SCO1_HUMAN
ID SCO1_HUMAN Reviewed; 301 AA.
AC O75880; B2RDM0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Protein SCO1 homolog, mitochondrial;
DE Flags: Precursor;
GN Name=SCO1; Synonyms=SCOD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9878253; DOI=10.1006/geno.1998.5580;
RA Petruzzella V., Tiranti V., Fernandez P., Ianna P., Carrozzo R.,
RA Zeviani M.;
RT "Identification and characterization of human cDNAs specific to BCS1,
RT PET112, SCO1, COX15, and COX11, five genes involved in the formation and
RT function of the mitochondrial respiratory chain.";
RL Genomics 54:494-504(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11027508; DOI=10.1006/bbrc.2000.3495;
RA Horvath R., Lochmuller H., Stucka R., Yao J., Shoubridge E.A., Kim S.-H.,
RA Gerbitz K.-D., Jaksch M.;
RT "Characterization of human SCO1 and COX17 genes in mitochondrial
RT cytochrome-c-oxidase deficiency.";
RL Biochem. Biophys. Res. Commun. 276:530-533(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RA Peng Y., Li Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.;
RT "A novel gene expressed in human adrenal gland.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-301.
RC TISSUE=Brain;
RA Mei G., Yu W., Gibbs R.A.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND SUBUNIT.
RX PubMed=15229189; DOI=10.1093/hmg/ddh197;
RA Leary S.C., Kaufman B.A., Pellecchia G., Guercin G.H., Mattman A.,
RA Jaksch M., Shoubridge E.A.;
RT "Human SCO1 and SCO2 have independent, cooperative functions in copper
RT delivery to cytochrome c oxidase.";
RL Hum. Mol. Genet. 13:1839-1848(2004).
RN [9]
RP FUNCTION, AND CHARACTERIZATION OF VARIANT MC4DN4 LEU-174.
RX PubMed=17189203; DOI=10.1016/j.cmet.2006.12.001;
RA Leary S.C., Cobine P.A., Kaufman B.A., Guercin G.H., Mattman A., Palaty J.,
RA Lockitch G., Winge D.R., Rustin P., Horvath R., Shoubridge E.A.;
RT "The human cytochrome c oxidase assembly factors SCO1 and SCO2 have
RT regulatory roles in the maintenance of cellular copper homeostasis.";
RL Cell Metab. 5:9-20(2007).
RN [10]
RP FUNCTION, AND CHARACTERIZATION OF VARIANT MC4DN4 LEU-174.
RX PubMed=19336478; DOI=10.1093/hmg/ddp158;
RA Leary S.C., Sasarman F., Nishimura T., Shoubridge E.A.;
RT "Human SCO2 is required for the synthesis of CO II and as a thiol-
RT disulphide oxidoreductase for SCO1.";
RL Hum. Mol. Genet. 18:2230-2240(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP INTERACTION WITH COX20.
RX PubMed=24403053; DOI=10.1093/hmg/ddu003;
RA Bourens M., Boulet A., Leary S.C., Barrientos A.;
RT "Human COX20 cooperates with SCO1 and SCO2 to mature COX2 and promote the
RT assembly of cytochrome c oxidase.";
RL Hum. Mol. Genet. 23:2901-2913(2014).
RN [13]
RP INTERACTION WITH COA6.
RX PubMed=26160915; DOI=10.1093/hmg/ddv265;
RA Stroud D.A., Maher M.J., Lindau C., Voegtle F.N., Frazier A.E.,
RA Surgenor E., Mountford H., Singh A.P., Bonas M., Oeljeklaus S.,
RA Warscheid B., Meisinger C., Thorburn D.R., Ryan M.T.;
RT "COA6 is a mitochondrial complex IV assembly factor critical for biogenesis
RT of mtDNA-encoded COX2.";
RL Hum. Mol. Genet. 24:5404-5415(2015).
RN [14]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER LEU-67, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP IDENTIFICATION IN A COMPLEX WITH TMEM177; COA6; MT-CO2; COX20; COX18 AND
RP SCO2, AND INTERACTION WITH TMEM177 AND COX20.
RX PubMed=29154948; DOI=10.1016/j.bbamcr.2017.11.010;
RA Lorenzi I., Oeljeklaus S., Aich A., Ronsoer C., Callegari S., Dudek J.,
RA Warscheid B., Dennerlein S., Rehling P.;
RT "The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis.";
RL Biochim. Biophys. Acta 1865:323-333(2017).
RN [16]
RP INTERACTION WITH COX20.
