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Copper chaperone for superoxide dismutase (Superoxide dismutase copper chaperone)

 CCS_MOUSE               Reviewed;         274 AA.
Q9WU84; Q9CRJ9;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 153.
RecName: Full=Copper chaperone for superoxide dismutase;
AltName: Full=Superoxide dismutase copper chaperone;
Name=Ccs; Synonyms=Ccsd;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=10694572; DOI=10.1073/pnas.040461197;
Wong P.C., Waggoner D., Subramaniam J.R., Tessarollo L.,
Bartnikas T.B., Culotta V.C., Price D.L., Rothstein J., Gitlin J.D.;
"Copper chaperone for superoxide dismutase is essential to activate
mammalian Cu/Zn superoxide dismutase.";
Proc. Natl. Acad. Sci. U.S.A. 97:2886-2891(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=NOD; TISSUE=Brain;
PubMed=10773661;
Moore S.D., Chen M.M., Cox D.W.;
"Cloning and mapping of murine superoxide dismutase copper chaperone
(Ccsd) and mapping of the human ortholog.";
Cytogenet. Cell Genet. 88:35-37(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-274.
STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Delivers copper to copper zinc superoxide dismutase
(SOD1).
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000250|UniProtKB:O14618};
Note=Binds 2 copper ions per subunit.
{ECO:0000250|UniProtKB:O14618};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:O14618};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O14618};
-!- SUBUNIT: Homodimer, and heterodimer with SOD1. Interacts with
COMMD1 (By similarity). Interacts with XIAP/BIRC4 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SIMILARITY: In the C-terminal section; belongs to the Cu-Zn
superoxide dismutase family. {ECO:0000305}.
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EMBL; AF121906; AAD23832.1; -; mRNA.
EMBL; AF173379; AAF70242.1; -; mRNA.
EMBL; AK010264; BAB26806.1; -; mRNA.
EMBL; BC026938; AAH26938.1; -; mRNA.
CCDS; CCDS29438.1; -.
RefSeq; NP_058588.1; NM_016892.3.
UniGene; Mm.434411; -.
ProteinModelPortal; Q9WU84; -.
SMR; Q9WU84; -.
BioGrid; 198563; 2.
DIP; DIP-48692N; -.
IntAct; Q9WU84; 2.
STRING; 10090.ENSMUSP00000035486; -.
iPTMnet; Q9WU84; -.
PhosphoSitePlus; Q9WU84; -.
SwissPalm; Q9WU84; -.
EPD; Q9WU84; -.
MaxQB; Q9WU84; -.
PaxDb; Q9WU84; -.
PRIDE; Q9WU84; -.
Ensembl; ENSMUST00000037246; ENSMUSP00000035486; ENSMUSG00000034108.
GeneID; 12460; -.
KEGG; mmu:12460; -.
UCSC; uc008gba.1; mouse.
CTD; 9973; -.
MGI; MGI:1333783; Ccs.
eggNOG; ENOG410IPMW; Eukaryota.
eggNOG; COG2032; LUCA.
GeneTree; ENSGT00530000063226; -.
HOGENOM; HOG000263450; -.
HOVERGEN; HBG018933; -.
InParanoid; Q9WU84; -.
KO; K04569; -.
OMA; GVTLWEE; -.
OrthoDB; EOG091G0FQ1; -.
PhylomeDB; Q9WU84; -.
TreeFam; TF105184; -.
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:Q9WU84; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000034108; Expressed in 265 organ(s), highest expression level in membranous labyrinth.
CleanEx; MM_CCS; -.
ExpressionAtlas; Q9WU84; baseline and differential.
Genevisible; Q9WU84; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005507; F:copper ion binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0004784; F:superoxide dismutase activity; IEA:InterPro.
GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0030001; P:metal ion transport; IEA:InterPro.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; IMP:MGI.
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;
Chaperone; Complete proteome; Copper; Cytoplasm; Disulfide bond;
Isopeptide bond; Metal-binding; Phosphoprotein; Reference proteome;
Ubl conjugation; Zinc.
CHAIN 1 274 Copper chaperone for superoxide
dismutase.
/FTId=PRO_0000213544.
DOMAIN 12 75 HMA. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
REGION 88 234 Superoxide dismutase-like.
METAL 22 22 Copper 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 25 25 Copper 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 147 147 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 155 155 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 164 164 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 167 167 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 244 244 Copper 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 246 246 Copper 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
MOD_RES 267 267 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
DISULFID 141 227 {ECO:0000250}.
CROSSLNK 76 76 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O14618}.
CROSSLNK 189 189 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O14618}.
CROSSLNK 216 216 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O14618}.
CROSSLNK 241 241 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O14618}.
SEQUENCE 274 AA; 28912 MW; 19DCE48376C9D5A2 CRC64;
MASKSGDGGT VCALEFAVQM SCQSCVDAVH KTLKGVAGVQ NVDVQLENQM VLVQTTLPSQ
EVQALLESTG RQAVLKGMGS SQLQNLGAAV AILEGCGSIQ GVVRFLQLSS ELCLIEGTID
GLEPGLHGLH VHQYGDLTRD CNSCGDHFNP DGASHGGPQD TDRHRGDLGN VRAEAGGRAT
FRIEDKQLKV WDVIGRSLVI DEGEDDLGRG GHPLSKITGN SGKRLACGII ARSAGLFQNP
KQICSCDGLT IWEERGRPIA GQGRKDSAQP PAHL


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