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SCO1_SCHPO
ID   SCO1_SCHPO              Reviewed;         263 AA.
AC   O42899;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Protein sco1;
GN   Name=sco1; ORFNames=SPBC119.06;
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).
CC   -!- FUNCTION: Acts as a copper chaperone, transporting copper to the Cu(A)
CC       site on the cytochrome c oxidase subunit II (COX2). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA17921.1; -; Genomic_DNA.
DR   PIR; T39304; T39304.
DR   RefSeq; NP_595287.1; NM_001021194.2.
DR   AlphaFoldDB; O42899; -.
DR   SMR; O42899; -.
DR   BioGRID; 276375; 2.
DR   STRING; 4896.SPBC119.06.1; -.
DR   MaxQB; O42899; -.
DR   PaxDb; O42899; -.
DR   PRIDE; O42899; -.
DR   EnsemblFungi; SPBC119.06.1; SPBC119.06.1:pep; SPBC119.06.
DR   GeneID; 2539826; -.
DR   KEGG; spo:SPBC119.06; -.
DR   PomBase; SPBC119.06; sco1.
DR   VEuPathDB; FungiDB:SPBC119.06; -.
DR   eggNOG; KOG2792; Eukaryota.
DR   HOGENOM; CLU_050131_0_3_1; -.
DR   InParanoid; O42899; -.
DR   OMA; MISIRAL; -.
DR   PhylomeDB; O42899; -.
DR   PRO; PR:O42899; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:PomBase.
DR   GO; GO:0016531; F:copper chaperone activity; ISS:PomBase.
DR   GO; GO:0005507; F:copper ion binding; ISS:PomBase.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; IEA:InterPro.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISS:PomBase.
DR   CDD; cd02968; SCO; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR017276; Synth_of_cyt-c-oxidase_Sco1/2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12151; PTHR12151; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   PIRSF; PIRSF037736; SCO1; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   3: Inferred from homology;
KW   Chaperone; Copper; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome.
FT   CHAIN           1..263
FT                   /note="Protein sco1"
FT                   /id="PRO_0000173873"
FT   BINDING         130
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   263 AA;  30240 MW;  F54380DB32CD1E4D CRC64;
     MFRRGLVFSR HCHYSLIRPR FPLNRTCLAR FADGRKNLAT DNRTQTYQSW RGMISIRALL
     LAAATSVGLY AYFQHEKKKV LERQNDKVLA TIGRPQLGGA FSLIDHHGNR VTDNDFKGKF
     SLIYFGFTRC PDICPDELDK MSAAIDIVNN VVGDVVYPIF ITCDPARDPP QEMAEYLEDF
     NPKIVGLTGS YEEIKDICKK FRVYFSTPKN IDPKKDDYLV DHSVFFYLMD PEGKFIEVFG
     RNSTSEDLAR AIGSYYLSRK KQK
 
 
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