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 27-MAR-2024, entry version 215.
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; 26.
DR DIP; DIP-7178N; -.
DR IntAct; P00045; 2.
DR MINT; P00045; -.
DR STRING; 4932.YEL039C; -.
DR MaxQB; P00045; -.
DR PaxDb; 4932-YEL039C; -.
DR PeptideAtlas; P00045; -.
DR EnsemblFungi; YEL039C_mRNA; YEL039C; YEL039C.
DR GeneID; 856672; -.
DR KEGG; sce:YEL039C; -.
DR AGR; SGD:S000000765; -.
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; MPAPYKK; -.
DR OrthoDB; 4150at2759; -.
DR BioCyc; YEAST:G3O-30160-MONOMER; -.
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 BioGRID-ORCS; 856672; 0 hits in 10 CRISPR screens.
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; Cytochrome c-like domain; 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; CYTOCHROME C; 1.
DR PANTHER; PTHR11961:SF12; CYTOCHROME C; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; Cytochrome c; 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
//
