SCO2_DANRE
ID SCO2_DANRE Reviewed; 279 AA.
AC Q5RH02;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protein SCO2 homolog, mitochondrial;
DE Flags: Precursor;
GN Name=sco2; ORFNames=si:dkey-202b22.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Copper metallochaperone essential for the synthesis and
CC maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved
CC in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a
CC thiol-disulfide oxidoreductase to regulate the redox state of the
CC cysteines in SCO1 during maturation of MT-CO2/COX2.
CC {ECO:0000250|UniProtKB:O43819}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O43819}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O43819}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
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DR EMBL; BX649398; CAI20823.1; -; Genomic_DNA.
DR RefSeq; NP_001038697.1; NM_001045232.1.
DR RefSeq; XP_005164828.1; XM_005164771.3.
DR AlphaFoldDB; Q5RH02; -.
DR SMR; Q5RH02; -.
DR STRING; 7955.ENSDARP00000066987; -.
DR PaxDb; Q5RH02; -.
DR Ensembl; ENSDART00000150221; ENSDARP00000123722; ENSDARG00000045555.
DR Ensembl; ENSDART00000185200; ENSDARP00000149326; ENSDARG00000045555.
DR GeneID; 606683; -.
DR KEGG; dre:606683; -.
DR CTD; 9997; -.
DR ZFIN; ZDB-GENE-041210-173; sco2.
DR eggNOG; KOG2792; Eukaryota.
DR GeneTree; ENSGT00390000004323; -.
DR HOGENOM; CLU_050131_0_3_1; -.
DR InParanoid; Q5RH02; -.
DR OMA; KHAGRDY; -.
DR OrthoDB; 1462537at2759; -.
DR PhylomeDB; Q5RH02; -.
DR Reactome; R-DRE-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DRE-611105; Respiratory electron transport.
DR Reactome; R-DRE-9707564; Cytoprotection by HMOX1.
DR PRO; PR:Q5RH02; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000045555; Expressed in ovary and 22 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0016531; F:copper chaperone activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISS:UniProtKB.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IEA:InterPro.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISS:UniProtKB.
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 3: Inferred from homology;
KW Chaperone; Copper; Disulfide bond; 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 ?..279
FT /note="Protein SCO2 homolog, mitochondrial"
FT /id="PRO_0000354069"
FT TOPO_DOM ?..72
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT TRANSMEM 73..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..279
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT DOMAIN 97..271
FT /note="Thioredoxin"
FT BINDING 145
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT BINDING 149
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT BINDING 236
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT DISULFID 145..149
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 279 AA; 32111 MW; 79D2DEA5420A1827 CRC64;
MLRLRVFDRH KRLWSVLQST IRGNNISNHI PNTTCRSSAP PHLCARQRAF YSQNSPKTPN
PGSSAGIKLR TRLVVTLLFG GGIIGTWWYV HQEKEKRIQM QRLEQLRKVA LGQGDFHLLD
HTGQRRTKRD FLGHWVLLYF GFTHCPDICP DELEKLTSVV HILDKDPSLP SVQPLFITVD
PERDDVSAMA RYVKDFHPRL VGLTGSAEEV KQAGRDFRVY ASNGPKDEDG DYIVDHSIVI
YLVNPDGLFI DYYNRMKNDT QIAESIRNHM KTFVRLFPD
