ATPK_BOVIN
ID ATPK_BOVIN Reviewed; 88 AA.
AC Q28851; Q32P94;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ATP synthase subunit f, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase membrane subunit f {ECO:0000305};
GN Name=ATP5MF {ECO:0000250|UniProtKB:P56134}; Synonyms=ATP5J2;
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], PROTEIN SEQUENCE OF 2-88, AND MASS
RP SPECTROMETRY.
RC TISSUE=Heart;
RX PubMed=8011660; DOI=10.1021/bi00191a026;
RA Collinson I.R., Runswick M.J., Buchanan S.K., Fearnley I.M., Skehel J.M.,
RA van Raaij M.J., Griffiths D.E., Walker J.E.;
RT "F0 membrane domain of ATP synthase from bovine heart mitochondria:
RT purification, subunit composition, and reconstitution with F1-ATPase.";
RL Biochemistry 33:7971-7978(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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. Minor subunit located with subunit a in the membrane.
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 {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=10209.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8011660};
CC -!- SIMILARITY: Belongs to the ATPase F chain family. {ECO:0000305}.
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DR EMBL; S70447; AAB31107.2; -; mRNA.
DR EMBL; BC108208; AAI08209.1; -; mRNA.
DR PIR; A54211; A54211.
DR RefSeq; NP_001107191.1; NM_001113719.2.
DR PDB; 6ZBB; EM; 3.61 A; f=2-88.
DR PDB; 6ZIQ; EM; 4.33 A; f=2-88.
DR PDB; 6ZIT; EM; 3.49 A; f=2-88.
DR PDB; 6ZIU; EM; 6.02 A; f=2-88.
DR PDB; 6ZPO; EM; 4.00 A; f=2-88.
DR PDB; 6ZQM; EM; 3.29 A; f=2-88.
DR PDB; 6ZQN; EM; 4.00 A; f=2-88.
DR PDB; 7AJB; EM; 9.20 A; Af/f=2-88.
DR PDB; 7AJC; EM; 11.90 A; Af/f=2-88.
DR PDB; 7AJD; EM; 9.00 A; Af/f=2-88.
DR PDB; 7AJE; EM; 9.40 A; Af/f=2-88.
DR PDB; 7AJF; EM; 8.45 A; Af/f=2-88.
DR PDB; 7AJG; EM; 10.70 A; Af/f=2-88.
DR PDB; 7AJH; EM; 9.70 A; Af/f=2-88.
DR PDB; 7AJI; EM; 11.40 A; Af/f=2-88.
DR PDB; 7AJJ; EM; 13.10 A; Af/f=2-88.
DR PDBsum; 6ZBB; -.
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; Q28851; -.
DR SMR; Q28851; -.
DR IntAct; Q28851; 1.
DR MINT; Q28851; -.
DR STRING; 9913.ENSBTAP00000041308; -.
DR PaxDb; Q28851; -.
DR PeptideAtlas; Q28851; -.
DR PRIDE; Q28851; -.
DR Ensembl; ENSBTAT00000043764; ENSBTAP00000041308; ENSBTAG00000002094.
DR GeneID; 506492; -.
DR KEGG; bta:506492; -.
DR CTD; 9551; -.
DR VEuPathDB; HostDB:ENSBTAG00000002094; -.
DR VGNC; VGNC:26305; ATP5MF.
DR eggNOG; KOG4092; Eukaryota.
DR GeneTree; ENSGT00510000046986; -.
DR HOGENOM; CLU_169781_0_0_1; -.
DR InParanoid; Q28851; -.
DR OMA; HKYVQPK; -.
DR OrthoDB; 1479342at2759; -.
DR TreeFam; TF342865; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000002094; Expressed in tongue muscle and 107 other tissues.
DR ExpressionAtlas; Q28851; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR InterPro; IPR019344; F1F0-ATPsyn_F_prd.
DR PANTHER; PTHR13080; PTHR13080; 1.
DR Pfam; PF10206; WRW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P56134,
FT ECO:0000269|PubMed:8011660"
FT CHAIN 2..88
FT /note="ATP synthase subunit f, mitochondrial"
FT /id="PRO_0000194823"
FT TRANSMEM 55..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P56134"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZAF6"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56135"
FT CONFLICT 42
FT /note="Y -> N (in Ref. 2; AAI08209)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="L -> H (in Ref. 2; AAI08209)"
FT /evidence="ECO:0000305"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:6ZIT"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 31..49
FT /evidence="ECO:0007829|PDB:6ZIT"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 58..80
FT /evidence="ECO:0007829|PDB:6ZIT"
SQ SEQUENCE 88 AA; 10297 MW; AC5D4BF93F53277B CRC64;
MASVVPLKEK KLLEVKLGEL PSWILMRDFT PSGIAGAFQR GYYRYYNKYV NVKKGSIAGL
SMVLAAYVFL NYCRSYKELK HERLRKYH
