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Copper chaperone for superoxide dismutase (Superoxide dismutase copper chaperone)

 CCS_HUMAN               Reviewed;         274 AA.
O14618; Q2M366; Q8NEV0;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 170.
RecName: Full=Copper chaperone for superoxide dismutase;
AltName: Full=Superoxide dismutase copper chaperone;
Name=CCS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9295278; DOI=10.1074/jbc.272.38.23469;
Culotta V.C., Klomp L.W., Strain J., Casareno R.L.B., Krems B.,
Gitlin J.D.;
"The copper chaperone for superoxide dismutase.";
J. Biol. Chem. 272:23469-23472(1997).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[4]
STRUCTURE BY NMR OF 1-85, COPPER-BINDING SITES, AND SUBUNIT.
PubMed=23625804; DOI=10.1002/cbic.201300042;
Banci L., Cantini F., Kozyreva T., Rubino J.T.;
"Mechanistic aspects of hSOD1 maturation from the solution structure
of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1
mutants.";
ChemBioChem 14:1839-1844(2013).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Bhat K.S.;
"Human macrophage copper chaperone for superoxide dismutase (CCS),
full length mRNA sequence.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=9726962; DOI=10.1074/jbc.273.37.23625;
Casareno R.L.B., Waggoner D., Gitlin J.D.;
"The copper chaperone CCS directly interacts with copper/zinc
superoxide dismutase.";
J. Biol. Chem. 273:23625-23628(1998).
[9]
MUTAGENESIS OF CYS-22; CYS-25; CYS-244 AND CYS-246, AND METAL-BINDING.
PubMed=15736924; DOI=10.1021/bi0478392;
Stasser J.P., Eisses J.F., Barry A.N., Kaplan J.H., Blackburn N.J.;
"Cysteine-to-serine mutants of the human copper chaperone for
superoxide dismutase reveal a copper cluster at a domain III dimer
interface.";
Biochemistry 44:3143-3152(2005).
[10]
INTERACTION WITH COMMD1.
PubMed=20595380; DOI=10.1074/jbc.M110.101477;
Vonk W.I., Wijmenga C., Berger R., van de Sluis B., Klomp L.W.;
"Cu,Zn superoxide dismutase maturation and activity are regulated by
COMMD1.";
J. Biol. Chem. 285:28991-29000(2010).
[11]
UBIQUITINATION AT LYS-76; LYS-189; LYS-216 AND LYS-241 BY XIAP/BIRC4,
AND INTERACTION WITH XIAP/BIRC4.
PubMed=20154138; DOI=10.1128/MCB.00900-09;
Brady G.F., Galban S., Liu X., Basrur V., Gitlin J.D.,
Elenitoba-Johnson K.S., Wilson T.E., Duckett C.S.;
"Regulation of the copper chaperone CCS by XIAP-mediated
ubiquitination.";
Mol. Cell. Biol. 30:1923-1936(2010).
[12]
INTERACTION WITH SOD1, VARIANT TRP-163, AND CHARACTERIZATION OF
VARIANT TRP-163.
PubMed=22508683; DOI=10.1002/humu.22099;
Huppke P., Brendel C., Korenke G.C., Marquardt I., Donsante A., Yi L.,
Hicks J.D., Steinbach P.J., Wilson C., Elpeleg O., Moller L.B.,
Christodoulou J., Kaler S.G., Gartner J.;
"Molecular and biochemical characterization of a unique mutation in
CCS, the human copper chaperone to superoxide dismutase.";
Hum. Mutat. 33:1207-1215(2012).
[13]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 84-237 IN COMPLEX WITH ZINC,
SUBUNIT, AND DISULFIDE BOND.
PubMed=10677207; DOI=10.1021/bi992822i;
Lamb A.L., Wernimont A.K., Pufahl R.A., O'Halloran T.V.,
Rosenzweig A.C.;
"Crystal structure of the second domain of the human copper chaperone
for superoxide dismutase.";
Biochemistry 39:1589-1595(2000).
[14]
STRUCTURE BY NMR OF 1-87.
RIKEN structural genomics initiative (RSGI);
"The apo form of HMA domain of copper chaperone for superoxide
dismutase.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: Delivers copper to copper zinc superoxide dismutase
(SOD1).
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000244|PDB:2RSQ};
Note=Binds 2 copper ions per subunit. {ECO:0000244|PDB:2RSQ};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:10677207};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10677207};
-!- SUBUNIT: Homodimer, and heterodimer with SOD1. Interacts with
COMMD1. Interacts with XIAP/BIRC4. {ECO:0000269|PubMed:10677207,
ECO:0000269|PubMed:20154138, ECO:0000269|PubMed:20595380,
ECO:0000269|PubMed:22508683, ECO:0000269|PubMed:23625804,
ECO:0000269|PubMed:9726962}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9726962}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Ubiquitinion by XIAP/BIRC4 leads to enhancement of its
chaperone activity toward its physiologic target, SOD1, rather
than proteasomal degradation. XIAP/BIRC4 preferentially
ubiquitinates at Lys-241. {ECO:0000269|PubMed:20154138}.
