CCS1_YEAST
ID CCS1_YEAST Reviewed; 249 AA.
AC P40202; D6VZL3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Superoxide dismutase 1 copper chaperone;
GN Name=CCS1; Synonyms=LYS7; OrderedLocusNames=YMR038C; ORFNames=YM9532.03C;
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=7557423; DOI=10.1016/0378-1119(95)00325-z;
RA Horecka J., Kinsey P.T., Sprague G.F. Jr.;
RT "Cloning and characterization of the Saccharomyces cerevisiae LYS7 gene:
RT evidence for function outside of lysine biosynthesis.";
RL Gene 162:87-92(1995).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9295278; DOI=10.1074/jbc.272.38.23469;
RA Culotta V.C., Klomp L.W., Strain J., Casareno R.L.B., Krems B.,
RA Gitlin J.D.;
RT "The copper chaperone for superoxide dismutase.";
RL J. Biol. Chem. 272:23469-23472(1997).
RN [6]
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 [7]
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 [8]
RP SUBUNIT.
RX PubMed=11101286; DOI=10.1021/bi002207a;
RA Lamb A.L., Torres A.S., O'Halloran T.V., Rosenzweig A.C.;
RT "Heterodimer formation between superoxide dismutase and its copper
RT chaperone.";
RL Biochemistry 39:14720-14727(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
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 (1.80 ANGSTROMS) OF 2-223, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=10426947; DOI=10.1038/11489;
RA Lamb A.L., Wernimont A.K., Pufahl R.A., Culotta V.C., O'Halloran T.V.,
RA Rosenzweig A.C.;
RT "Crystal structure of the copper chaperone for superoxide dismutase.";
RL Nat. Struct. Biol. 6:724-729(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 78-217, AND SUBUNIT.
RX PubMed=10736160; DOI=10.1021/bi992716g;
RA Hall L.T., Sanchez R.J., Holloway S.P., Zhu H., Stine J.E., Lyons T.J.,
RA Demeler B., Schirf V., Hansen J.C., Nersissian A.M., Valentine J.S.,
RA Hart P.J.;
RT "X-ray crystallographic and analytical ultracentrifugation analyses of
RT truncated and full-length yeast copper chaperones for SOD (LYS7): a dimer-
RT dimer model of LYS7-SOD association and copper delivery.";
RL Biochemistry 39:3611-3623(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH ZINC AND SOD1,
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: Copper chaperone for apo superoxide dismutase 1 (SOD1). Binds
CC copper ions and delivers them specifically to apo-SOD1.
CC {ECO:0000269|PubMed:9295278}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00280};
CC Note=Binds 2 copper ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00280};
CC -!- SUBUNIT: Homodimer, and heterodimer with apo-SOD1. Zinc-binding at His-
CC 16 of CCS1 and 'Glu-43' of apo-SOD1 is required for this
CC heterodimerization. {ECO:0000269|PubMed:10426947,
CC ECO:0000269|PubMed:10736160, ECO:0000269|PubMed:11101286,
CC ECO:0000269|PubMed:11524675}.
CC -!- INTERACTION:
CC P40202; P00445: SOD1; NbExp=2; IntAct=EBI-10287, EBI-17635;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289}. Note=A small percentage (around 1-5
CC percent) localizes to the mitochondrial intermembrane space.
CC -!- MISCELLANEOUS: Present with 12000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CCS1 family. {ECO:0000305}.
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DR EMBL; U17378; AAC49068.1; -; Genomic_DNA.
DR EMBL; Z48502; CAA88404.1; -; Genomic_DNA.
DR EMBL; AY558398; AAS56724.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09937.1; -; Genomic_DNA.
DR PIR; S50245; S50245.
DR RefSeq; NP_013752.1; NM_001182535.1.
DR PDB; 1EJ8; X-ray; 1.55 A; A=78-217.
DR PDB; 1JK9; X-ray; 2.90 A; B/D=1-249.
DR PDB; 1QUP; X-ray; 1.80 A; A/B=2-223.
DR PDB; 5U9M; X-ray; 2.35 A; B/D=2-249.
DR PDBsum; 1EJ8; -.
