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Database: UniProt
Entry: CCS1_YEAST
LinkDB: CCS1_YEAST
Original site: 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   13-FEB-2019, entry version 180.
DE   RecName: Full=Superoxide dismutase 1 copper chaperone;
GN   Name=CCS1; Synonyms=LYS7; OrderedLocusNames=YMR038C;
GN   ORFNames=YM9532.03C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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
RT   gene: 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.,
RA   Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA   Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding 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
RT   metallochaperone, CCS, localize to the intermembrane space of
RT   mitochondria. A physiological role for SOD1 in guarding against
RT   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.,
RA   Dephoure N., 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
RP   SCALE 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
RP   DISULFIDE 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.,
RA   Lyons T.J., Demeler B., Schirf V., Hansen J.C., Nersissian A.M.,
RA   Valentine J.S., Hart P.J.;
RT   "X-ray crystallographic and analytical ultracentrifugation analyses of
RT   truncated and full-length yeast copper chaperones for SOD (LYS7): a
RT   dimer-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).
CC       Binds 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
CC       His-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       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}.
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   ProteinModelPortal; P40202; -.
DR   SMR; P40202; -.
DR   BioGrid; 35210; 183.
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_mRNA; YMR038C.
DR   GeneID; 855054; -.
DR   KEGG; sce:YMR038C; -.
DR   EuPathDB; FungiDB:YMR038C; -.
DR   SGD; S000004641; CCS1.
DR   GeneTree; ENSGT00940000159785; -.
DR   HOGENOM; HOG000263450; -.
DR   InParanoid; P40202; -.
DR   KO; K04569; -.
DR   OMA; QDSDRHR; -.
DR   BioCyc; YEAST:G3O-32743-MONOMER; -.
DR   EvolutionaryTrace; P40202; -.
DR   PRO; PR:P40202; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IMP:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR   GO; GO:0015680; P:protein maturation by copper ion transfer; IMP:SGD.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00080; Sod_Cu; 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; Complete proteome; Copper; Cytoplasm;
KW   Disulfide bond; Metal-binding; Mitochondrion; Reference proteome;
KW   Zinc.
FT   CHAIN         1    249       Superoxide dismutase 1 copper chaperone.
FT                                /FTId=PRO_0000213542.
FT   DOMAIN        7     70       HMA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL        16     16       Zinc; shared with apo-SOD1.
FT                                {ECO:0000244|PDB:1JK9,
FT                                ECO:0000255|PROSITE-ProRule:PRU00280,
FT                                ECO:0000269|PubMed:11524675}.
FT   METAL        17     17       Copper 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL        20     20       Copper 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       229    229       Copper 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       231    231       Copper 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   DISULFID     27     64       {ECO:0000244|PDB:1QUP,
FT                                ECO:0000269|PubMed:7557423}.
FT   DISULFID    229    229       Interchain (with C-58 in apo-SOD1).
FT                                {ECO:0000244|PDB:1JK9,
FT                                ECO:0000269|PubMed:24374639}.
FT   HELIX         3      5       {ECO:0000244|PDB:1QUP}.
FT   STRAND        7     12       {ECO:0000244|PDB:1QUP}.
FT   STRAND       17     19       {ECO:0000244|PDB:1JK9}.
FT   HELIX        20     28       {ECO:0000244|PDB:1QUP}.
FT   STRAND       34     40       {ECO:0000244|PDB:1QUP}.
FT   TURN         41     44       {ECO:0000244|PDB:1QUP}.
FT   STRAND       45     52       {ECO:0000244|PDB:1QUP}.
FT   HELIX        54     63       {ECO:0000244|PDB:1QUP}.
FT   STRAND       69     71       {ECO:0000244|PDB:1QUP}.
FT   STRAND       79     85       {ECO:0000244|PDB:1EJ8}.
FT   STRAND      100    110       {ECO:0000244|PDB:1EJ8}.
FT   STRAND      113    125       {ECO:0000244|PDB:1EJ8}.
FT   STRAND      127    135       {ECO:0000244|PDB:1EJ8}.
FT   HELIX       142    145       {ECO:0000244|PDB:1EJ8}.
FT   STRAND      148    152       {ECO:0000244|PDB:1EJ8}.
FT   STRAND      157    159       {ECO:0000244|PDB:1EJ8}.
FT   STRAND      161    164       {ECO:0000244|PDB:1EJ8}.
FT   TURN        165    168       {ECO:0000244|PDB:1EJ8}.
FT   STRAND      169    179       {ECO:0000244|PDB:1EJ8}.
FT   HELIX       182    184       {ECO:0000244|PDB:1EJ8}.
FT   TURN        185    187       {ECO:0000244|PDB:1EJ8}.
FT   STRAND      188    195       {ECO:0000244|PDB:1EJ8}.
FT   HELIX       199    201       {ECO:0000244|PDB:1EJ8}.
FT   STRAND      202    205       {ECO:0000244|PDB:1JK9}.
FT   STRAND      208    214       {ECO:0000244|PDB:1EJ8}.
FT   STRAND      216    218       {ECO:0000244|PDB:1QUP}.
FT   STRAND      227    229       {ECO:0000244|PDB:5U9M}.
FT   STRAND      235    238       {ECO:0000244|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
//
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