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CYC7_YEAST
ID   CYC7_YEAST              Reviewed;         113 AA.
AC   P00045; D3DLL0;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 209.
DE   RecName: Full=Cytochrome c isoform 2;
DE            Short=Iso-2-cytochrome c;
DE   AltName: Full=Cytochrome c hypoxic isoform;
GN   Name=CYC7; Synonyms=CYP3; OrderedLocusNames=YEL039C;
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].
RX   PubMed=6244566; DOI=10.1073/pnas.77.1.541;
RA   Montgomery D.L., Leung D.W., Smith M., Shalit P., Faye G., Hall B.D.;
RT   "Isolation and sequence of the gene for iso-2-cytochrome c in Saccharomyces
RT   cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:541-545(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B-6441;
RX   PubMed=8411151; DOI=10.1006/jmbi.1993.1518;
RA   Melnick L., Sherman F.;
RT   "The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of
RT   Saccharomyces cerevisiae share a common ancestry.";
RL   J. Mol. Biol. 233:372-388(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [4]
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   [5]
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   [6]
RP   FUNCTION.
RX   PubMed=7814361; DOI=10.1074/jbc.270.1.110;
RA   Allen L.A., Zhao X.J., Caughey W., Poyton R.O.;
RT   "Isoforms of yeast cytochrome c oxidase subunit V affect the binuclear
RT   reaction center and alter the kinetics of interaction with the isoforms of
RT   yeast cytochrome c.";
RL   J. Biol. Chem. 270:110-118(1995).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8636074; DOI=10.1074/jbc.271.12.6708;
RA   Wang X., Dumont M.E., Sherman F.;
RT   "Sequence requirements for mitochondrial import of yeast cytochrome c.";
RL   J. Biol. Chem. 271:6594-6604(1996).
RN   [8]
RP   INDUCTION.
RX   PubMed=9169434; DOI=10.1074/jbc.272.23.14705;
RA   Burke P.V., Raitt D.C., Allen L.A., Kellogg E.A., Poyton R.O.;
RT   "Effects of oxygen concentration on the expression of cytochrome c and
RT   cytochrome c oxidase genes in yeast.";
RL   J. Biol. Chem. 272:14705-14712(1997).
RN   [9]
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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA   Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA   Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT   "Intermembrane space proteome of yeast mitochondria.";
RL   Mol. Cell. Proteomics 11:1840-1852(2012).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH HEME.
RX   PubMed=1326054; DOI=10.1016/0022-2836(92)90689-h;
RA   Murphy M.E.P., Nall B.T., Brayer G.D.;
RT   "Structure determination and analysis of yeast iso-2-cytochrome c and a
RT   composite mutant protein.";
RL   J. Mol. Biol. 227:160-176(1992).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH HEME.
RX   PubMed=18390544; DOI=10.1074/jbc.m710126200;
RA   Solmaz S.R., Hunte C.;
RT   "Structure of complex III with bound cytochrome c in reduced state and
RT   definition of a minimal core interface for electron transfer.";
RL   J. Biol. Chem. 283:17542-17549(2008).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC       c heme group can accept an electron from the heme group of the
CC       cytochrome c1 subunit of ubiquinol-cytochrome c oxidoreductase.
CC       Cytochrome c then transfers this electron to the dinuclear copper A
CC       center (CU(A)) of the COX2 subunit of cytochrome oxidase, the final
CC       protein carrier in the mitochondrial electron-transport chain. Isoform
CC       2 (CYC7) is the predominant cytochrome c under anaerobic/hypoxic
CC       conditions. {ECO:0000269|PubMed:7814361, ECO:0000269|PubMed:9169434}.
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000269|PubMed:18390544};
CC       Note=Binds 1 heme c group covalently per subunit.
CC       {ECO:0000269|PubMed:18390544};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:8636074}.
CC   -!- INDUCTION: By low oxygen levels (hypoxia) at the level of
CC       transcription. Not expressed until the oxygen concentration is below
CC       0.5 uM O(2). {ECO:0000269|PubMed:9169434}.
CC   -!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC       November 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/076";
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DR   EMBL; S65964; AAD13974.1; -; Genomic_DNA.
