CCS1_CANGA
ID CCS1_CANGA Reviewed; 239 AA.
AC Q6FU61;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Superoxide dismutase 1 copper chaperone;
GN Name=CCS1; OrderedLocusNames=CAGL0F06017g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Copper chaperone for superoxide dismutase 1 (SOD1). Binds
CC copper ions and delivers them specifically to SOD1 (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CCS1 family. {ECO:0000305}.
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DR EMBL; CR380952; CAG59157.1; -; Genomic_DNA.
DR RefSeq; XP_446233.1; XM_446233.1.
DR AlphaFoldDB; Q6FU61; -.
DR SMR; Q6FU61; -.
DR STRING; 5478.XP_446233.1; -.
DR EnsemblFungi; CAG59157; CAG59157; CAGL0F06017g.
DR GeneID; 2887621; -.
DR KEGG; cgr:CAGL0F06017g; -.
DR CGD; CAL0130932; LYS7.
DR VEuPathDB; FungiDB:CAGL0F06017g; -.
DR eggNOG; KOG4656; Eukaryota.
DR HOGENOM; CLU_056632_0_0_1; -.
DR InParanoid; Q6FU61; -.
DR OMA; KGMGSDQ; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0101031; C:chaperone complex; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:1902693; C:superoxide dismutase complex; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IEA:EnsemblFungi.
DR GO; GO:0006825; P:copper ion transport; IEA:EnsemblFungi.
DR GO; GO:0015680; P:protein maturation by copper ion transfer; IEA:EnsemblFungi.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:EnsemblFungi.
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 PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00403; HMA; 1.
DR SUPFAM; SSF49329; SSF49329; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW Chaperone; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..239
FT /note="Superoxide dismutase 1 copper chaperone"
FT /id="PRO_0000239061"
FT DOMAIN 7..70
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 18
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 21
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 219
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT BINDING 221
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT DISULFID 28..65
FT /evidence="ECO:0000250|UniProtKB:P40202"
FT DISULFID 219
FT /note="Interchain (with C-58 in apo-SOD1)"
FT /evidence="ECO:0000250|UniProtKB:P40202"
SQ SEQUENCE 239 AA; 26124 MW; E3FBFF3A740C7713 CRC64;
MTANADFYEA TYAVPMHCTD CTDDIKKCLN GITGIKDLQF DISQQMMSVN SCVAPSVIIN
ALRDCGRDAI IRGAGKPNSS AVAILETFED VDLKKDTAVR GLARIVQVSD QKTLFDVTVN
GVPFSGKYQA KIHSNGNISE GVKSTGDVYY KFEEPIECSD ASDLDKSLYS GQNFVSAPLP
IWDLIGRSFV IFREGEPAYD IAGVIARSAG VWENDKQVCA CTGKTVWEER KDALKNNIK
