SCO2_MOUSE
ID SCO2_MOUSE Reviewed; 255 AA.
AC Q8VCL2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein SCO2 homolog, mitochondrial;
DE Flags: Precursor;
GN Name=Sco2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=23643385; DOI=10.1016/j.ajhg.2013.04.005;
RA Tran-Viet K.N., Powell C., Barathi V.A., Klemm T., Maurer-Stroh S.,
RA Limviphuvadh V., Soler V., Ho C., Yanovitch T., Schneider G., Li Y.J.,
RA Nading E., Metlapally R., Saw S.M., Goh L., Rozen S., Young T.L.;
RT "Mutations in SCO2 are associated with autosomal-dominant high-grade
RT myopia.";
RL Am. J. Hum. Genet. 92:820-826(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. Interacts with COA6. Found in a complex with
CC TMEM177, COX20, COA6, MT-CO2/COX2, COX18 and SCO1. Interacts with
CC TMEM177 in a COX20-dependent manner. Interacts with COX20 in a MT-
CC CO2/COX2- and COX18-dependent manner. Interacts with COX16.
CC {ECO:0000250|UniProtKB:O43819}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O43819}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in retina, retinal pigment epithelium,
CC and sclera. {ECO:0000269|PubMed:23643385}.
CC -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
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DR EMBL; BC019554; AAH19554.1; -; mRNA.
DR CCDS; CCDS49701.1; -.
DR RefSeq; NP_001104758.1; NM_001111288.1.
DR AlphaFoldDB; Q8VCL2; -.
DR SMR; Q8VCL2; -.
DR BioGRID; 792533; 2.
DR STRING; 10090.ENSMUSP00000131943; -.
DR PhosphoSitePlus; Q8VCL2; -.
DR SwissPalm; Q8VCL2; -.
DR EPD; Q8VCL2; -.
DR jPOST; Q8VCL2; -.
DR MaxQB; Q8VCL2; -.
DR PaxDb; Q8VCL2; -.
DR PeptideAtlas; Q8VCL2; -.
DR PRIDE; Q8VCL2; -.
DR ProteomicsDB; 255365; -.
DR Antibodypedia; 78977; 175 antibodies from 31 providers.
DR Ensembl; ENSMUST00000167643; ENSMUSP00000131943; ENSMUSG00000091780.
DR Ensembl; ENSMUST00000228977; ENSMUSP00000155150; ENSMUSG00000091780.
DR GeneID; 100126824; -.
DR KEGG; mmu:100126824; -.
DR UCSC; uc033gwc.1; mouse.
DR CTD; 9997; -.
DR MGI; MGI:3818630; Sco2.
DR VEuPathDB; HostDB:ENSMUSG00000091780; -.
DR eggNOG; KOG2792; Eukaryota.
DR GeneTree; ENSGT00390000004323; -.
DR HOGENOM; CLU_050131_0_3_1; -.
DR InParanoid; Q8VCL2; -.
DR OMA; KHAGRDY; -.
DR OrthoDB; 1462537at2759; -.
DR PhylomeDB; Q8VCL2; -.
DR TreeFam; TF313752; -.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 100126824; 10 hits in 42 CRISPR screens.
DR PRO; PR:Q8VCL2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8VCL2; protein.
DR Bgee; ENSMUSG00000091780; Expressed in yolk sac and 65 other tissues.
DR Genevisible; Q8VCL2; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0030016; C:myofibril; ISO:MGI.
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:0055070; P:copper ion homeostasis; IMP:MGI.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISS:UniProtKB.
DR GO; GO:0003012; P:muscle system process; IMP:MGI.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; IMP:MGI.
DR GO; GO:0022904; P:respiratory electron transport chain; IMP:MGI.
DR GO; GO:0014823; P:response to activity; IMP:MGI.
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 InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151; PTHR12151; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR PIRSF; PIRSF037736; SCO1; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Copper; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..255
FT /note="Protein SCO2 homolog, mitochondrial"
FT /id="PRO_0000354068"
FT TOPO_DOM 42..49
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT TRANSMEM 50..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..255
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT DOMAIN 74..248
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT BINDING 122
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT BINDING 126
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT BINDING 213
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT DISULFID 122..126
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 255 AA; 28944 MW; 4EEB327CA12D89B4 CRC64;
MLLALGPKAW PKLSQFKPLL RISGGETLHR NSRHWAGQGQ RQGPGLRTRL LITALFGAGL
GWAWLAARAE KEQWRQQQRT EALRQAAVGQ GDFSLLDHKG QPRCKADFRG QWVLMYFGFT
HCPDICPDEL EKLVQVVRKL EAEPDLPLVQ PVFITVDPER DDVAAMARYV QEFHPRLLGL
TGSTEQVAHA SRNYRVYYSA GPKDEDQDYI VDHSIAIYLL NPDGLFTDYY GRSRSAEQIV
ESIRRHIAAF HSVLP
