O75880 (SCO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein SCO1 homolog, mitochondrial

Gene names

Name:	SCO1
Synonyms:	SCOD1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX. Ref.8 Ref.10 Ref.11
Subunit structure	Homodimer. Ref.11
Subcellular location	Mitochondrion Ref.1.
Tissue specificity	Predominantly expressed in tissues characterized by high rates of oxidative phosphorylation (OxPhos), including muscle, heart, and brain. Ref.1
Involvement in disease	Mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental delay, delayed motor development and mental retardation. Some affected individuals manifest a fatal hypertrophic cardiomyopathy resulting in neonatal death. A subset of patients manifest Leigh syndrome. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.13
Sequence similarities	Belongs to the SCO1/2 family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	Copper Metal-binding
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular copper ion homeostasis Inferred from electronic annotation. Source: InterPro copper ion transport Inferred from electronic annotation. Source: InterPro generation of precursor metabolites and energy Traceable author statement Ref.1. Source: ProtInc respiratory chain complex IV assembly Traceable author statement Ref.1. Source: ProtInc
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: InterPro mitochondrion Traceable author statement Ref.1. Source: ProtInc
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion Potential

Chain

? – 301

Protein SCO1 homolog, mitochondrial

PRO_0000031921

Regions

Region

118 – 131

14

Important for dimerization

Sites

Metal binding

169

1

Copper

Metal binding

173

1

Copper

Metal binding

260

1

Copper

Natural variations

Natural variant

58

1

P → S.
Corresponds to variant rs1802083 [ dbSNP | Ensembl ].

VAR_014537

Natural variant

174

1

P → L in MT-C4D. Ref.8 Ref.13

VAR_012109

Secondary structure

1

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301

Helix Strand Turn

Details...

Beta strand

141 – 144

4

Beta strand

149 – 151

3

Helix

152 – 155

4

Beta strand

159 – 165

7

Helix

172 – 189

18

Beta strand

190 – 193

4

Beta strand

196 – 203

8

Turn

205 – 207

3

Helix

210 – 218

9

Beta strand

225 – 228

4

Helix

231 – 239

9

Turn

240 – 242

3

Beta strand

245 – 250

6

Helix

252 – 254

3

Beta strand

256 – 260

5

Beta strand

263 – 267

5

Helix

269 – 271

3

Beta strand

273 – 278

6

Helix

283 – 294

12

Helix

295 – 297

3

Sequences

	Sequence		Length	Mass (Da)
	O75880 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: C4A0F35A1741894F	FASTA	301	33,814
	10 20 30 40 50 60 MAMLVLVPGR VMRPLGGQLW RFLPRGLEFW GPAEGTARVL LRQFCARQAE AWRASGRPGY 70 80 90 100 110 120 CLGTRPLSTA RPPPPWSQKG PGDSTRPSKP GPVSWKSLAI TFAIGGALLA GMKHVKKEKA 130 140 150 160 170 180 EKLEKERQRH IGKPLLGGPF SLTTHTGERK TDKDYLGQWL LIYFGFTHCP DVCPEELEKM 190 200 210 220 230 240 IQVVDEIDSI TTLPDLTPLF ISIDPERDTK EAIANYVKEF SPKLVGLTGT REEVDQVARA 250 260 270 280 290 300 YRVYYSPGPK DEDEDYIVDH TIIMYLIGPD GEFLDYFGQN KRKGEIAASI ATHMRPYRKK S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain." Petruzzella V., Tiranti V., Fernandez P., Ianna P., Carrozzo R., Zeviani M. Genomics 54:494-504(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency." Horvath R., Lochmuller H., Stucka R., Yao J., Shoubridge E.A., Kim S.-H., Gerbitz K.-D., Jaksch M. Biochem. Biophys. Res. Commun. 276:530-533(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"A novel gene expressed in human adrenal gland." Peng Y., Li Y., Tu Y., Xu S., Han Z., Fu G., Chen Z. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Adrenal gland.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[7]	Mei G., Yu W., Gibbs R.A. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-301. Tissue: Brain.
[8]	"The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis." Leary S.C., Cobine P.A., Kaufman B.A., Guercin G.H., Mattman A., Palaty J., Lockitch G., Winge D.R., Rustin P., Horvath R., Shoubridge E.A. Cell Metab. 5:9-20(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CHARACTERIZATION OF VARIANT MT-C4D LEU-174.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase 'assembly' protein." Williams J.C., Sue C., Banting G.S., Yang H., Glerum D.M., Hendrickson W.A., Schon E.A. J. Biol. Chem. 280:15202-15211(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 138-301, FUNCTION.
[11]	"A hint for the function of human Sco1 from different structures." Banci L., Bertini I., Calderone V., Ciofi-Baffoni S., Mangani S., Martinelli M., Palumaa P., Wang S. Proc. Natl. Acad. Sci. U.S.A. 103:8595-8600(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 132-301 IN COMPLEX WITH METAL IONS, FUNCTION, MASS SPECTROMETRY, SUBUNIT.
[12]	"Cytochrome c oxidase deficiency." Shoubridge E.A. Am. J. Med. Genet. 106:46-52(2001) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON MT-C4D.
[13]	"Mutations of the SCO1 gene in mitochondrial cytochrome c oxidase deficiency with neonatal-onset hepatic failure and encephalopathy." Valnot I., Osmond S., Gigarel N., Mehaye B., Amiel J., Cormier-Daire V., Munnich A., Bonnefont J.-P., Rustin P., Rotig A. Am. J. Hum. Genet. 67:1104-1109(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MT-C4D LEU-174.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF026852 mRNA. Translation: AAD08641.1.
AF295386 , AF295381, AF295382, AF295383, AF295384, AF295385 Genomic DNA. Translation: AAG23836.1.
AF183424 mRNA. Translation: AAG09693.1.
AK315595 mRNA. Translation: BAG37967.1.
CH471108 Genomic DNA. Translation: EAW89997.1.
BC015504 mRNA. Translation: AAH15504.1.
AF131816 mRNA. Translation: AAD20051.1.