RX PubMed=28330871; DOI=10.1074/jbc.m117.778514;
RA Bourens M., Barrientos A.;
RT "Human mitochondrial cytochrome c oxidase assembly factor COX18 acts
RT transiently as a membrane insertase within the subunit 2 maturation
RT module.";
RL J. Biol. Chem. 292:7774-7783(2017).
RN [17]
RP INTERACTION WITH COX16.
RX PubMed=29381136; DOI=10.7554/elife.32572;
RA Aich A., Wang C., Chowdhury A., Ronsoer C., Pacheu-Grau D.,
RA Richter-Dennerlein R., Dennerlein S., Rehling P.;
RT "COX16 promotes COX2 metallation and assembly during respiratory complex IV
RT biogenesis.";
RL Elife 7:0-0(2018).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 138-301, AND FUNCTION.
RX PubMed=15659396; DOI=10.1074/jbc.m410705200;
RA Williams J.C., Sue C., Banting G.S., Yang H., Glerum D.M.,
RA Hendrickson W.A., Schon E.A.;
RT "Crystal structure of human SCO1: implications for redox signaling by a
RT mitochondrial cytochrome c oxidase 'assembly' protein.";
RL J. Biol. Chem. 280:15202-15211(2005).
RN [19]
RP STRUCTURE BY NMR OF 132-301 IN COMPLEX WITH METAL IONS, FUNCTION, SUBUNIT,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16735468; DOI=10.1073/pnas.0601375103;
RA Banci L., Bertini I., Calderone V., Ciofi-Baffoni S., Mangani S.,
RA Martinelli M., Palumaa P., Wang S.;
RT "A hint for the function of human Sco1 from different structures.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8595-8600(2006).
RN [20]
RP REVIEW ON MC4DN4.
RX PubMed=11579424; DOI=10.1002/ajmg.1378;
RA Shoubridge E.A.;
RT "Cytochrome c oxidase deficiency.";
RL Am. J. Med. Genet. 106:46-52(2001).
RN [21]
RP VARIANT MC4DN4 LEU-174.
RX PubMed=11013136; DOI=10.1086/321202;
RA Valnot I., Osmond S., Gigarel N., Mehaye B., Amiel J., Cormier-Daire V.,
RA Munnich A., Bonnefont J.-P., Rustin P., Rotig A.;
RT "Mutations of the SCO1 gene in mitochondrial cytochrome c oxidase
RT deficiency with neonatal-onset hepatic failure and encephalopathy.";
RL Am. J. Hum. Genet. 67:1104-1109(2000).
RN [22]
RP CHARACTERIZATION OF VARIANT MC4DN4 LEU-174.
RX PubMed=17182746; DOI=10.1073/pnas.0606189103;
RA Banci L., Bertini I., Ciofi-Baffoni S., Leontari I., Martinelli M.,
RA Palumaa P., Sillard R., Wang S.;
RT "Human Sco1 functional studies and pathological implications of the P174L
RT mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15-20(2007).
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 (PubMed:15659396,
CC PubMed:16735468, PubMed:17189203, PubMed:19336478, PubMed:15229189).
CC Plays an important role in the regulation of copper homeostasis by
CC controlling the abundance and cell membrane localization of copper
CC transporter CTR1 (By similarity). {ECO:0000250|UniProtKB:Q5SUC9,
CC ECO:0000269|PubMed:15229189, ECO:0000269|PubMed:15659396,
CC ECO:0000269|PubMed:16735468, ECO:0000269|PubMed:17189203,
CC ECO:0000269|PubMed:19336478}.
CC -!- SUBUNIT: Homodimer (PubMed:16735468, PubMed:15229189). Interacts with
CC COA6 (PubMed:26160915). Found in a complex with TMEM177, COX20, COA6,
CC MT-CO2/COX2, COX18 and SCO2 (PubMed:29154948). Interacts with TMEM177
CC in a COX20-dependent manner (PubMed:29154948). Interacts with COX20 in
CC a MT-CO2/COX2- and COX18-dependent manner (PubMed:29154948,
CC PubMed:24403053, PubMed:28330871). Interacts with COX16
CC (PubMed:29381136). {ECO:0000269|PubMed:15229189,
CC ECO:0000269|PubMed:16735468, ECO:0000269|PubMed:24403053,
CC ECO:0000269|PubMed:26160915, ECO:0000269|PubMed:28330871,
CC ECO:0000269|PubMed:29154948, ECO:0000269|PubMed:29381136}.
