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SCO1_YEAST
ID   SCO1_YEAST              Reviewed;         295 AA.
AC   P23833; D6VQ37;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 172.
DE   RecName: Full=Protein SCO1, mitochondrial;
DE   Flags: Precursor;
GN   Name=SCO1; OrderedLocusNames=YBR037C; ORFNames=YBR0406;
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].
RX   PubMed=2543907; DOI=10.1007/bf00332228;
RA   Schulze M., Roedel G.;
RT   "Accumulation of the cytochrome c oxidase subunits I and II in yeast
RT   requires a mitochondrial membrane-associated protein, encoded by the
RT   nuclear SCO1 gene.";
RL   Mol. Gen. Genet. 216:37-43(1989).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=1944230; DOI=10.1007/bf00267464;
RA   Buchwald P., Krummeck G., Roedel G.;
RT   "Immunological identification of yeast SCO1 protein as a component of the
RT   inner mitochondrial membrane.";
RL   Mol. Gen. Genet. 229:413-420(1991).
RN   [6]
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).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 96-295 IN COMPLEX WITH COPPER
RP   IONS, AND FUNCTION.
RX   PubMed=16570183; DOI=10.1007/s00775-006-0096-7;
RA   Abajian C., Rosenzweig A.C.;
RT   "Crystal structure of yeast Sco1.";
RL   J. Biol. Inorg. Chem. 11:459-466(2006).
CC   -!- FUNCTION: Required for the accumulation of subunits 1 and 2 of
CC       cytochrome c oxidase complex. Thought to play a role in either
CC       mitochondrial copper transport or insertion of copper into the active
CC       site of COX. {ECO:0000269|PubMed:16570183}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:1944230}.
CC   -!- MISCELLANEOUS: Present with 2550 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
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DR   EMBL; X17441; CAA35490.1; -; Genomic_DNA.
DR   EMBL; Z35906; CAA84979.1; -; Genomic_DNA.
DR   EMBL; AY557863; AAS56189.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07157.1; -; Genomic_DNA.
DR   PIR; JE0051; JE0051.
DR   RefSeq; NP_009593.1; NM_001178385.1.
DR   PDB; 2B7J; X-ray; 2.30 A; A/B/C/D=96-295.
DR   PDB; 2B7K; X-ray; 1.80 A; A/B/C/D=96-295.
DR   PDBsum; 2B7J; -.
DR   PDBsum; 2B7K; -.
DR   AlphaFoldDB; P23833; -.
DR   SMR; P23833; -.
DR   BioGRID; 32738; 168.
DR   DIP; DIP-7610N; -.
DR   IntAct; P23833; 3.
DR   STRING; 4932.YBR037C; -.
DR   MaxQB; P23833; -.
DR   PaxDb; P23833; -.
DR   PRIDE; P23833; -.
DR   EnsemblFungi; YBR037C_mRNA; YBR037C; YBR037C.
DR   GeneID; 852325; -.
DR   KEGG; sce:YBR037C; -.
DR   SGD; S000000241; SCO1.
DR   VEuPathDB; FungiDB:YBR037C; -.
DR   eggNOG; KOG2792; Eukaryota.
DR   GeneTree; ENSGT00390000004323; -.
DR   HOGENOM; CLU_050131_0_1_1; -.
DR   InParanoid; P23833; -.
DR   OMA; IVAHMRP; -.
DR   BioCyc; YEAST:G3O-29012-MON; -.
DR   EvolutionaryTrace; P23833; -.
DR   PRO; PR:P23833; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P23833; protein.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner 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; IMP:SGD.
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   1: Evidence at protein level;
KW   3D-structure; 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           ?..295
FT                   /note="Protein SCO1, mitochondrial"
FT                   /id="PRO_0000031923"
FT   TRANSMEM        76..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         148
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   STRAND          120..123
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   HELIX           131..134
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   STRAND          139..144
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   HELIX           151..170
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   STRAND          175..181
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   TURN            183..185
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   HELIX           188..195
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   STRAND          203..206
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   HELIX           209..218
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   TURN            237..239
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   STRAND          243..246
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   STRAND          252..256
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   HELIX           264..275
FT                   /evidence="ECO:0007829|PDB:2B7K"
FT   STRAND          284..291
FT                   /evidence="ECO:0007829|PDB:2B7J"
SQ   SEQUENCE   295 AA;  33166 MW;  500EFD92A0F44DDA CRC64;
     MLKLSRSANL RLVQLPAARL SGNGAKLLTQ RGFFTVTRLW QSNGKKPLSR VPVGGTPIKD
     NGKVREGSIE FSTGKAIALF LAVGGALSYF FNREKRRLET QKEAEANRGY GKPSLGGPFH
     LEDMYGNEFT EKNLLGKFSI IYFGFSNCPD ICPDELDKLG LWLNTLSSKY GITLQPLFIT
     CDPARDSPAV LKEYLSDFHP SILGLTGTFD EVKNACKKYR VYFSTPPNVK PGQDYLVDHS
     IFFYLMDPEG QFVDALGRNY DEKTGVDKIV EHVKSYVPAE QRAKQKEAWY SFLFK
 
 
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