-!- SIMILARITY: In the C-terminal section; belongs to the Cu-Zn
superoxide dismutase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF002210; AAC51764.1; -; mRNA.
EMBL; AY113179; AAM50090.1; -; mRNA.
EMBL; CR541928; CAG46726.1; -; mRNA.
EMBL; BC105016; AAI05017.1; -; mRNA.
EMBL; BC112055; AAI12056.1; -; mRNA.
CCDS; CCDS8146.1; -.
RefSeq; NP_005116.1; NM_005125.1.
UniGene; Hs.502917; -.
PDB; 1DO5; X-ray; 2.75 A; A/B/C/D=84-237.
PDB; 2CRL; NMR; -; A=1-85.
PDB; 2RSQ; NMR; -; A=1-85.
PDBsum; 1DO5; -.
PDBsum; 2CRL; -.
PDBsum; 2RSQ; -.
ProteinModelPortal; O14618; -.
SMR; O14618; -.
BioGrid; 115298; 18.
IntAct; O14618; 1.
MINT; MINT-153485; -.
STRING; 9606.ENSP00000436318; -.
iPTMnet; O14618; -.
PhosphoSitePlus; O14618; -.
SwissPalm; O14618; -.
BioMuta; CCS; -.
OGP; O14618; -.
EPD; O14618; -.
MaxQB; O14618; -.
PaxDb; O14618; -.
PeptideAtlas; O14618; -.
PRIDE; O14618; -.
DNASU; 9973; -.
Ensembl; ENST00000533244; ENSP00000436318; ENSG00000173992.
GeneID; 9973; -.
KEGG; hsa:9973; -.
UCSC; uc001oir.4; human.
CTD; 9973; -.
DisGeNET; 9973; -.
EuPathDB; HostDB:ENSG00000173992.8; -.
GeneCards; CCS; -.
HGNC; HGNC:1613; CCS.
HPA; CAB008672; -.
HPA; HPA040026; -.
HPA; HPA044090; -.
MIM; 603864; gene.
neXtProt; NX_O14618; -.
OpenTargets; ENSG00000173992; -.
PharmGKB; PA26177; -.
eggNOG; ENOG410IPMW; Eukaryota.
eggNOG; COG2032; LUCA.
GeneTree; ENSGT00530000063226; -.
HOGENOM; HOG000263450; -.
HOVERGEN; HBG018933; -.
InParanoid; O14618; -.
KO; K04569; -.
OMA; TQRPWSE; -.
OrthoDB; EOG091G0FQ1; -.
PhylomeDB; O14618; -.
TreeFam; TF105184; -.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
EvolutionaryTrace; O14618; -.
GeneWiki; CCS_(gene); -.
GenomeRNAi; 9973; -.
PRO; PR:O14618; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000173992; -.
CleanEx; HS_CCS; -.
ExpressionAtlas; O14618; baseline and differential.
Genevisible; O14618; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0005507; F:copper ion binding; IDA:GO_Central.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; TAS:Reactome.
GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0015680; P:intracellular copper ion transport; TAS:ProtInc.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; IEA:Ensembl.
GO; GO:0006801; P:superoxide metabolic process; TAS:ProtInc.
CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
CDD; cd00371; HMA; 1.
Gene3D; 2.60.40.200; -; 1.
InterPro; IPR006121; HMA_dom.
InterPro; IPR036163; HMA_dom_sf.
InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
InterPro; IPR018152; SOD_Cu/Zn_BS.
InterPro; IPR001424; SOD_Cu_Zn_dom.
PANTHER; PTHR10003; PTHR10003; 1.
Pfam; PF00403; HMA; 1.
Pfam; PF00080; Sod_Cu; 1.
PRINTS; PR00068; CUZNDISMTASE.
SUPFAM; SSF49329; SSF49329; 1.
SUPFAM; SSF55008; SSF55008; 1.
PROSITE; PS50846; HMA_2; 1.
PROSITE; PS00332; SOD_CU_ZN_2; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Complete proteome; Copper; Cytoplasm;
Disulfide bond; Isopeptide bond; Metal-binding; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation; Zinc.
CHAIN 1 274 Copper chaperone for superoxide
dismutase.
/FTId=PRO_0000213543.
DOMAIN 12 75 HMA. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
REGION 88 234 Superoxide dismutase-like.
METAL 22 22 Copper 1. {ECO:0000244|PDB:2RSQ}.
METAL 25 25 Copper 1. {ECO:0000244|PDB:2RSQ}.
