Reviewed, UniProtKB/Swiss-Prot O14144 (ERV1_SCHPO)

Names and origin

Protein names

Recommended name:
    Mitochondrial FAD-linked sulfhydryl oxidase erv1
    EC=1.8.3.2

Gene names

Name:	erv1
ORF Names:	SPAC3G6.08

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	182 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS) By similarity.
Catalytic activity	4 R'C(R)SH + O2 = 2 R'C(R)S-S(R)CR' + 2 H2O.
Cofactor	FAD By similarity.
Subcellular location	Mitochondrion intermembrane space By similarity.
Sequence similarities	Contains 1 ERV/ALR sulfhydryl oxidase domain.

Ontologies

Keywords
Cellular component	Mitochondrion
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	thiol oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 182	182	Mitochondrial FAD-linked sulfhydryl oxidase erv1		PRO_0000339121
Regions
	Domain	75 – 177	103	ERV/ALR sulfhydryl oxidase
	Region	160 – 177	18	FAD-binding By similarity
Amino acid modifications
	Disulfide bond	122 ↔ 125		Redox-active By similarity
	Disulfide bond	153 ↔ 170		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O14144-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: C8756CB2022F4746	FASTA	182	20,769
	10 20 30 40 50 60 MVFGKRYRDK ETGIIYDENG RPCKTCNIFS SFRNVAQQPN SSTVPEVKSN TQLESKQSSI 70 80 90 100 110 120 DCNTNAIPDS VSFPRLPDVA ELGRSTWTFL HAMAANFPKN PTPTQQNDMS SFLYNFSKFY 130 140 150 160 170 180 PCWSCAEDLR IWMAKYGNSP RVDSRESLCE WICEAHNDVN ERLGKPLFNC QVWSKKASEL AD

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB16284.1.
PIR	T38727.
RefSeq	NP_594974.1.
3D structure databases
HSSP	HSSP built from PDB template 1OQC based on UniProtKB Q63042.
ModBase	Search...
Protein-protein interaction databases
STRING	O14144.
Genome annotation databases
GeneID	2543175.
GenomeReviews	Gene locus erv1 in contig CU329670_GR.
KEGG	spo:SPAC3G6.08.
NMPDR	fig|4896.1.peg.4944.
Organism-specific databases
GeneDB_Spombe	SPAC3G6.08.
Phylogenomic databases
OMA	GRSTWTF.
Gene expression databases
ArrayExpress	O14144.
Family and domain databases
InterPro	IPR017905. ERV/ALR_sulphydryl_oxidase. IPR006863. Evr1_Alr. [Graphical view]
Gene3D	G3DSA:1.20.120.310. Evr1_Alr. 1 hit.
Pfam	PF04777. Evr1_Alr. 1 hit. [Graphical view]
PROSITE	PS51324. ERV_ALR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ERV1_SCHPO

Accession

Primary (citable) accession number: O14144

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)