CCS1_SCHPO
ID CCS1_SCHPO Reviewed; 297 AA.
AC Q10357;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Superoxide dismutase 1 copper chaperone;
GN Name=ccs1; Synonyms=pccs; ORFNames=SPAC22E12.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15107426; DOI=10.1074/jbc.m403426200;
RA Laliberte J., Whitson L.J., Beaudoin J., Holloway S.P., Hart P.J.,
RA Labbe S.;
RT "The Schizosaccharomyces pombe Pccs protein functions in both copper
RT trafficking and metal detoxification pathways.";
RL J. Biol. Chem. 279:28744-28755(2004).
CC -!- FUNCTION: Copper chaperone for superoxide dismutase 1 (sod1). Binds
CC copper ions and delivers them specifically to sod1. Also has a role in
CC cell protection against copper ion toxicity during conditions of copper
CC excess. The C-terminal region is thought to act specifically in this
CC sequestration role. {ECO:0000269|PubMed:15107426}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15107426}.
CC -!- SIMILARITY: Belongs to the CCS1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA93891.1; -; Genomic_DNA.
DR PIR; T38161; T38161.
DR RefSeq; NP_594830.1; NM_001020259.2.
DR AlphaFoldDB; Q10357; -.
DR SMR; Q10357; -.
DR BioGRID; 278294; 3.
DR STRING; 4896.SPAC22E12.04.1; -.
DR iPTMnet; Q10357; -.
DR MaxQB; Q10357; -.
DR PaxDb; Q10357; -.
DR EnsemblFungi; SPAC22E12.04.1; SPAC22E12.04.1:pep; SPAC22E12.04.
DR PomBase; SPAC22E12.04; ccs1.
DR VEuPathDB; FungiDB:SPAC22E12.04; -.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_0_0_1; -.
DR InParanoid; Q10357; -.
DR PhylomeDB; Q10357; -.
DR Reactome; R-SPO-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q10357; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016531; F:copper chaperone activity; IDA:PomBase.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IMP:PomBase.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:PomBase.
DR GO; GO:0071248; P:cellular response to metal ion; IMP:PomBase.
DR GO; GO:0019430; P:removal of superoxide radicals; IMP:PomBase.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR SUPFAM; SSF49329; SSF49329; 1.
PE 3: Inferred from homology;
KW Chaperone; Copper; Cytoplasm; Metal-binding; Reference proteome.
FT CHAIN 1..297
FT /note="Superoxide dismutase 1 copper chaperone"
FT /id="PRO_0000213547"
FT REGION 222..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O14618"
SQ SEQUENCE 297 AA; 32244 MW; 70C128A3BBE2B2BA CRC64;
MFEVEYLIKD CDDVNKNTLE QEFQDLNIED WKWDAATGQL IVKGSVSPSK VLRRLENATS
KPILIRGASN KESGVSILYE ANEDITQIPK VYGLCRFIPT EEKIFLDLIA TQLLPNREYT
GLVTISGDIS RGLKSAGDSL VTLFNANSNE QGKIVLDKEV SGSLPNWIGH CFVLKCVDDS
DSATMGIISR SAGLGQNTKQ ICACTGKSLW TEHAELKSVN EGSSCCSKKD SSPSEKPSCC
SQEKKSCCSS KKPSCCSQEK KGCCSTEKTS CCSQEKKSCC TSEKPSCCSN GKSTVCA
