SODC_YEAST
ID SODC_YEAST Reviewed; 154 AA.
AC P00445; D6VWS3; Q68HB2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P85978};
GN Name=SOD1 {ECO:0000303|PubMed:11500508}; OrderedLocusNames=YJR104C;
GN ORFNames=J1968;
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=3290902; DOI=10.1073/pnas.85.13.4789;
RA Bermingham-Mcdonogh O., Gralla E., Valentine J.;
RT "The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae:
RT cloning, sequencing, and biological activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4789-4793(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ping Y.;
RT "Cloning and sequence analysis of copper, zinc-superoxide dismutase gene.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 PROTEIN SEQUENCE OF 2-154.
RA Johansen J.T., Overballe-Petersen C., Martin B., Hasemann V., Svendsen I.;
RT "The complete amino acid sequence of copper, zinc superoxide dismutase from
RT Saccharomyces cerevisiae.";
RL Carlsberg Res. Commun. 44:201-217(1979).
RN [7]
RP PROTEIN SEQUENCE OF 2-154.
RX PubMed=6993479; DOI=10.1016/s0021-9258(18)43637-x;
RA Steinman H.M.;
RT "The amino acid sequence of copper-zinc superoxide dismutase from bakers'
RT yeast.";
RL J. Biol. Chem. 255:6758-6765(1980).
RN [8]
RP PROTEIN SEQUENCE OF 2-11.
RC STRAIN=ATCC 26786 / X2180-1A;
RA Frutiger S., Hughes G.J., Sanchez J.-C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11500508; DOI=10.1074/jbc.m105296200;
RA Sturtz L.A., Diekert K., Jensen L.T., Lill R., Culotta V.C.;
RT "A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone,
RT CCS, localize to the intermembrane space of mitochondria. A physiological
RT role for SOD1 in guarding against mitochondrial oxidative damage.";
RL J. Biol. Chem. 276:38084-38089(2001).
RN [10]
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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-70, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=15166219; DOI=10.1074/jbc.m404173200;
RA Zhou W., Ryan J.J., Zhou H.;
RT "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.
RT Induction of protein sumoylation by cellular stresses.";
RL J. Biol. Chem. 279:32262-32268(2004).
RN [12]
RP MUTAGENESIS OF GLY-123; 131-ASP-THR-132; PRO-143 AND PRO-145.
RX PubMed=15069187; DOI=10.1073/pnas.0308298101;
RA Carroll M.C., Girouard J.B., Ulloa J.L., Subramaniam J.R., Wong P.C.,
RA Valentine J.S., Culotta V.C.;
RT "Mechanisms for activating Cu- and Zn-containing superoxide dismutase in
RT the absence of the CCS Cu chaperone.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5964-5969(2004).
RN [13]
RP MUTAGENESIS OF PRO-143 AND PRO-145.
RX PubMed=16234242; DOI=10.1074/jbc.m509142200;
RA Jensen L.T., Culotta V.C.;
RT "Activation of CuZn superoxide dismutases from Caenorhabditis elegans does
RT not require the copper chaperone CCS.";
RL J. Biol. Chem. 280:41373-41379(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-117 AND THR-132, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-39 AND SER-99, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-99 AND THR-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [18]
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 [19]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1772629; DOI=10.1107/s0108768191004949;
RA Djinovic K., Gatti G., Coda A., Antolini L., Pelosi G., Desideri A.,
RA Falconi M., Marmocchi F., Rotilio G., Bolognesi M.;
RT "Structure solution and molecular dynamics refinement of the yeast Cu,Zn
RT enzyme superoxide dismutase.";
RL Acta Crystallogr. B 47:918-927(1991).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1602482; DOI=10.1016/0022-2836(92)90401-5;
RA Djinovic K., Gatti G., Coda A., Antolini L., Pelosi G., Desideri A.,
RA Falconi M., Marmocchi F., Rotilio G., Bolognesi M.;
RT "Crystal structure of yeast Cu,Zn superoxide dismutase. Crystallographic
RT refinement at 2.5-A resolution.";
RL J. Mol. Biol. 225:791-809(1992).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC IONS.
RX PubMed=8652572; DOI=10.1021/bi951930b;
RA Ogihara N.L., Parge H.E., Hart P.J., Weiss M.S., Goto J.J., Crane B.R.,
RA Tsang J., Slater K., Roe J.A., Valentine J.S., Eisenberg D., Tainer J.A.;
RT "Unusual trigonal-planar copper configuration revealed in the atomic
RT structure of yeast copper-zinc superoxide dismutase.";
RL Biochemistry 35:2316-2321(1996).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG;
RP COPPER AND ZINC, AND DISULFIDE BONDS.