DR PDBsum; 1JK9; -.
DR PDBsum; 1QUP; -.
DR PDBsum; 5U9M; -.
DR AlphaFoldDB; P40202; -.
DR SMR; P40202; -.
DR BioGRID; 35210; 189.
DR ComplexPortal; CPX-2267; SOD1-CCS1 superoxide dismutase heterodimer.
DR ComplexPortal; CPX-2895; Superoxide dismutase 1 copper chaperone.
DR DIP; DIP-4507N; -.
DR IntAct; P40202; 2.
DR MINT; P40202; -.
DR STRING; 4932.YMR038C; -.
DR iPTMnet; P40202; -.
DR MaxQB; P40202; -.
DR PaxDb; P40202; -.
DR PRIDE; P40202; -.
DR EnsemblFungi; YMR038C_mRNA; YMR038C; YMR038C.
DR GeneID; 855054; -.
DR KEGG; sce:YMR038C; -.
DR SGD; S000004641; CCS1.
DR VEuPathDB; FungiDB:YMR038C; -.
DR eggNOG; KOG4656; Eukaryota.
DR GeneTree; ENSGT00940000159785; -.
DR HOGENOM; CLU_056632_0_0_1; -.
DR InParanoid; P40202; -.
DR OMA; KGMGSDQ; -.
DR BioCyc; YEAST:G3O-32743-MON; -.
DR Reactome; R-SCE-3299685; Detoxification of Reactive Oxygen Species.
DR EvolutionaryTrace; P40202; -.
DR PRO; PR:P40202; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40202; protein.
DR GO; GO:0101031; C:chaperone complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
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:0016532; F:superoxide dismutase copper chaperone activity; IMP:SGD.
DR GO; GO:0006825; P:copper ion transport; IDA:ComplexPortal.
DR GO; GO:0015680; P:protein maturation by copper ion transfer; IDA:ComplexPortal.
DR GO; GO:0019430; P:removal of superoxide radicals; IDA:ComplexPortal.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00403; HMA; 1.
DR SUPFAM; SSF49329; SSF49329; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW Mitochondrion; Reference proteome; Zinc.
FT CHAIN 1..249
FT /note="Superoxide dismutase 1 copper chaperone"
FT /id="PRO_0000213542"
FT DOMAIN 6..69
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared with apo-SOD1"
FT /evidence="ECO:0000269|PubMed:11524675,
FT ECO:0007744|PDB:1JK9"
FT BINDING 17
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 20
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 229
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT BINDING 231
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT DISULFID 27..64
FT /evidence="ECO:0000269|PubMed:7557423,
FT ECO:0007744|PDB:1QUP"
FT DISULFID 229
FT /note="Interchain (with C-58 in apo-SOD1)"
FT /evidence="ECO:0000269|PubMed:24374639,
FT ECO:0007744|PDB:1JK9"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1QUP"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:1QUP"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1JK9"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:1QUP"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1QUP"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:1QUP"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:1QUP"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:1QUP"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1QUP"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1EJ8"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:1EJ8"
FT STRAND 113..125
FT /evidence="ECO:0007829|PDB:1EJ8"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:1EJ8"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:1EJ8"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1EJ8"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1EJ8"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1EJ8"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:1EJ8"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:1EJ8"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1EJ8"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:1EJ8"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:1EJ8"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1EJ8"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1JK9"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:1EJ8"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1QUP"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:5U9M"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:5U9M"
SQ SEQUENCE 249 AA; 27330 MW; 81DB7E728CDF9366 CRC64;
MTTNDTYEAT YAIPMHCENC VNDIKACLKN VPGINSLNFD IEQQIMSVES SVAPSTIINT
LRNCGKDAII RGAGKPNSSA VAILETFQKY TIDQKKDTAV RGLARIVQVG ENKTLFDITV
NGVPEAGNYH ASIHEKGDVS KGVESTGKVW HKFDEPIECF NESDLGKNLY SGKTFLSAPL
PTWQLIGRSF VISKSLNHPE NEPSSVKDYS FLGVIARSAG VWENNKQVCA CTGKTVWEER
KDALANNIK
