CCS_DICDI
ID CCS_DICDI Reviewed; 316 AA.
AC Q54F73;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable copper chaperone for superoxide dismutase;
DE AltName: Full=Superoxide dismutase copper chaperone;
GN Name=ccs; Synonyms=ccsA; ORFNames=DDB_G0291031;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Delivers copper to copper zinc superoxide dismutases.
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 -!- SUBUNIT: Homodimer, and heterodimer with SOD1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; AAFI02000174; EAL61946.1; -; Genomic_DNA.
DR RefSeq; XP_635464.1; XM_630372.1.
DR AlphaFoldDB; Q54F73; -.
DR SMR; Q54F73; -.
DR STRING; 44689.DDB0238038; -.
DR PaxDb; Q54F73; -.
DR EnsemblProtists; EAL61946; EAL61946; DDB_G0291031.
DR GeneID; 8627964; -.
DR KEGG; ddi:DDB_G0291031; -.
DR dictyBase; DDB_G0291031; ccs.
DR eggNOG; KOG4656; Eukaryota.
DR HOGENOM; CLU_056632_0_2_1; -.
DR InParanoid; Q54F73; -.
DR OMA; KGMGSDQ; -.
DR PhylomeDB; Q54F73; -.
DR Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q54F73; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005829; C:cytosol; ISS:dictyBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:dictyBase.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR GO; GO:0016532; F:superoxide dismutase copper chaperone activity; ISS:dictyBase.
DR GO; GO:0015680; P:protein maturation by copper ion transfer; ISS:dictyBase.
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 InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 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..316
FT /note="Probable copper chaperone for superoxide dismutase"
FT /id="PRO_0000329400"
FT DOMAIN 7..71
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 99..298
FT /note="Superoxide dismutase-like"
FT REGION 179..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 308
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT DISULFID 169..291
FT /evidence="ECO:0000250"
SQ SEQUENCE 316 AA; 34468 MW; C167C77135B10589 CRC64;
MDDKNLEIKV ELNVDISCQS CVDSISKELR EKLENTKLVE HDIPEQRIVL QGTDLTQDIL
ETIKNTGRNA TICGLSSTTT TTSTSPSSST CHKKQETVSG SAVCSLGLIE NWQKGCGGSG
GVGSKGVYGV IRLLRASTTK TLFEGRITGL KPGKHSLVVH EFGNLMNGCD DLGEPFISNV
ENNNNNNNNN NNNNNNNNNN NNNNNNNNKN INKCKEILNK IIGTSDVKQD GKAEFRVLSD
KYDFWDLIGR SIVLHSQDSK YSPIEDLNNN NNNKNIVNSE SDKILGERVA CGIISRAASI
GQNHKKVCPC DGTTAI