CC -!- INTERACTION:
CC O75880; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-6656171, EBI-7062247;
CC O75880; P21964-2: COMT; NbExp=3; IntAct=EBI-6656171, EBI-10200977;
CC O75880; Q14061: COX17; NbExp=3; IntAct=EBI-6656171, EBI-711311;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9878253}.
CC Mitochondrion inner membrane {ECO:0000269|PubMed:15229189}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in tissues characterized by
CC high rates of oxidative phosphorylation (OxPhos), including muscle,
CC heart, and brain. {ECO:0000269|PubMed:9878253}.
CC -!- DISEASE: Mitochondrial complex IV deficiency, nuclear type 4 (MC4DN4)
CC [MIM:619048]: An autosomal recessive mitochondrial disorder
CC characterized by hypotonia, encephalopathy, metabolic acidosis, poor
CC feeding, hepatomegaly, and hypertrophic cardiomyopathy in some
CC patients. Death occurs in infancy. Patient tissues show decreased
CC levels and activity of mitochondrial respiratory complex IV.
CC {ECO:0000269|PubMed:11013136, ECO:0000269|PubMed:17182746,
CC ECO:0000269|PubMed:17189203, ECO:0000269|PubMed:19336478}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
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DR EMBL; AF026852; AAD08641.1; -; mRNA.
DR EMBL; AF295386; AAG23836.1; -; Genomic_DNA.
DR EMBL; AF295381; AAG23836.1; JOINED; Genomic_DNA.
DR EMBL; AF295382; AAG23836.1; JOINED; Genomic_DNA.
DR EMBL; AF295383; AAG23836.1; JOINED; Genomic_DNA.
DR EMBL; AF295384; AAG23836.1; JOINED; Genomic_DNA.
DR EMBL; AF295385; AAG23836.1; JOINED; Genomic_DNA.
DR EMBL; AF183424; AAG09693.1; -; mRNA.
DR EMBL; AK315595; BAG37967.1; -; mRNA.
DR EMBL; CH471108; EAW89997.1; -; Genomic_DNA.
DR EMBL; BC015504; AAH15504.1; -; mRNA.
DR EMBL; AF131816; AAD20051.1; -; mRNA.
DR CCDS; CCDS11158.1; -.
DR RefSeq; NP_004580.1; NM_004589.3.
DR RefSeq; XP_005256808.1; XM_005256751.3.
DR PDB; 1WP0; X-ray; 2.80 A; A/B/C=138-301.
DR PDB; 2GGT; X-ray; 2.40 A; A/B=135-298.
DR PDB; 2GQK; NMR; -; A=132-301.
DR PDB; 2GQL; NMR; -; A=132-301.
DR PDB; 2GQM; NMR; -; A=132-301.
DR PDB; 2GT5; NMR; -; A=132-301.
DR PDB; 2GT6; NMR; -; A=132-301.
DR PDB; 2GVP; NMR; -; A=132-301.
DR PDB; 2HRF; NMR; -; A=132-301.
DR PDB; 2HRN; NMR; -; A=132-301.
DR PDBsum; 1WP0; -.
DR PDBsum; 2GGT; -.
DR PDBsum; 2GQK; -.
DR PDBsum; 2GQL; -.
DR PDBsum; 2GQM; -.
DR PDBsum; 2GT5; -.
DR PDBsum; 2GT6; -.
DR PDBsum; 2GVP; -.
DR PDBsum; 2HRF; -.
DR PDBsum; 2HRN; -.
DR AlphaFoldDB; O75880; -.
DR SMR; O75880; -.
DR BioGRID; 112245; 151.
DR DIP; DIP-46086N; -.
DR IntAct; O75880; 124.
DR MINT; O75880; -.
DR STRING; 9606.ENSP00000255390; -.
DR DrugBank; DB09130; Copper.
DR iPTMnet; O75880; -.
DR PhosphoSitePlus; O75880; -.
DR BioMuta; SCO1; -.
DR EPD; O75880; -.
DR jPOST; O75880; -.
DR MassIVE; O75880; -.
DR MaxQB; O75880; -.
DR PaxDb; O75880; -.
DR PeptideAtlas; O75880; -.
DR PRIDE; O75880; -.
DR ProteomicsDB; 50236; -.
DR TopDownProteomics; O75880; -.
DR Antibodypedia; 12932; 164 antibodies from 29 providers.
DR DNASU; 6341; -.
DR Ensembl; ENST00000255390.10; ENSP00000255390.5; ENSG00000133028.12.