METAL 147 147 Zinc. {ECO:0000244|PDB:1DO5,
ECO:0000255|PROSITE-ProRule:PRU00280,
ECO:0000269|PubMed:10677207}.
METAL 155 155 Zinc. {ECO:0000244|PDB:1DO5,
ECO:0000255|PROSITE-ProRule:PRU00280,
ECO:0000269|PubMed:10677207}.
METAL 164 164 Zinc. {ECO:0000244|PDB:1DO5,
ECO:0000255|PROSITE-ProRule:PRU00280,
ECO:0000269|PubMed:10677207}.
METAL 167 167 Zinc. {ECO:0000244|PDB:1DO5,
ECO:0000255|PROSITE-ProRule:PRU00280,
ECO:0000269|PubMed:10677207}.
METAL 244 244 Copper 2.
METAL 246 246 Copper 2.
MOD_RES 267 267 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
DISULFID 141 227 {ECO:0000244|PDB:1DO5,
ECO:0000269|PubMed:10677207}.
CROSSLNK 76 76 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:20154138}.
CROSSLNK 189 189 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:20154138}.
CROSSLNK 216 216 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:20154138}.
CROSSLNK 241 241 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:20154138}.
VARIANT 163 163 R -> W (found in a patient with
congenital cataracts, hearing loss,
neurodegeneration, neonatal hypotonia and
hypoglycemia, pericardial effusion and
neurodevelopmental regression after
infection; the patient also carries a
mutation in SLC33A1; mutant protein does
not interact with SOD1;
dbSNP:rs142340643).
{ECO:0000269|PubMed:22508683}.
/FTId=VAR_068078.
MUTAGEN 22 22 C->S: Reduces copper binding by half;
when associated with S-25. Negligible
effect on zinc binding.
{ECO:0000269|PubMed:15736924}.
MUTAGEN 25 25 C->S: Reduces copper binding by half;
when associated with S-22. Negligible
effect on zinc binding.
{ECO:0000269|PubMed:15736924}.
MUTAGEN 244 244 C->S: Reduces copper binding by half;
when associated with S-246. Negligible
effect on zinc binding.
{ECO:0000269|PubMed:15736924}.
MUTAGEN 246 246 C->S: Reduces copper binding by half;
when associated with S-244. Negligible
effect on zinc binding.
{ECO:0000269|PubMed:15736924}.
CONFLICT 116 116 E -> D (in Ref. 4; AAM50090).
{ECO:0000305}.
STRAND 12 18 {ECO:0000244|PDB:2CRL}.
HELIX 23 31 {ECO:0000244|PDB:2CRL}.
TURN 32 35 {ECO:0000244|PDB:2CRL}.
STRAND 41 45 {ECO:0000244|PDB:2CRL}.
TURN 46 49 {ECO:0000244|PDB:2CRL}.
STRAND 50 57 {ECO:0000244|PDB:2CRL}.
HELIX 59 67 {ECO:0000244|PDB:2CRL}.
TURN 68 70 {ECO:0000244|PDB:2CRL}.
STRAND 73 78 {ECO:0000244|PDB:2CRL}.
STRAND 87 94 {ECO:0000244|PDB:1DO5}.
STRAND 96 98 {ECO:0000244|PDB:1DO5}.
STRAND 100 109 {ECO:0000244|PDB:1DO5}.
STRAND 112 121 {ECO:0000244|PDB:1DO5}.
STRAND 124 133 {ECO:0000244|PDB:1DO5}.
HELIX 140 142 {ECO:0000244|PDB:1DO5}.
STRAND 161 163 {ECO:0000244|PDB:1DO5}.
STRAND 167 173 {ECO:0000244|PDB:1DO5}.
STRAND 177 187 {ECO:0000244|PDB:1DO5}.
HELIX 190 193 {ECO:0000244|PDB:1DO5}.
STRAND 196 203 {ECO:0000244|PDB:1DO5}.
TURN 213 220 {ECO:0000244|PDB:1DO5}.
STRAND 224 229 {ECO:0000244|PDB:1DO5}.
STRAND 231 233 {ECO:0000244|PDB:1DO5}.
SEQUENCE 274 AA; 29041 MW; A392432954B65760 CRC64;
MASDSGNQGT LCTLEFAVQM TCQSCVDAVR KSLQGVAGVQ DVEVHLEDQM VLVHTTLPSQ
EVQALLEGTG RQAVLKGMGS GQLQNLGAAV AILGGPGTVQ GVVRFLQLTP ERCLIEGTID
GLEPGLHGLH VHQYGDLTNN CNSCGNHFNP DGASHGGPQD SDRHRGDLGN VRADADGRAI
FRMEDEQLKV WDVIGRSLII DEGEDDLGRG GHPLSKITGN SGERLACGII ARSAGLFQNP
KQICSCDGLT IWEERGRPIA GKGRKESAQP PAHL


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