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Q9Y806 (ERV2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
FAD-linked sulfhydryl oxidase erv2

EC=1.8.3.2
Gene names
Name:erv2
ORF Names:SPBC146.04
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation in the endoplasmic reticulum lumen By similarity.

Catalytic activity

2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2.

Cofactor

FAD By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type III membrane protein; Lumenal side By similarity. Cytoplasm. Nucleus Ref.2.

Sequence similarities

Contains 1 ERV/ALR sulfhydryl oxidase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 192192FAD-linked sulfhydryl oxidase erv2
PRO_0000339122

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2921Helical; Signal-anchor; Potential
Topological domain30 – 192163Lumenal Potential
Domain61 – 162102ERV/ALR sulfhydryl oxidase
Region66 – 749FAD-binding By similarity
Region141 – 16222FAD-binding By similarity

Amino acid modifications

Disulfide bond138 ↔ 155 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Y806 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A14DCB3F731AB47B

FASTA19222,389
        10         20         30         40         50         60 
MILNRRIQVI LPTLLILSFI IWIFHSVMVD KDWRLFMPEI KSLPDREGQG RKPIEMMSTK 

        70         80         90        100        110        120 
HDNNTNNLMV NAYWKLIHTV VSNYPNRPTL DERDILRHYL FSSAITMPCG EYSVELQKIL 

       130        140        150        160        170        180 
DVHPPQTSSR KAATTWACKV HNQLNEKMNQ PKTSCDGFNE RYVIGSPTYR ESEAENVPER 

       190 
VQVINEDHDY SG 

« Hide

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. expand/collapse author list , 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: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAB46757.1.
PIRT39418.
RefSeqNP_595393.1. NM_001021300.1.

3D structure databases

HSSPHSSP built from PDB template 1JR8 based on UniProtKB Q12284.
ProteinModelPortalQ9Y806.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC146.04.1; SPBC146.04.1:pep; SPBC146.04.
GeneID2539721.
GenomeReviewsGene locus erv2 in contig CU329671_GR.
KEGGspo:SPBC146.04.
NMPDRfig|4896.1.peg.1259.

Organism-specific databases

GeneDB_SpombeSPBC146.04.

Phylogenomic databases

eggNOGfuNOG10324.
GeneTreeEFGT00050000003949.
OrthoDBEOG4DRDNC.

Gene expression databases

ArrayExpressQ9Y806.

Family and domain databases

InterProIPR017905. ERV/ALR_sulphydryl_oxidase.
IPR006863. Evr1_Alr.
[Graphical view]
Gene3DG3DSA:1.20.120.310. Evr1_Alr. 1 hit.
PfamPF04777. Evr1_Alr. 1 hit.
[Graphical view]
SUPFAMSSF69000. Evr1_Alr. 1 hit.
PROSITEPS51324. ERV_ALR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameERV2_SCHPO
AccessionPrimary (citable) accession number: Q9Y806
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: November 1, 1999
Last modified: December 14, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families