CCS_MOUSE
ID CCS_MOUSE Reviewed; 274 AA.
AC Q9WU84; Q9CRJ9;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Copper chaperone for superoxide dismutase;
DE AltName: Full=Superoxide dismutase copper chaperone;
GN Name=Ccs; Synonyms=Ccsd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10694572; DOI=10.1073/pnas.040461197;
RA Wong P.C., Waggoner D., Subramaniam J.R., Tessarollo L., Bartnikas T.B.,
RA Culotta V.C., Price D.L., Rothstein J., Gitlin J.D.;
RT "Copper chaperone for superoxide dismutase is essential to activate
RT mammalian Cu/Zn superoxide dismutase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2886-2891(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NOD; TISSUE=Brain;
RX PubMed=10773661; DOI=10.1159/000015480;
RA Moore S.D., Chen M.M., Cox D.W.;
RT "Cloning and mapping of murine superoxide dismutase copper chaperone (Ccsd)
RT and mapping of the human ortholog.";
RL Cytogenet. Cell Genet. 88:35-37(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-274.
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Delivers copper to copper zinc superoxide dismutase (SOD1).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:O14618};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:O14618};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O14618};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O14618};
CC -!- SUBUNIT: Homodimer, and heterodimer with SOD1. Interacts with COMMD1
CC (By similarity). Interacts with XIAP/BIRC4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Ubiquitinion by XIAP/BIRC4 leads to enhancement of its chaperone
CC activity toward its physiologic target, SOD1, rather than proteasomal
CC degradation. XIAP/BIRC4 preferentially ubiquitinates at Lys-241 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the Cu-Zn superoxide
CC dismutase family. {ECO:0000305}.
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DR EMBL; AF121906; AAD23832.1; -; mRNA.
DR EMBL; AF173379; AAF70242.1; -; mRNA.
DR EMBL; AK010264; BAB26806.1; -; mRNA.
DR EMBL; BC026938; AAH26938.1; -; mRNA.
DR CCDS; CCDS29438.1; -.
DR RefSeq; NP_058588.1; NM_016892.3.
DR AlphaFoldDB; Q9WU84; -.
DR SMR; Q9WU84; -.
DR BioGRID; 198563; 4.
DR DIP; DIP-48692N; -.
DR IntAct; Q9WU84; 3.
DR MINT; Q9WU84; -.
DR STRING; 10090.ENSMUSP00000035486; -.
DR iPTMnet; Q9WU84; -.
DR PhosphoSitePlus; Q9WU84; -.
DR SwissPalm; Q9WU84; -.
DR EPD; Q9WU84; -.
DR jPOST; Q9WU84; -.
DR MaxQB; Q9WU84; -.
DR PaxDb; Q9WU84; -.
DR PRIDE; Q9WU84; -.
DR ProteomicsDB; 281257; -.
DR Antibodypedia; 30210; 375 antibodies from 32 providers.
DR DNASU; 12460; -.
DR Ensembl; ENSMUST00000037246; ENSMUSP00000035486; ENSMUSG00000034108.
DR GeneID; 12460; -.
DR KEGG; mmu:12460; -.
DR UCSC; uc008gba.1; mouse.
DR CTD; 9973; -.
DR MGI; MGI:1333783; Ccs.
DR VEuPathDB; HostDB:ENSMUSG00000034108; -.
DR eggNOG; KOG4656; Eukaryota.
DR GeneTree; ENSGT00940000159785; -.
DR HOGENOM; CLU_056632_0_2_1; -.
DR InParanoid; Q9WU84; -.
DR OMA; KGMGSDQ; -.
DR OrthoDB; 1527306at2759; -.
DR PhylomeDB; Q9WU84; -.
DR TreeFam; TF105184; -.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR BioGRID-ORCS; 12460; 12 hits in 75 CRISPR screens.
DR ChiTaRS; Ccs; mouse.
DR PRO; PR:Q9WU84; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9WU84; protein.
DR Bgee; ENSMUSG00000034108; Expressed in saccule of membranous labyrinth and 240 other tissues.
DR ExpressionAtlas; Q9WU84; baseline and differential.
DR Genevisible; Q9WU84; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IMP:MGI.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
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; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; SSF49329; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR PROSITE; PS50846; HMA_2; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Copper; Cytoplasm; Disulfide bond; Isopeptide bond;
KW Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..274
FT /note="Copper chaperone for superoxide dismutase"
FT /id="PRO_0000213544"
FT DOMAIN 11..74
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 88..234
FT /note="Superoxide dismutase-like"
FT BINDING 22
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 25
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 244
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT BINDING 246
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 141..227
FT /evidence="ECO:0000250"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O14618"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O14618"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O14618"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O14618"
SQ 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