RX PubMed=10026301; DOI=10.1021/bi982284u;
RA Hart P.J., Balbirnie M.M., Ogihara N.L., Nersissian A.M., Weiss M.S.,
RA Valentine J.S., Eisenberg D.;
RT "A structure-based mechanism for copper-zinc superoxide dismutase.";
RL Biochemistry 38:2167-2178(1999).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH ZINC AND CCS1,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=11524675; DOI=10.1038/nsb0901-751;
RA Lamb A.L., Torres A.S., O'Halloran T.V., Rosenzweig A.C.;
RT "Heterodimeric structure of superoxide dismutase in complex with its
RT metallochaperone.";
RL Nat. Struct. Biol. 8:751-755(2001).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000250|UniProtKB:P00442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC Evidence={ECO:0000250|UniProtKB:P85978};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:8652572};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:10026301,
CC ECO:0000269|PubMed:8652572};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:11524675};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10026301,
CC ECO:0000269|PubMed:11524675};
CC -!- SUBUNIT: Homodimer in holo form. In apo form, heterodimer with CCS1.
CC Zinc-binding at 'His-16' of CCS1 and Glu-43 of apo-SOD1 is required for
CC this heterodimerization. {ECO:0000269|PubMed:10026301,
CC ECO:0000269|PubMed:11524675, ECO:0000269|PubMed:8652572}.
CC -!- INTERACTION:
CC P00445; P40202: CCS1; NbExp=2; IntAct=EBI-17635, EBI-10287;
CC P00445; P23291: YCK1; NbExp=2; IntAct=EBI-17635, EBI-4718;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11500508}.
CC Mitochondrion intermembrane space {ECO:0000269|PubMed:11500508,
CC ECO:0000269|PubMed:22984289}. Note=A small percentage (around 1-5
CC percent) localizes to the mitochondrial intermembrane space.
CC {ECO:0000269|PubMed:11500508}.
CC -!- MISCELLANEOUS: Present with 519000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; J03279; AAA34543.1; -; Genomic_DNA.
DR EMBL; AY690619; AAT99430.1; -; Genomic_DNA.
DR EMBL; Z49604; CAA89634.1; -; Genomic_DNA.
DR EMBL; AY558073; AAS56399.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08889.1; -; Genomic_DNA.
DR PIR; A36171; DSBYC.
DR RefSeq; NP_012638.1; NM_001181762.1.
DR PDB; 1B4L; X-ray; 1.80 A; A=2-154.
DR PDB; 1B4T; X-ray; 1.80 A; A=2-154.
DR PDB; 1F18; X-ray; 1.70 A; A=1-154.
DR PDB; 1F1A; X-ray; 1.80 A; A=1-154.
DR PDB; 1F1D; X-ray; 2.10 A; A=1-154.
DR PDB; 1F1G; X-ray; 1.35 A; A/B/C/D/E/F=1-154.
DR PDB; 1JCV; X-ray; 1.55 A; A=2-154.
DR PDB; 1JK9; X-ray; 2.90 A; A/C=2-154.
DR PDB; 1SDY; X-ray; 2.50 A; A/B/C/D=2-154.
DR PDB; 1YAZ; X-ray; 1.70 A; A=2-154.
DR PDB; 1YSO; X-ray; 1.73 A; A=2-154.
DR PDB; 2JCW; X-ray; 1.70 A; A=2-154.
DR PDBsum; 1B4L; -.
DR PDBsum; 1B4T; -.
DR PDBsum; 1F18; -.
DR PDBsum; 1F1A; -.
DR PDBsum; 1F1D; -.
DR PDBsum; 1F1G; -.
DR PDBsum; 1JCV; -.
DR PDBsum; 1JK9; -.
DR PDBsum; 1SDY; -.
DR PDBsum; 1YAZ; -.
DR PDBsum; 1YSO; -.
DR PDBsum; 2JCW; -.
DR AlphaFoldDB; P00445; -.
DR SMR; P00445; -.
DR BioGRID; 33860; 255.
DR ComplexPortal; CPX-2267; SOD1-CCS1 superoxide dismutase heterodimer.
DR ComplexPortal; CPX-2896; [Cu-Zn] Superoxide dismutase complex.