DR GeneID; 6341; -.
DR KEGG; hsa:6341; -.
DR MANE-Select; ENST00000255390.10; ENSP00000255390.5; NM_004589.4; NP_004580.1.
DR UCSC; uc002gmr.5; human.
DR CTD; 6341; -.
DR DisGeNET; 6341; -.
DR GeneCards; SCO1; -.
DR GeneReviews; SCO1; -.
DR HGNC; HGNC:10603; SCO1.
DR HPA; ENSG00000133028; Low tissue specificity.
DR MalaCards; SCO1; -.
DR MIM; 603644; gene.
DR MIM; 619048; phenotype.
DR neXtProt; NX_O75880; -.
DR OpenTargets; ENSG00000133028; -.
DR Orphanet; 1561; Fatal infantile cytochrome C oxidase deficiency.
DR PharmGKB; PA35012; -.
DR VEuPathDB; HostDB:ENSG00000133028; -.
DR eggNOG; KOG2792; Eukaryota.
DR GeneTree; ENSGT00390000004323; -.
DR HOGENOM; CLU_050131_0_3_1; -.
DR InParanoid; O75880; -.
DR OMA; IVAHMRP; -.
DR OrthoDB; 1462537at2759; -.
DR PhylomeDB; O75880; -.
DR TreeFam; TF313752; -.
DR PathwayCommons; O75880; -.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR SignaLink; O75880; -.
DR BioGRID-ORCS; 6341; 132 hits in 1097 CRISPR screens.
DR ChiTaRS; SCO1; human.
DR EvolutionaryTrace; O75880; -.
DR GeneWiki; SCO1; -.
DR GenomeRNAi; 6341; -.
DR Pharos; O75880; Tbio.
DR PRO; PR:O75880; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75880; protein.
DR Bgee; ENSG00000133028; Expressed in left ventricle myocardium and 168 other tissues.
DR ExpressionAtlas; O75880; baseline and differential.
DR Genevisible; O75880; HS.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0016531; F:copper chaperone activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IEA:InterPro.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP: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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Copper; Disease variant; Disulfide bond; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Primary mitochondrial disease; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..67
FT /note="Mitochondrion"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:25944712"
FT CHAIN 68..301
FT /note="Protein SCO1 homolog, mitochondrial"
FT /id="PRO_0000031921"
FT TOPO_DOM 68..92
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:15229189"
FT TRANSMEM 93..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..301
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:15229189"
FT REGION 63..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..131
FT /note="Important for dimerization"
FT BINDING 169
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 173
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 260
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT DISULFID 169..173
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VARIANT 58
FT /note="P -> S (in dbSNP:rs1802083)"
FT /id="VAR_014537"
FT VARIANT 174
FT /note="P -> L (in MC4DN4; no effect on synthesis of
FT cytochrome c oxidase subunit II; reduced stability of newly
FT synthesized cytochrome c oxidase subunit II; reduced
FT copper-binding; dbSNP:rs104894630)"
FT /evidence="ECO:0000269|PubMed:11013136,
FT ECO:0000269|PubMed:17182746, ECO:0000269|PubMed:17189203,
FT ECO:0000269|PubMed:19336478"
FT /id="VAR_012109"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2GGT"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2GGT"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:2GGT"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:2GGT"
FT HELIX 172..189
FT /evidence="ECO:0007829|PDB:2GGT"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:2GGT"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:2GGT"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2GGT"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:2GGT"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:2GGT"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:2GGT"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:2GGT"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2GGT"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1WP0"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:2GGT"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:2GGT"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:2GQL"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:2GGT"
FT HELIX 283..294
FT /evidence="ECO:0007829|PDB:2GGT"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2GGT"
SQ SEQUENCE 301 AA; 33814 MW; C4A0F35A1741894F CRC64;
MAMLVLVPGR VMRPLGGQLW RFLPRGLEFW GPAEGTARVL LRQFCARQAE AWRASGRPGY
CLGTRPLSTA RPPPPWSQKG PGDSTRPSKP GPVSWKSLAI TFAIGGALLA GMKHVKKEKA
EKLEKERQRH IGKPLLGGPF SLTTHTGERK TDKDYLGQWL LIYFGFTHCP DVCPEELEKM
IQVVDEIDSI TTLPDLTPLF ISIDPERDTK EAIANYVKEF SPKLVGLTGT REEVDQVARA
YRVYYSPGPK DEDEDYIVDH TIIMYLIGPD GEFLDYFGQN KRKGEIAASI ATHMRPYRKK
S
