SCO1_MOUSE
ID SCO1_MOUSE Reviewed; 284 AA.
AC Q5SUC9; Q3UTD6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein SCO1 homolog, mitochondrial;
DE Flags: Precursor;
GN Name=Sco1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-284.
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC 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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25683716; DOI=10.1016/j.celrep.2015.01.019;
RA Hlynialuk C.J., Ling B., Baker Z.N., Cobine P.A., Yu L.D., Boulet A.,
RA Wai T., Hossain A., El Zawily A.M., McFie P.J., Stone S.J., Diaz F.,
RA Moraes C.T., Viswanathan D., Petris M.J., Leary S.C.;
RT "The mitochondrial metallochaperone SCO1 is required to sustain expression
RT of the high-affinity copper transporter CTR1 and preserve copper
RT homeostasis.";
RL Cell Rep. 10:933-943(2015).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-115.
RX PubMed=28973536; DOI=10.1093/hmg/ddx344;
RA Baker Z.N., Jett K., Boulet A., Hossain A., Cobine P.A., Kim B.E.,
RA El Zawily A.M., Lee L., Tibbits G.F., Petris M.J., Leary S.C.;
RT "The mitochondrial metallochaperone SCO1 maintains CTR1 at the plasma
RT membrane to preserve copper homeostasis in the murine heart.";
RL Hum. Mol. Genet. 26:4617-4628(2017).
CC -!- FUNCTION: Copper metallochaperone essential for the maturation of
CC cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the
CC synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT-
CC CO2/COX2 during its subsequent maturation. Involved in transporting
CC copper to the Cu(A) site on MT-CO2/COX2 (By similarity). Plays an
CC important role in the regulation of copper homeostasis by controlling
CC the abundance and cell membrane localization of copper transporter CTR1
CC (PubMed:25683716, PubMed:28973536). {ECO:0000250|UniProtKB:O75880,
CC ECO:0000269|PubMed:25683716, ECO:0000269|PubMed:28973536}.
CC -!- SUBUNIT: Homodimer. Interacts with COA6. Found in a complex with
CC TMEM177, COX20, COA6, MT-CO2/COX2, COX18 and SCO2. 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:O75880}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O75880}.
CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:O75880}; Single-
CC pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Heart-specific and striated muscle-specific
CC knockout mice exhibit a lethal phenotype due to a combined COX and
CC copper deficiency that results in a dilated cardiomyopathy. Cardiac
CC copper deficiency is caused by the mislocalization of copper
CC transporter CTR1 to the cytoplasm (PubMed:28973536). Liver-specific
CC knockout mice exhibit a lethal phenotype associated with profound
CC hepatic COX and copper deficiencies. Hepatic copper deficiency is due
CC to reduced localization of CTR1 at the cell membrane and an enhanced
CC proteasomal degradation of CTR1 (PubMed:25683716).
CC {ECO:0000269|PubMed:25683716, ECO:0000269|PubMed:28973536}.
CC -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
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DR EMBL; AL645988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139008; AAI39009.1; -; mRNA.
DR EMBL; BC139009; AAI39010.1; -; mRNA.
DR EMBL; AK139512; BAE24044.1; -; mRNA.
DR CCDS; CCDS36183.1; -.
DR RefSeq; NP_001035115.1; NM_001040026.1.
DR AlphaFoldDB; Q5SUC9; -.
DR SMR; Q5SUC9; -.
DR BioGRID; 206870; 38.
DR STRING; 10090.ENSMUSP00000090673; -.
DR iPTMnet; Q5SUC9; -.
DR PhosphoSitePlus; Q5SUC9; -.
DR EPD; Q5SUC9; -.
DR jPOST; Q5SUC9; -.
DR MaxQB; Q5SUC9; -.
DR PaxDb; Q5SUC9; -.
DR PeptideAtlas; Q5SUC9; -.
DR PRIDE; Q5SUC9; -.
DR ProteomicsDB; 255364; -.
DR Antibodypedia; 12932; 164 antibodies from 29 providers.
DR Ensembl; ENSMUST00000092996; ENSMUSP00000090673; ENSMUSG00000069844.
DR GeneID; 52892; -.
DR KEGG; mmu:52892; -.
DR UCSC; uc007jlu.1; mouse.
DR CTD; 6341; -.
DR MGI; MGI:106362; Sco1.
DR VEuPathDB; HostDB:ENSMUSG00000069844; -.
DR eggNOG; KOG2792; Eukaryota.
DR GeneTree; ENSGT00390000004323; -.
DR HOGENOM; CLU_050131_0_3_1; -.
DR InParanoid; Q5SUC9; -.
DR OMA; IVAHMRP; -.
DR OrthoDB; 1462537at2759; -.
DR PhylomeDB; Q5SUC9; -.
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; 52892; 21 hits in 70 CRISPR screens.
DR ChiTaRS; Kit; mouse.
DR PRO; PR:Q5SUC9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SUC9; protein.
DR Bgee; ENSMUSG00000069844; Expressed in interventricular septum and 170 other tissues.
DR ExpressionAtlas; Q5SUC9; baseline and differential.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IDA:MGI.
DR GO; GO:0019371; P:cyclooxygenase pathway; IMP:MGI.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP:MGI.
DR GO; GO:1900077; P:negative regulation of cellular response to insulin stimulus; IDA:MGI.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IDA:MGI.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:1904959; P:regulation of cytochrome-c oxidase activity; IMP:MGI.
DR CDD; cd02968; SCO; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151; PTHR12151; 1.
DR Pfam; PF02630; SCO1-SenC; 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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..284
FT /note="Protein SCO1 homolog, mitochondrial"
FT /id="PRO_0000354066"
FT TOPO_DOM ?..80
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:O75880"
FT TRANSMEM 81..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..284
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:O75880"
FT REGION 46..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..114
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT DISULFID 152..156
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MUTAGEN 115
FT /note="G->S: Knockin mice hearts exhibit a severe combined
FT COX and copper deficiency and a mislocalization of copper
FT transporter protein CTR1 to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:28973536"
SQ SEQUENCE 284 AA; 31617 MW; 9CEC7E19F9977FF5 CRC64;
MAALVRAAVV RSQCRQLWRL FPRGHGLRDV AERPRPEEAC SCLRSRAFSA GPPPPGAGPE
PKGGQAGSHR PKPGPVSWKS LALTFAIGGS LLAGMKYFKK EKIEKLEKQR HRSIGKPLLG
GPFSLTTHNG EPKTDKDYLG QWVLIYFGFT HCPDICPEEL EKMIEVVEEI DSIPSLPNLT
PLFITIDPER DTKEAIATYV KEFSPKLVGL TGTKEEIDGV ARAYRVYYSP GPKDEDEDYI
VDHTIIMYLI GPDGEFLDYF GQNKKKAEIA GSIAAHMRSH MKKR
