM; 7.40 A; V=32-108.
DR PDB; 5FIJ; EM; 7.40 A; V=32-108.
DR PDB; 5FIK; EM; 6.40 A; V=32-108.
DR PDB; 5FIL; EM; 7.10 A; V=32-108.
DR PDB; 6YY0; EM; 3.23 A; h=33-108.
DR PDB; 6Z1R; EM; 3.29 A; h=33-108.
DR PDB; 6Z1U; EM; 3.47 A; h=33-108.
DR PDB; 6ZIQ; EM; 4.33 A; h=33-108.
DR PDB; 6ZIT; EM; 3.49 A; h=33-108.
DR PDB; 6ZIU; EM; 6.02 A; h=33-108.
DR PDB; 6ZPO; EM; 4.00 A; h=33-108.
DR PDB; 6ZQM; EM; 3.29 A; h=33-108.
DR PDB; 6ZQN; EM; 4.00 A; h=33-108.
DR PDB; 7AJB; EM; 9.20 A; Ah/h=33-108.
DR PDB; 7AJC; EM; 11.90 A; Ah/h=33-108.
DR PDB; 7AJD; EM; 9.00 A; Ah/h=33-108.
DR PDB; 7AJE; EM; 9.40 A; Ah/h=33-108.
DR PDB; 7AJF; EM; 8.45 A; Ah/h=33-108.
DR PDB; 7AJG; EM; 10.70 A; Ah/h=33-108.
DR PDB; 7AJH; EM; 9.70 A; Ah/h=33-108.
DR PDB; 7AJI; EM; 11.40 A; Ah/h=33-108.
DR PDB; 7AJJ; EM; 13.10 A; Ah/h=33-108.
DR PDBsum; 1VZS; -.
DR PDBsum; 2CLY; -.
DR PDBsum; 2WSS; -.
DR PDBsum; 4B2Q; -.
DR PDBsum; 5ARA; -.
DR PDBsum; 5ARE; -.
DR PDBsum; 5ARH; -.
DR PDBsum; 5ARI; -.
DR PDBsum; 5FIJ; -.
DR PDBsum; 5FIK; -.
DR PDBsum; 5FIL; -.
DR PDBsum; 6YY0; -.
DR PDBsum; 6Z1R; -.
DR PDBsum; 6Z1U; -.
DR PDBsum; 6ZIQ; -.
DR PDBsum; 6ZIT; -.
DR PDBsum; 6ZIU; -.
DR PDBsum; 6ZPO; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; P02721; -.
DR BMRB; P02721; -.
DR SMR; P02721; -.
DR CORUM; P02721; -.
DR DIP; DIP-39023N; -.
DR IntAct; P02721; 2.
DR MINT; P02721; -.
DR STRING; 9913.ENSBTAP00000032359; -.
DR PaxDb; P02721; -.
DR PeptideAtlas; P02721; -.
DR PRIDE; P02721; -.
DR Ensembl; ENSBTAT00000066011; ENSBTAP00000054675; ENSBTAG00000000605.
DR GeneID; 282690; -.
DR KEGG; bta:282690; -.
DR CTD; 522; -.
DR VEuPathDB; HostDB:ENSBTAG00000000605; -.
DR VGNC; VGNC:26304; ATP5PF.
DR eggNOG; KOG4634; Eukaryota.
DR GeneTree; ENSGT00390000008902; -.
DR HOGENOM; CLU_145649_1_0_1; -.
DR InParanoid; P02721; -.
DR OrthoDB; 328455at32523; -.
DR TreeFam; TF318998; -.
DR EvolutionaryTrace; P02721; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000000605; Expressed in oocyte and 104 other tissues.
DR ExpressionAtlas; P02721; baseline and differential.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA: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 DisProt; DP00201; -.
DR Gene3D; 1.10.246.110; -; 1.
DR InterPro; IPR008387; ATP_synth_f6_mt.
DR InterPro; IPR036204; ATP_synth_f6_sf_mt.
DR PANTHER; PTHR12441; PTHR12441; 1.
DR Pfam; PF05511; ATP-synt_F6; 1.
DR PIRSF; PIRSF002455; ATP_synthase_coupling_factor_6; 1.
DR SUPFAM; SSF111357; SSF111357; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1827992,
FT ECO:0000269|PubMed:6149548"
FT CHAIN 33..108
FT /note="ATP synthase-coupling factor 6, mitochondrial"
FT /id="PRO_0000002526"
FT MOD_RES 41
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 84
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 84
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 99
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 99
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97450"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18859"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21571"
FT CONFLICT 94
FT /note="T -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:2CLY"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:2CLY"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2CLY"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:2CLY"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1VZS"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1VZS"
SQ SEQUENCE 108 AA; 12532 MW; E5376A0518C3E1C8 CRC64;
MILQRLFRLS SAVQSAISVS WRRNIGITAV AFNKELDPVQ KLFVDKIREY RTKRQTSGGP
VDAGPEYQQD LDRELFKLKQ MYGKADMNTF PNFTFEDPKF EVVEKPQS
