CCS1_YARLI
ID CCS1_YARLI Reviewed; 234 AA.
AC Q6BZU2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Superoxide dismutase 1 copper chaperone;
GN Name=CCS1; OrderedLocusNames=YALI0F30877g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382132; CAG78883.1; -; Genomic_DNA.
DR RefSeq; XP_506070.1; XM_506070.1.
DR AlphaFoldDB; Q6BZU2; -.
DR SMR; Q6BZU2; -.
DR STRING; 4952.CAG78883; -.
DR EnsemblFungi; CAG78883; CAG78883; YALI0_F30877g.
DR GeneID; 2907912; -.
DR KEGG; yli:YALI0F30877g; -.
DR VEuPathDB; FungiDB:YALI0_F30877g; -.
DR HOGENOM; CLU_056632_0_0_1; -.
DR InParanoid; Q6BZU2; -.
DR OMA; KGMGSDQ; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0101031; C:chaperone complex; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
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; IBA:GO_Central.
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.
FT CHAIN 1..234
FT /note="Superoxide dismutase 1 copper chaperone"
FT /id="PRO_0000239064"
FT DOMAIN 2..65
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 13
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 16
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 211
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT BINDING 213
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT DISULFID 211
FT /note="Interchain (with C-58 in apo-SOD1)"
FT /evidence="ECO:0000250|UniProtKB:P40202"
SQ SEQUENCE 234 AA; 24371 MW; 4F16849B800EDCC4 CRC64;
MSFTTTFAVP LECESCCDSV KQALANVQGI ESVDCKLVDQ LISVTGTSAP SQIVKAVQNI
GKDAIVRGTG QPNSAAVCIL ESHAPEDQAQ PIKGLARIVS VSKTLALIDI TLNGLPKGTY
YPSIRTSGDI SDAPQSLGGV YQALGSVEVN ESDSASGLFS GQAFVKSETQ ISSLIGRGMA
VSTSPDVVKP HALVGVIARS AGVWENDKTV CSCSGKTVWE ERKDVQSKGL EGQL
