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Database: UniProt
Entry: Q5SUC9
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Original site: Q5SUC9 
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   24-JAN-2024, entry version 124.
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; 10090-ENSMUSP00000090673; -.
DR   PeptideAtlas; Q5SUC9; -.
DR   ProteomicsDB; 255364; -.
DR   Pumba; Q5SUC9; -.
DR   Antibodypedia; 12932; 186 antibodies from 29 providers.
DR   Ensembl; ENSMUST00000092996.5; ENSMUSP00000090673.5; ENSMUSG00000069844.13.
DR   GeneID; 52892; -.
DR   KEGG; mmu:52892; -.
DR   UCSC; uc007jlu.1; mouse.
DR   AGR; MGI:106362; -.
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; 169656at2759; -.
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 75 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 173 other cell types or tissues.
DR   ExpressionAtlas; Q5SUC9; baseline and differential.
DR   GO; GO:0005743; C: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:0019371; P:cyclooxygenase pathway; IMP:MGI.
DR   GO; GO:0006878; P:intracellular copper ion homeostasis; IDA: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:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:MGI.
DR   GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP: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   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   PANTHER; PTHR12151:SF4; PROTEIN SCO1 HOMOLOG, MITOCHONDRIAL; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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
//
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