IPI

IPI00027233.

RefSeq

NP_004580.1. NM_004589.2.

UniGene

Hs.14511.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WP0	X-ray	2.80	A/B/C	138-301	[»]
2GGT	X-ray	2.40	A/B	135-298	[»]
2GQK	NMR	-	A	132-301	[»]
2GQL	NMR	-	A	132-301	[»]
2GQM	NMR	-	A	132-301	[»]
2GT5	NMR	-	A	132-301	[»]
2GT6	NMR	-	A	132-301	[»]
2GVP	NMR	-	A	132-301	[»]
2HRF	NMR	-	A	132-301	[»]
2HRN	NMR	-	A	132-301	[»]

ProteinModelPortal

O75880.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46086N.

STRING

9606.ENSP00000255390.

PTM databases

PhosphoSite

O75880.

Proteomic databases

PaxDb

O75880.

PRIDE

O75880.

Protocols and materials databases

DNASU

6341.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000255390; ENSP00000255390; ENSG00000133028.

GeneID

6341.

KEGG

hsa:6341.

UCSC

uc002gmr.4. human.

Organism-specific databases

CTD

6341.

GeneCards

GC17M010583.

HGNC

HGNC:10603. SCO1.

HPA

HPA021565.
HPA021579.

MIM

220110. phenotype.
603644. gene.

neXtProt

NX_O75880.

Orphanet

1561. Fatal infantile cytochrome C oxidase deficiency.

PharmGKB

PA35012.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1999.

HOGENOM

HOG000258140.

HOVERGEN

HBG000428.

InParanoid

O75880.

KO

K07152.

OMA

FSLTTHT.

OrthoDB

EOG45DWQG.

PhylomeDB

O75880.

Gene expression databases

Bgee

O75880.

CleanEx

HS_SCO1.

Genevestigator

O75880.

GermOnline

ENSG00000133028. Homo sapiens.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR003782. SCO1/SenC.
IPR017276. Synth_of_cyt-c-oxidase_Sco1/2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

PANTHER

PTHR12151. PTHR12151. 1 hit.

Pfam

PF02630. SCO1-SenC. 1 hit.
[Graphical view]

PIRSF

PIRSF037736. SCO1. 1 hit.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O75880.

GenomeRNAi

6341.

NextBio

24624.

SOURCE

Search...

Entry information

Entry name

SCO1_HUMAN

Accession

Primary (citable) accession number: O75880
Secondary accession number(s): B2RDM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.