CCS_PIG
ID CCS_PIG Reviewed; 274 AA.
AC Q6PWT7;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Copper chaperone for superoxide dismutase;
DE AltName: Full=Superoxide dismutase copper chaperone;
GN Name=CCS;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15265083; DOI=10.1111/j.1365-2052.2004.01150.x;
RA Silahtaroglu A.N., Jensen L.R., Harboe T.L., Horn P., Bendixen C.,
RA Tommerup N., Tumer Z.;
RT "Sequencing and mapping of the porcine CCS gene.";
RL Anim. Genet. 35:353-354(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; AY573056; AAS91658.1; -; mRNA.
DR RefSeq; NP_001001866.1; NM_001001866.1.
DR STRING; 9823.ENSSSCP00000027331; -.
DR PaxDb; Q6PWT7; -.
DR PeptideAtlas; Q6PWT7; -.
DR PRIDE; Q6PWT7; -.
DR GeneID; 414913; -.
DR KEGG; ssc:414913; -.
DR CTD; 9973; -.
DR eggNOG; KOG4656; Eukaryota.
DR InParanoid; Q6PWT7; -.
DR OrthoDB; 1527306at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Chaperone; Copper; Cytoplasm; Disulfide bond; Isopeptide bond;
KW Metal-binding; Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..274
FT /note="Copper chaperone for superoxide dismutase"
FT /id="PRO_0000213545"
FT DOMAIN 11..74
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 88..234
FT /note="Superoxide dismutase-like"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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; 29397 MW; DBB4316841BEFBE4 CRC64;
MASDSRDRET ACMLEFAVQM TCQSCVDAVS RSLQGVAGIQ SVEVQLENQM VLVQTTLPSQ
VVQALLEDTG RQAVLKGMGS GRWQNLEAAV AILGGSGPVQ GVVRFLQLTP ERCLIEGTID
GLKPGLHGLH VHQFGDLTRN CNSCGDHFNP DGMSHGGPQD SDRHRGDLGN VCADADGRAV
FRMEDELLKV WDVIGRSLVI DEGEDDLGRG GHPLSKITGN SGERLACGII ARSAGLFQNP
KQICSCDGLT IWEERXRPIA GEGRKEPAQP PAHL
