AT5F1_BOVIN
ID AT5F1_BOVIN Reviewed; 256 AA.
AC P13619; Q2TBH4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=ATP synthase F(0) complex subunit B1, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase peripheral stalk-membrane subunit b {ECO:0000305};
DE AltName: Full=ATP synthase subunit b;
DE Short=ATPase subunit b;
DE Flags: Precursor;
GN Name=ATP5PB {ECO:0000250|UniProtKB:P24539}; Synonyms=ATP5F, ATP5F1;
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 [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 43-256, AND PROTEIN SEQUENCE OF 43-256.
RX PubMed=2890767; DOI=10.1016/0022-2836(87)90611-5;
RA Walker J.E., Runswick M.J., Poulter L.;
RT "ATP synthase from bovine mitochondria. The characterization and sequence
RT analysis of two membrane-associated sub-units and of the corresponding
RT cDNAs.";
RL J. Mol. Biol. 197:89-100(1987).
RN [3]
RP PROTEIN SEQUENCE OF 43-53.
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 [4]
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 [5]
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
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the 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.
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. {ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:25851905}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC110212; AAI10213.1; -; mRNA.
DR EMBL; X06088; CAA29472.1; -; mRNA.
DR PIR; S00763; S00763.
DR RefSeq; NP_001033590.1; NM_001038501.2.
DR PDB; 2CLY; X-ray; 2.80 A; A/D=43-256.
DR PDB; 2WSS; X-ray; 3.20 A; T/X=141-256.
DR PDB; 4B2Q; EM; 37.00 A; T/t=121-249.
DR PDB; 5ARA; EM; 6.70 A; T=76-249.
DR PDB; 5ARE; EM; 7.40 A; T=76-249.
DR PDB; 5ARH; EM; 7.20 A; T=76-249.
DR PDB; 5ARI; EM; 7.40 A; T=76-249.
DR PDB; 5FIJ; EM; 7.40 A; T=76-249.
DR PDB; 5FIK; EM; 6.40 A; T=76-249.
DR PDB; 5FIL; EM; 7.10 A; T=76-249.
DR PDB; 6YY0; EM; 3.23 A; b=43-256.
DR PDB; 6Z1R; EM; 3.29 A; b=43-256.
DR PDB; 6Z1U; EM; 3.47 A; b=43-256.
DR PDB; 6ZBB; EM; 3.61 A; b=43-256.
DR PDB; 6ZIQ; EM; 4.33 A; b=43-256.
DR PDB; 6ZIT; EM; 3.49 A; b=43-256.
DR PDB; 6ZIU; EM; 6.02 A; b=43-256.
DR PDB; 6ZPO; EM; 4.00 A; b=43-256.
DR PDB; 6ZQM; EM; 3.29 A; b=43-256.
DR PDB; 6ZQN; EM; 4.00 A; b=43-256.
DR PDB; 7AJB; EM; 9.20 A; Ab/b=43-256.
DR PDB; 7AJC; EM; 11.90 A; Ab/b=43-256.
DR PDB; 7AJD; EM; 9.00 A; Ab/b=43-256.
DR PDB; 7AJE; EM; 9.40 A; Ab/b=43-256.
DR PDB; 7AJF; EM; 8.45 A; Ab/b=43-256.
DR PDB; 7AJG; EM; 10.70 A; Ab/b=43-256.
DR PDB; 7AJH; EM; 9.70 A; Ab/b=43-256.
DR PDB; 7AJI; EM; 11.40 A; Ab/b=43-256.
DR PDB; 7AJJ; EM; 13.10 A; Ab/b=43-256.
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; 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; P13619; -.
DR SMR; P13619; -.
DR CORUM; P13619; -.
DR DIP; DIP-38983N; -.
DR IntAct; P13619; 17.
DR MINT; P13619; -.
DR STRING; 9913.ENSBTAP00000008447; -.
DR PaxDb; P13619; -.
DR PeptideAtlas; P13619; -.
DR PRIDE; P13619; -.
DR Ensembl; ENSBTAT00000008447; ENSBTAP00000008447; ENSBTAG00000006441.
DR GeneID; 282701; -.
DR KEGG; bta:282701; -.
DR CTD; 515; -.
DR VEuPathDB; HostDB:ENSBTAG00000006441; -.
DR VGNC; VGNC:26303; ATP5PB.
DR eggNOG; KOG3976; Eukaryota.
DR GeneTree; ENSGT00390000001958; -.
DR HOGENOM; CLU_087186_1_0_1; -.
DR InParanoid; P13619; -.
DR OMA; HMVNWIV; -.
DR OrthoDB; 1314411at2759; -.
DR TreeFam; TF313250; -.
DR EvolutionaryTrace; P13619; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000006441; Expressed in cardiac ventricle and 105 other tissues.
DR ExpressionAtlas; P13619; 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); IBA:GO_Central.
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 InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR InterPro; IPR013837; ATP_synth_F0_suB.
DR PANTHER; PTHR12733; PTHR12733; 1.
DR Pfam; PF05405; Mt_ATP-synt_B; 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; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1827992,
FT ECO:0000269|PubMed:2890767"
FT CHAIN 43..256
FT /note="ATP synthase F(0) complex subunit B1, mitochondrial"
FT /id="PRO_0000071671"
FT MOD_RES 131
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT MOD_RES 162
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT MOD_RES 221
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24539"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24539"
FT MOD_RES 244
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT CONFLICT 53
FT /note="K -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 122..159
FT /evidence="ECO:0007829|PDB:2CLY"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2CLY"
FT HELIX 164..223
FT /evidence="ECO:0007829|PDB:2CLY"
FT HELIX 232..250
FT /evidence="ECO:0007829|PDB:6YY0"
SQ SEQUENCE 256 AA; 28822 MW; 5766369D254B3D9A CRC64;
MLSRVVLSAA AAAAPSLKNA ALLGPGVLQA TRIFHTGQPS LAPVPPLPEH GGKVRFGLIP
EEFFQFLYPK TGVTGPYVLG TGLILYLLSK EIYVITPETF SAISTIGFLV YIVKKYGASV
GEFADKLNEQ KIAQLEEVKQ ASIKQIQDAI DMEKSQQALV QKRHYLFDVQ RNNIAMALEV
TYRERLHRVY REVKNRLDYH ISVQNMMRQK EQEHMINWVE KRVVQSISAQ QEKETIAKCI
ADLKLLSKKA QAQPVM