DR DIP; DIP-5859N; -.
DR IntAct; P00445; 13.
DR MINT; P00445; -.
DR STRING; 4932.YJR104C; -.
DR MoonProt; P00445; -.
DR iPTMnet; P00445; -.
DR SWISS-2DPAGE; P00445; -.
DR MaxQB; P00445; -.
DR PaxDb; P00445; -.
DR PRIDE; P00445; -.
DR TopDownProteomics; P00445; -.
DR EnsemblFungi; YJR104C_mRNA; YJR104C; YJR104C.
DR GeneID; 853568; -.
DR KEGG; sce:YJR104C; -.
DR SGD; S000003865; SOD1.
DR VEuPathDB; FungiDB:YJR104C; -.
DR eggNOG; KOG0441; Eukaryota.
DR GeneTree; ENSGT00940000168521; -.
DR HOGENOM; CLU_056632_4_2_1; -.
DR InParanoid; P00445; -.
DR OMA; AQRGFHI; -.
DR BioCyc; YEAST:MON3O-1629; -.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR Reactome; R-SCE-3299685; Detoxification of Reactive Oxygen Species.
DR EvolutionaryTrace; P00445; -.
DR PHI-base; PHI:2813; -.
DR PRO; PR:P00445; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P00445; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1902693; C:superoxide dismutase complex; IPI:ComplexPortal.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:SGD.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:SGD.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:1901856; P:negative regulation of cellular respiration; IMP:SGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:SGD.
DR GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:SGD.
DR GO; GO:0015680; P:protein maturation by copper ion transfer; IDA:ComplexPortal.
DR GO; GO:0050821; P:protein stabilization; IMP:SGD.
DR GO; GO:0019430; P:removal of superoxide radicals; IDA:ComplexPortal.
DR GO; GO:0006801; P:superoxide metabolic process; IMP:SGD.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Copper; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Isopeptide bond; Metal-binding; Mitochondrion;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6993479, ECO:0000269|Ref.6,
FT ECO:0000269|Ref.8"
FT CHAIN 2..154
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164129"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared with CCS1"
FT /note="in apo form"
FT /evidence="ECO:0000269|PubMed:10026301,
FT ECO:0000269|PubMed:11524675"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10026301,
FT ECO:0000269|PubMed:8652572"
FT BINDING 49
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10026301,
FT ECO:0000269|PubMed:8652572"
FT BINDING 64
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10026301,
FT ECO:0000269|PubMed:8652572"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:10026301,
FT ECO:0000269|PubMed:11524675"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:10026301,
FT ECO:0000269|PubMed:11524675"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:10026301,
FT ECO:0000269|PubMed:11524675"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:10026301,
FT ECO:0000269|PubMed:11524675"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10026301,
FT ECO:0000269|PubMed:8652572"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 132
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT DISULFID 58..147
FT DISULFID 58
FT /note="Interchain (with C-229 in CCS1); in linked form"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15166219"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15166219"
FT MUTAGEN 123
FT /note="G->K: Does not enable copper chaperone-independent
FT activation."
FT /evidence="ECO:0000269|PubMed:15069187"
FT MUTAGEN 131..132
FT /note="DT->GN: Does not enable copper chaperone-independent
FT activation."
FT /evidence="ECO:0000269|PubMed:15069187"
FT MUTAGEN 143
FT /note="P->A,S: Enables copper chaperone-independent
FT activation; when associated with A-145 or with L-145."
FT /evidence="ECO:0000269|PubMed:15069187,
FT ECO:0000269|PubMed:16234242"
FT MUTAGEN 145
FT /note="P->A,L: Enables copper chaperone-independent
FT activation; when associated with A-143 or with S-143."
FT /evidence="ECO:0000269|PubMed:15069187,
FT ECO:0000269|PubMed:16234242"
FT CONFLICT 56
FT /note="N -> D (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="N -> D (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1SDY"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1F1G"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:1F1G"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1F1G"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1F1G"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1F1G"
SQ SEQUENCE 154 AA; 15855 MW; E263A74679AF11F7 CRC64;
MVQAVAVLKG DAGVSGVVKF EQASESEPTT VSYEIAGNSP NAERGFHIHE FGDATNGCVS
AGPHFNPFKK THGAPTDEVR HVGDMGNVKT DENGVAKGSF KDSLIKLIGP TSVVGRSVVI
HAGQDDLGKG DTEESLKTGN AGPRPACGVI GLTN
