COX17_SCHPO
ID COX17_SCHPO Reviewed; 70 AA.
AC Q9P7Z7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cytochrome c oxidase copper chaperone;
GN Name=cox17; ORFNames=SPBC26H8.14c;
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: Copper chaperone for cytochrome c oxidase (COX). Binds two
CC copper ions and deliver them to the Cu(A) site of COX (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the COX17 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB75401.1; -; Genomic_DNA.
DR RefSeq; NP_596649.1; NM_001022571.2.
DR AlphaFoldDB; Q9P7Z7; -.
DR SMR; Q9P7Z7; -.
DR STRING; 4896.SPBC26H8.14c.1; -.
DR MaxQB; Q9P7Z7; -.
DR PaxDb; Q9P7Z7; -.
DR EnsemblFungi; SPBC26H8.14c.1; SPBC26H8.14c.1:pep; SPBC26H8.14c.
DR GeneID; 2540423; -.
DR KEGG; spo:SPBC26H8.14c; -.
DR PomBase; SPBC26H8.14c; cox17.
DR VEuPathDB; FungiDB:SPBC26H8.14c; -.
DR eggNOG; KOG3496; Eukaryota.
DR HOGENOM; CLU_149618_1_3_1; -.
DR InParanoid; Q9P7Z7; -.
DR OMA; QYKTCMA; -.
DR PhylomeDB; Q9P7Z7; -.
DR PRO; PR:Q9P7Z7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; ISS:PomBase.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:PomBase.
DR GO; GO:0016531; F:copper chaperone activity; ISS:PomBase.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISS:PomBase.
DR GO; GO:0015680; P:protein maturation by copper ion transfer; ISS:PomBase.
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 3: Inferred from homology;
KW Chaperone; Copper; Disulfide bond; Metal-binding; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..70
FT /note="Cytochrome c oxidase copper chaperone"
FT /id="PRO_0000239059"
FT DOMAIN 28..70
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 31..41
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 52..62
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q14061"
FT BINDING 29
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q14061"
FT DISULFID 31..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 41..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 70 AA; 7493 MW; B56C3AD2C763E9FB CRC64;
MSSSTEPSTA TKVSEPAPIA SEEKPKPCCA CPETKQARDA CMLQSSNGPI ECAKLIEAHK
KCMAQYGYEV