CCS_RAT
ID CCS_RAT Reviewed; 274 AA.
AC Q9JK72; B0BMW1;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Copper chaperone for superoxide dismutase;
DE AltName: Full=Superoxide dismutase copper chaperone;
GN Name=Ccs;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RC STRAIN=Sprague-Dawley;
RX PubMed=10964676; DOI=10.1006/bbrc.2000.3328;
RA Hiromura M., Chino H., Sonoda T., Sakurai H.;
RT "Molecular cloning and characterization of a copper chaperone for
RT copper/zinc superoxide dismutase from the rat.";
RL Biochem. Biophys. Res. Commun. 275:394-400(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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).
CC -!- FUNCTION: Delivers copper to copper zinc superoxide dismutase (SOD1).
CC {ECO:0000250}.
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 -!- 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.
CC -!- SIMILARITY: In the C-terminal section; belongs to the Cu-Zn superoxide
CC dismutase family. {ECO:0000305}.
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DR EMBL; AF255305; AAF65572.1; -; mRNA.
DR EMBL; BC158586; AAI58587.1; -; mRNA.
DR RefSeq; NP_445877.1; NM_053425.1.
DR AlphaFoldDB; Q9JK72; -.
DR SMR; Q9JK72; -.
DR IntAct; Q9JK72; 1.
DR STRING; 10116.ENSRNOP00000026670; -.
DR iPTMnet; Q9JK72; -.
DR PhosphoSitePlus; Q9JK72; -.
DR jPOST; Q9JK72; -.
DR PaxDb; Q9JK72; -.
DR PRIDE; Q9JK72; -.
DR GeneID; 84485; -.
DR KEGG; rno:84485; -.
DR UCSC; RGD:620403; rat.
DR CTD; 9973; -.
DR RGD; 620403; Ccs.
DR eggNOG; KOG4656; Eukaryota.
DR InParanoid; Q9JK72; -.
DR OrthoDB; 1527306at2759; -.
DR PhylomeDB; Q9JK72; -.
DR TreeFam; TF105184; -.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q9JK72; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005507; F:copper ion binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR GO; GO:0016532; F:superoxide dismutase copper chaperone activity; TAS:RGD.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISO:RGD.
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_0000213546"
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:0000250|UniProtKB:O14618"
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"
FT CONFLICT 99
FT /note="V -> I (in Ref. 2; AAI58587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 28890 MW; 55C95B72C808C800 CRC64;
MASKSGDGGT MCALEFTVQM SCQSCVDAVH KTLKGAAGVQ NVEVQLENQM VLVQTTLPSQ
EVQALLESTG RQAVLKGMGS SQLKNLGAAV AIMEGSGTVQ GVVRFLQLSS ELCLIEGTID
GLEPGLHGLH VHQYGDLTKD CSSCGDHFNP DGASHGGPQD TDRHRGDLGN VHAEASGRAT
FRIEDKQLKV WDVIGRSLVV DEGEDDLGRG GHPLSKVTGN SGKRLACGII ARSAGLFQNP
KQICSCDGLT IWEERGRPIA GQGRKDSAQP PAHL
