COX17_YEAST
ID COX17_YEAST Reviewed; 69 AA.
AC Q12287; D6VXZ3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Cytochrome c oxidase copper chaperone;
GN Name=COX17; OrderedLocusNames=YLL009C; ORFNames=L1343;
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 24657 / D273-10B;
RX PubMed=8662933; DOI=10.1074/jbc.271.24.14504;
RA Glerum D.M., Shtanko A., Tzagoloff A.;
RT "Characterization of COX17, a yeast gene involved in copper metabolism and
RT assembly of cytochrome oxidase.";
RL J. Biol. Chem. 271:14504-14509(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 PROTEIN SEQUENCE OF 2-6, CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=9407107; DOI=10.1074/jbc.272.52.33191;
RA Beers J., Glerum D.M., Tzagoloff A.;
RT "Purification, characterization, and localization of yeast Cox17p, a
RT mitochondrial copper shuttle.";
RL J. Biol. Chem. 272:33191-33196(1997).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9585572; DOI=10.1021/bi980418y;
RA Srinivasan C., Posewitz M.C., George G.N., Winge D.R.;
RT "Characterization of the copper chaperone Cox17 of Saccharomyces
RT cerevisiae.";
RL Biochemistry 37:7572-7577(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=15465825; DOI=10.1074/jbc.m408099200;
RA Abajian C., Yatsunyk L.A., Ramirez B.E., Rosenzweig A.C.;
RT "Yeast cox17 solution structure and copper(I) binding.";
RL J. Biol. Chem. 279:53584-53592(2004).
CC -!- FUNCTION: Copper chaperone for cytochrome c oxidase (COX). Binds two
CC copper ions and deliver them to the Cu(A) site of COX.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:9407107}.
CC -!- SIMILARITY: Belongs to the COX17 family. {ECO:0000305}.
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DR EMBL; L75948; AAA85477.1; -; Genomic_DNA.
DR EMBL; Z73114; CAA97453.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09309.1; -; Genomic_DNA.
DR PIR; S62056; S62056.
DR RefSeq; NP_013092.1; NM_001181829.1.
DR PDB; 1U96; NMR; -; A=1-69.
DR PDB; 1U97; NMR; -; A=1-69.
DR PDB; 1Z2G; NMR; -; A=1-69.
DR PDBsum; 1U96; -.
DR PDBsum; 1U97; -.
DR PDBsum; 1Z2G; -.
DR AlphaFoldDB; Q12287; -.
DR SMR; Q12287; -.
DR BioGRID; 31242; 214.
DR DIP; DIP-2915N; -.
DR IntAct; Q12287; 7.
DR MINT; Q12287; -.
DR STRING; 4932.YLL009C; -.
DR MaxQB; Q12287; -.
DR PaxDb; Q12287; -.
DR PRIDE; Q12287; -.
DR EnsemblFungi; YLL009C_mRNA; YLL009C; YLL009C.
DR GeneID; 850651; -.
DR KEGG; sce:YLL009C; -.
DR SGD; S000003932; COX17.
DR VEuPathDB; FungiDB:YLL009C; -.
DR eggNOG; KOG3496; Eukaryota.
DR HOGENOM; CLU_149618_3_1_1; -.
DR InParanoid; Q12287; -.
DR OMA; QYKTCMA; -.
DR BioCyc; YEAST:G3O-32114-MON; -.
DR EvolutionaryTrace; Q12287; -.
DR PRO; PR:Q12287; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12287; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0016531; F:copper chaperone activity; IDA:SGD.
DR GO; GO:1903136; F:cuprous ion binding; IDA:CAFA.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IDA:SGD.
DR GO; GO:0018343; P:protein farnesylation; IDA:MGI.
DR GO; GO:0015680; P:protein maturation by copper ion transfer; IDA:SGD.
DR DisProt; DP00277; -.
DR InterPro; IPR009069; Cys_alpha_HP_mot_SF.
DR InterPro; IPR007745; Cyt_c_oxidase_Cu-chaperone.
DR PANTHER; PTHR16719; PTHR16719; 1.
DR Pfam; PF05051; COX17; 1.
DR SUPFAM; SSF47072; SSF47072; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Copper; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Mitochondrion; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9407107"
FT CHAIN 2..69
FT /note="Cytochrome c oxidase copper chaperone"
FT /id="PRO_0000213541"
FT DOMAIN 23..65
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 26..36
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 47..57
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT BINDING 23
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q14061"
FT BINDING 24
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q14061"
FT DISULFID 26..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 36..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1U97"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:1U96"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1Z2G"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:1U96"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1U96"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:1U96"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1U96"
SQ SEQUENCE 69 AA; 8056 MW; 7DA9A5F97C8A3F78 CRC64;
MTETDKKQEQ ENHAECEDKP KPCCVCKPEK EERDTCILFN GQDSEKCKEF IEKYKECMKG
YGFEVPSAN