DR   EMBL; V01299; CAA24606.1; -; Genomic_DNA.
DR   EMBL; L22173; AAA34940.1; -; Genomic_DNA.
DR   EMBL; J01320; AAB59339.1; -; Genomic_DNA.
DR   EMBL; U18779; AAB65003.1; -; Genomic_DNA.
DR   EMBL; AY693032; AAT93051.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07614.1; -; Genomic_DNA.
DR   PIR; A00038; CCBYBC.
DR   RefSeq; NP_010875.1; NM_001178854.1.
DR   PDB; 1YEA; X-ray; 1.90 A; A=2-113.
DR   PDB; 1YEB; X-ray; 1.95 A; A=6-111.
DR   PDB; 1YTC; X-ray; 1.80 A; A=2-113.
DR   PDB; 3CXH; X-ray; 2.50 A; W=2-113.
DR   PDBsum; 1YEA; -.
DR   PDBsum; 1YEB; -.
DR   PDBsum; 1YTC; -.
DR   PDBsum; 3CXH; -.
DR   AlphaFoldDB; P00045; -.
DR   BMRB; P00045; -.
DR   SMR; P00045; -.
DR   BioGRID; 36690; 25.
DR   DIP; DIP-7178N; -.
DR   IntAct; P00045; 2.
DR   MINT; P00045; -.
DR   STRING; 4932.YEL039C; -.
DR   MaxQB; P00045; -.
DR   PaxDb; P00045; -.
DR   PRIDE; P00045; -.
DR   EnsemblFungi; YEL039C_mRNA; YEL039C; YEL039C.
DR   GeneID; 856672; -.
DR   KEGG; sce:YEL039C; -.
DR   SGD; S000000765; CYC7.
DR   VEuPathDB; FungiDB:YEL039C; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   GeneTree; ENSGT00940000168884; -.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   InParanoid; P00045; -.
DR   OMA; YSDAMKN; -.
DR   BioCyc; YEAST:G3O-30160-MON; -.
DR   Reactome; R-SCE-111457; Release of apoptotic factors from the mitochondria.
DR   Reactome; R-SCE-3299685; Detoxification of Reactive Oxygen Species.
DR   Reactome; R-SCE-5620971; Pyroptosis.
DR   Reactome; R-SCE-611105; Respiratory electron transport.
DR   EvolutionaryTrace; P00045; -.
DR   PRO; PR:P00045; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P00045; protein.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IDA:SGD.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IDA:SGD.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IDA:SGD.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Reference proteome; Respiratory chain; Transport.
FT   CHAIN           1..113
FT                   /note="Cytochrome c isoform 2"
FT                   /id="PRO_0000108338"
FT   BINDING         24
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:1326054,
FT                   ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA,
FT                   ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH"
FT   BINDING         27
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:1326054,
FT                   ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA,
FT                   ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH"
FT   BINDING         28
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:1326054,
FT                   ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA,
FT                   ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH"
FT   BINDING         90
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:1326054,
FT                   ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA,
FT                   ECO:0007744|PDB:1YEB"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:1YTC"
FT   HELIX           13..23
FT                   /evidence="ECO:0007829|PDB:1YTC"
FT   TURN            24..27
FT                   /evidence="ECO:0007829|PDB:1YTC"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:1YTC"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:1YEA"
FT   HELIX           60..65
FT                   /evidence="ECO:0007829|PDB:1YTC"
FT   HELIX           71..79
FT                   /evidence="ECO:0007829|PDB:1YTC"
FT   HELIX           81..84
FT                   /evidence="ECO:0007829|PDB:1YTC"
FT   HELIX           98..111
FT                   /evidence="ECO:0007829|PDB:1YTC"
SQ   SEQUENCE   113 AA;  12532 MW;  50CBD0F95B480CB7 CRC64;
     MAKESTGFKP GSAKKGATLF KTRCQQCHTI EEGGPNKVGP NLHGIFGRHS GQVKGYSYTD
     ANINKNVKWD EDSMSEYLTN PKKYIPGTKM AFAGLKKEKD RNDLITYMTK AAK
 
 
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