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ATP5I_BOVIN
ID   ATP5I_BOVIN             Reviewed;          71 AA.
AC   Q00361; Q3T0S4;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000305};
DE            Short=ATPase subunit e;
DE   AltName: Full=ATP synthase membrane subunit e {ECO:0000305};
GN   Name=ATP5ME {ECO:0000250|UniProtKB:P56385}; Synonyms=ATP5I;
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], AND PROTEIN SEQUENCE OF 2-36.
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   [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   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
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. 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   -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR   EMBL; M64751; AAA30390.1; -; mRNA.
DR   EMBL; BC102279; AAI02280.1; -; mRNA.
DR   PIR; A39566; A39566.
DR   RefSeq; NP_788812.1; NM_176639.2.
DR   PDB; 6ZBB; EM; 3.61 A; e=2-71.
DR   PDB; 6ZIQ; EM; 4.33 A; e=2-71.
DR   PDB; 6ZIT; EM; 3.49 A; e=2-71.
DR   PDB; 6ZIU; EM; 6.02 A; e=2-71.
DR   PDB; 6ZPO; EM; 4.00 A; e=2-71.
DR   PDB; 6ZQM; EM; 3.29 A; e=2-71.
DR   PDB; 6ZQN; EM; 4.00 A; e=2-71.
DR   PDB; 7AJB; EM; 9.20 A; Ae/e=2-71.
DR   PDB; 7AJC; EM; 11.90 A; Ae/e=2-71.
DR   PDB; 7AJD; EM; 9.00 A; Ae/e=2-71.
DR   PDB; 7AJE; EM; 9.40 A; Ae/e=2-71.
DR   PDB; 7AJF; EM; 8.45 A; Ae/e=2-71.
DR   PDB; 7AJG; EM; 10.70 A; Ae/e=2-71.
DR   PDB; 7AJH; EM; 9.70 A; Ae/e=2-71.
DR   PDB; 7AJI; EM; 11.40 A; Ae/e=2-71.
DR   PDB; 7AJJ; EM; 13.10 A; Ae/e=2-71.
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; Q00361; -.
DR   SMR; Q00361; -.
DR   CORUM; Q00361; -.
DR   IntAct; Q00361; 3.
DR   MINT; Q00361; -.
DR   STRING; 9913.ENSBTAP00000023255; -.
DR   PaxDb; Q00361; -.
DR   PeptideAtlas; Q00361; -.
DR   PRIDE; Q00361; -.
DR   Ensembl; ENSBTAT00000023255; ENSBTAP00000023255; ENSBTAG00000017496.
DR   GeneID; 338040; -.
DR   KEGG; bta:338040; -.
DR   CTD; 521; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017496; -.
DR   VGNC; VGNC:104569; ATP5ME.
DR   eggNOG; KOG4326; Eukaryota.
DR   GeneTree; ENSGT00390000005102; -.
DR   HOGENOM; CLU_180903_0_0_1; -.
DR   InParanoid; Q00361; -.
DR   OMA; GAFHQNR; -.
DR   OrthoDB; 1640426at2759; -.
DR   TreeFam; TF314719; -.
DR   Reactome; R-BTA-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-BTA-8949613; Cristae formation.
DR   Proteomes; UP000009136; Chromosome 6.
DR   Bgee; ENSBTAG00000017496; Expressed in tongue muscle and 106 other tissues.
DR   ExpressionAtlas; Q00361; baseline.
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   InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR   PANTHER; PTHR12427; PTHR12427; 1.
DR   Pfam; PF05680; ATP-synt_E; 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; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1827992"
FT   CHAIN           2..71
FT                   /note="ATP synthase subunit e, mitochondrial"
FT                   /id="PRO_0000071682"
FT   MOD_RES         34
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06185"
FT   HELIX           9..42
FT                   /evidence="ECO:0007829|PDB:6ZIT"
SQ   SEQUENCE   71 AA;  8321 MW;  18E63DB09EF1A132 CRC64;
     MVPPVQVSPL IKLGRYSALF LGMAYGAKRY NYLKPRAEEE RRLAAEEKKK RDEQKRIERE
     LAEAQEDTIL K
 
 
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