COX15_YEAST
ID COX15_YEAST Reviewed; 486 AA.
AC P40086; D3DM48;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cytochrome c oxidase assembly protein COX15 {ECO:0000305};
DE AltName: Full=Heme a synthase COX15 {ECO:0000303|PubMed:26940873};
DE Flags: Precursor;
GN Name=COX15 {ECO:0000303|PubMed:9228094};
GN OrderedLocusNames=YER141W {ECO:0000312|SGD:S000000943};
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 24657 / D273-10B;
RX PubMed=9228094; DOI=10.1074/jbc.272.30.19088;
RA Glerum D.M., Muroff I., Jin C., Tzagoloff A.;
RT "COX15 codes for a mitochondrial protein essential for the assembly of
RT yeast cytochrome oxidase.";
RL J. Biol. Chem. 272:19088-19094(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 FUNCTION.
RX PubMed=11248251; DOI=10.1016/s0014-5793(01)02249-9;
RA Barros M.H., Carlson C.G., Glerum D.M., Tzagoloff A.;
RT "Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of
RT heme O.";
RL FEBS Lett. 492:133-138(2001).
RN [5]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF HIS-169; THR-236; HIS-245; HIS-368
RP AND HIS-431.
RX PubMed=26940873; DOI=10.1074/jbc.m115.707539;
RA Swenson S., Cannon A., Harris N.J., Taylor N.G., Fox J.L., Khalimonchuk O.;
RT "Analysis of oligomerization properties of heme a synthase provides
RT insights into its function in eukaryotes.";
RL J. Biol. Chem. 291:10411-10425(2016).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29897761; DOI=10.1021/acs.jproteome.8b00032;
RA He C., Jia C., Zhang Y., Xu P.;
RT "Enrichment-based proteogenomics identifies microproteins, missing
RT proteins, and novel smORFs in Saccharomyces cerevisiae.";
RL J. Proteome Res. 17:2335-2344(2018).
CC -!- FUNCTION: Required for the assembly of yeast cytochrome oxidase.
CC Involved in the biosynthesis of heme A and the initial step in this
CC pathway, the hydroxylation of heme O, is thought to be catalyzed by a
CC three-component mono-oxygenase consisting of COX15, ferredoxin YAH1 and
CC ferredoxin reductase ARH1. {ECO:0000269|PubMed:11248251,
CC ECO:0000269|PubMed:9228094}.
CC -!- SUBUNIT: Forms 200-350 kDa oligomeric complexes independent on heme
CC binding. {ECO:0000269|PubMed:26940873}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:9228094}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9228094}.
CC -!- SIMILARITY: Belongs to the COX15/CtaA family. {ECO:0000305}.
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DR EMBL; L38643; AAA57471.1; -; Genomic_DNA.
DR EMBL; U18917; AAB64668.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07802.1; -; Genomic_DNA.
DR PIR; S50644; S50644.
DR RefSeq; NP_011068.1; NM_001179031.1.
DR AlphaFoldDB; P40086; -.
DR SMR; P40086; -.
DR BioGRID; 36890; 75.
DR IntAct; P40086; 12.
DR MINT; P40086; -.
DR STRING; 4932.YER141W; -.
DR MaxQB; P40086; -.
DR PaxDb; P40086; -.
DR PRIDE; P40086; -.
DR EnsemblFungi; YER141W_mRNA; YER141W; YER141W.
DR GeneID; 856884; -.
DR KEGG; sce:YER141W; -.
DR SGD; S000000943; COX15.
DR VEuPathDB; FungiDB:YER141W; -.
DR eggNOG; KOG2725; Eukaryota.
DR GeneTree; ENSGT00390000002223; -.
DR HOGENOM; CLU_017627_4_1_1; -.
DR InParanoid; P40086; -.
DR OMA; YWWEWGH; -.
DR BioCyc; YEAST:G3O-30302-MON; -.
DR BRENDA; 1.17.99.9; 984.
DR Reactome; R-SCE-189451; Heme biosynthesis.
