SCO2_YEAST
ID SCO2_YEAST Reviewed; 301 AA.
AC P38072; D6VQ26;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Protein SCO2, mitochondrial;
DE Flags: Precursor;
GN Name=SCO2; OrderedLocusNames=YBR024W; ORFNames=YBR0308;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091864; DOI=10.1002/yea.320100010;
RA Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT ten new open reading frames, five previously identified genes and a
RT homologue of the SCO1 gene.";
RL Yeast 10:S75-S80(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Acts as a copper chaperone, transporting copper to the Cu(A)
CC site on the cytochrome c oxidase subunit II (COX2).
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 1480 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SCO1/2 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; Z35893; CAA84966.1; -; Genomic_DNA.
DR EMBL; X76078; CAA53681.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07146.1; -; Genomic_DNA.
DR PIR; S45880; S45880.
DR RefSeq; NP_009580.1; NM_001178372.1.
DR AlphaFoldDB; P38072; -.
DR SMR; P38072; -.
DR BioGRID; 32727; 64.
DR DIP; DIP-3814N; -.
DR IntAct; P38072; 1.
DR STRING; 4932.YBR024W; -.
DR MaxQB; P38072; -.
DR PaxDb; P38072; -.
DR PRIDE; P38072; -.
DR EnsemblFungi; YBR024W_mRNA; YBR024W; YBR024W.
DR GeneID; 852312; -.
DR KEGG; sce:YBR024W; -.
DR SGD; S000000228; SCO2.
DR VEuPathDB; FungiDB:YBR024W; -.
DR eggNOG; KOG2792; Eukaryota.
DR GeneTree; ENSGT00390000004323; -.
DR HOGENOM; CLU_050131_0_1_1; -.
DR InParanoid; P38072; -.
DR OMA; MLYVKHE; -.
DR BioCyc; YEAST:G3O-29004-MON; -.
DR PRO; PR:P38072; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38072; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0016531; F:copper chaperone activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IDA:SGD.
DR GO; GO:0045454; P:cell redox homeostasis; IGI:SGD.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IBA:GO_Central.
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 InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151; PTHR12151; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR PIRSF; PIRSF037736; SCO1; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Copper; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..301
FT /note="Protein SCO2, mitochondrial"
FT /id="PRO_0000031924"
FT TRANSMEM 82..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 101..284
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT BINDING 154
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
SQ SEQUENCE 301 AA; 34889 MW; 247E1C4E91050E84 CRC64;
MLNSSRKYAC RSLFRQANVS IKGLFYNGGA YRRGFSTGCC LRSDNKESPS ARQPLDRLQL
GDEINEPEPI RTRFFQFSRW KATIALLLLS GGTYAYLSRK RRLLETEKEA DANRAYGSVA
LGGPFNLTDF NGKPFTEENL KGKFSILYFG FSHCPDICPE ELDRLTYWIS ELDDKDHIKI
QPLFISCDPA RDTPDVLKEY LSDFHPAIIG LTGTYDQVKS VCKKYKVYFS TPRDVKPNQD
YLVDHSIFFY LIDPEGQFID ALGRNYDEQS GLEKIREQIQ AYVPKEERER RSKKWYSFIF
N
