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ATP18_YEAST
ID   ATP18_YEAST             Reviewed;          59 AA.
AC   P81450; D6W0K1;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=ATP synthase subunit J, mitochondrial;
DE   AltName: Full=ATPase synthase I subunit;
GN   Name=ATP18; OrderedLocusNames=YML081C-A; ORFNames=YML081BC;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15,
RP   IDENTIFICATION, AND MASS SPECTROMETRY.
RC   STRAIN=ATCC 24657 / D273-10B;
RX   PubMed=9867878; DOI=10.1074/jbc.274.1.543;
RA   Vaillier J., Arselin G., Graves P.-V., Camougrand N., Velours J.;
RT   "Isolation of supernumerary yeast ATP synthase subunits e and i.
RT   Characterization of subunit i and disruption of its structural gene
RT   ATP18.";
RL   J. Biol. Chem. 274:543-548(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-13, AND IDENTIFICATION.
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=9867807; DOI=10.1074/jbc.274.1.36;
RA   Arnold I., Pfeiffer K., Neupert W., Stuart R.A., Schaegger H.;
RT   "ATP synthase of yeast mitochondria. Isolation of subunit j and disruption
RT   of the ATP18 gene.";
RL   J. Biol. Chem. 274:36-40(1999).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16823961; DOI=10.1021/pr050477f;
RA   Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT   "Toward the complete yeast mitochondrial proteome: multidimensional
RT   separation techniques for mitochondrial proteomics.";
RL   J. Proteome Res. 5:1543-1554(2006).
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. In yeast, the dimeric form
CC       of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta,
CC       epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j
CC       and k.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000269|PubMed:16823961}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:16823961}.
CC   -!- MASS SPECTROMETRY: Mass=6687.1; Mass_error=2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9867878};
CC   -!- MISCELLANEOUS: Present with 6540 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ATPase j subunit family. {ECO:0000305}.
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DR   EMBL; AF073791; AAD02949.1; -; Genomic_DNA.
DR   EMBL; Z46660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY558537; AAS56863.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09815.1; -; Genomic_DNA.
DR   PIR; S78730; S78730.
DR   RefSeq; NP_013629.1; NM_001184340.1.
DR   PDB; 6B2Z; EM; 3.60 A; S/i=1-59.
DR   PDB; 6B8H; EM; 3.60 A; i/w=1-59.
DR   PDB; 6CP3; EM; 3.80 A; J=1-37.
DR   PDB; 6CP5; EM; 4.20 A; J=1-37.
DR   PDB; 6CP6; EM; 3.60 A; J=1-37.
DR   PDB; 6CP7; EM; 4.10 A; J=1-37.
DR   PDB; 6WTD; EM; 4.20 A; J=1-37.
DR   PDBsum; 6B2Z; -.
DR   PDBsum; 6B8H; -.
DR   PDBsum; 6CP3; -.
DR   PDBsum; 6CP5; -.
DR   PDBsum; 6CP6; -.
DR   PDBsum; 6CP7; -.
DR   PDBsum; 6WTD; -.
DR   AlphaFoldDB; P81450; -.
DR   SMR; P81450; -.
DR   BioGRID; 35059; 356.
DR   ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR   DIP; DIP-3034N; -.
DR   IntAct; P81450; 7.
DR   STRING; 4932.YML081C-A; -.
DR   TCDB; 8.A.73.2.4; the mitochondrial atp synthase stress-responsive protein (masp) family.
DR   iPTMnet; P81450; -.
DR   MaxQB; P81450; -.
DR   PaxDb; P81450; -.
DR   PRIDE; P81450; -.
DR   TopDownProteomics; P81450; -.
DR   EnsemblFungi; YML081C-A_mRNA; YML081C-A; YML081C-A.
DR   GeneID; 854893; -.
DR   KEGG; sce:YML081C-A; -.
DR   SGD; S000007247; ATP18.
DR   VEuPathDB; FungiDB:YML081C-A; -.
DR   eggNOG; ENOG502SC94; Eukaryota.
DR   HOGENOM; CLU_174950_0_0_1; -.
DR   InParanoid; P81450; -.
DR   OMA; KFPAQIA; -.
DR   BioCyc; YEAST:G3O-33009-MON; -.
DR   PRO; PR:P81450; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P81450; protein.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:SGD.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IMP:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IMP:SGD.
DR   GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:SGD.
DR   InterPro; IPR006995; ATP_synth_F0_jsu.
DR   PANTHER; PTHR28060; PTHR28060; 1.
DR   Pfam; PF04911; ATP-synt_J; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; CF(0); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..59
FT                   /note="ATP synthase subunit J, mitochondrial"
FT                   /id="PRO_0000071697"
FT   TRANSMEM        9..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   59 AA;  6688 MW;  F0D7D450C4810025 CRC64;
     MLKRFPTPIL KVYWPFFVAG AAVYYGMSKA ADLSSNTKEF INDPRNPRFA KGGKFVEVD
 
 
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