DR PHI-base; PHI:503; -.
DR PRO; PR:P40086; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40086; 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:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; IMP:SGD.
DR GO; GO:0006784; P:heme A biosynthetic process; IMP:SGD.
DR HAMAP; MF_01665; HemeA_synth_type2; 1.
DR InterPro; IPR003780; COX15/CtaA_fam.
DR InterPro; IPR023754; HemeA_Synthase_type2.
DR PANTHER; PTHR23289; PTHR23289; 1.
DR Pfam; PF02628; COX15-CtaA; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..486
FT /note="Cytochrome c oxidase assembly protein COX15"
FT /id="PRO_0000183933"
FT TOPO_DOM 34..85
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..170
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..200
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..243
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..293
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..364
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 365..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..402
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..486
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT SITE 169
FT /note="Involved in either heme binding or the catalytic
FT mechanism of the enzyme"
FT /evidence="ECO:0000305|PubMed:26940873"
FT SITE 245
FT /note="Involved in either heme binding or the catalytic
FT mechanism of the enzyme"
FT /evidence="ECO:0000305|PubMed:26940873"
FT SITE 368
FT /note="Involved in either heme binding or the catalytic
FT mechanism of the enzyme"
FT /evidence="ECO:0000305|PubMed:26940873"
FT SITE 431
FT /note="Involved in either heme binding or the catalytic
FT mechanism of the enzyme"
FT /evidence="ECO:0000305|PubMed:26940873"
FT MUTAGEN 169
FT /note="H->A,C,Y: Fails to rescue the heme a biosynthetic
FT defect of a cox15delta mutant."
FT /evidence="ECO:0000269|PubMed:26940873"
FT MUTAGEN 236
FT /note="T->R: Converts to human ortholog residue: No
FT effect."
FT /evidence="ECO:0000269|PubMed:26940873"
FT MUTAGEN 236
FT /note="T->W: Mimicks pathogenic substituion found in human
FT patients: Fails to rescue the heme a biosynthetic defect of
FT a cox15delta mutant."
FT /evidence="ECO:0000269|PubMed:26940873"
FT MUTAGEN 245
FT /note="H->A,C,Y: Fails to rescue the heme a biosynthetic
FT defect of a cox15delta mutant."
FT /evidence="ECO:0000269|PubMed:26940873"
FT MUTAGEN 368
FT /note="H->A,C,Y: Fails to rescue the heme a biosynthetic
FT defect of a cox15delta mutant."
FT /evidence="ECO:0000269|PubMed:26940873"
FT MUTAGEN 431
FT /note="H->A,C,Y: Fails to rescue the heme a biosynthetic
FT defect of a cox15delta mutant."
FT /evidence="ECO:0000269|PubMed:26940873"
SQ SEQUENCE 486 AA; 54658 MW; 81E2B3C418D9527D CRC64;
MLFRNIEVGR QAAKLLTRTS SRLAWQSIGA SRNISTIRQQ IRKTQLYNFK KTVSIRPFSL
SSPVFKPHVA SESNPIESRL KTSKNVAYWL IGTSGLVFGI VVLGGLTRLT ESGLSITEWK
PVTGTLPPMN QKEWEEEFIK YKESPEFKLL NSHIDLDEFK FIFFMEWIHR LWGRAIGAVF
ILPAVYFAVS KKTSGHVNKR LFGLAGLLGL QGFVGWWMVK SGLDQEQLDA RKSKPTVSQY
RLTTHLGTAF FLYMGMLWTG LEILRECKWI KNPVQAISLF KKLDNPAIGP MRKISLALLA
VSFLTAMSGG MVAGLDAGWV YNTWPKMGER WFPSSRELMD ENFCRREDKK DLWWRNLLEN
PVTVQLVHRT CAYVAFTSVL AAHMYAIKKK AVIPRNAMTS LHVMMGVVTL QATLGILTIL
YLVPISLASI HQAGALALLT SSLVFASQLR KPRAPMRNVI ITLPHSSKVT SGKILSEASK
LASKPL
