NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1006/bbrc.2001.5440; PubMed=11549257 [NCBI, ExPASy, EBI, Israel, Japan]
Musard J.-F., Sallot M., Dulieu P., Fraichard A., Ordener C., Remy-Martin J.-P., Jouvenot M., Adami P.;
"Identification and expression of a new sulfhydryl oxidase SOx-3 during the cell cycle and the estrus cycle in uterine cells.";
Biochem. Biophys. Res. Commun. 287:83-91(2001).

Comments

FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins (By similarity).
CATALYTIC ACTIVITY: 4 R'C(R)SH + O₂ = 2 R'C(R)S-S(R)CR' + 2 H₂O.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Secreted. Note=Found in the extracellular medium.
TISSUE SPECIFICITY: Expressed in testis, placenta, pancreas, lung, ovary, endometrium, but not in brain, liver and kidney tissues. Higher expression in epithelial cells.
SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
SIMILARITY: Contains 1 ERV/ALR sulfhydryl oxidase domain.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U82982; AAB58401.2; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC7762; JC7762.

3D structure databases

ModBase

O08841.

Ontologies

GO:0005615;	Cellular component: extracellular space (inferred from sequence or structural similarity from UniProtKB).
GO:0030173;	Cellular component: integral to Golgi membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0016971;	Molecular function: flavin-linked sulfhydryl oxidase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
GO:0006467;	Biological process: protein thiol-disulfide exchange (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR006863; Evr1_Alr.
IPR006662; Thioredoxin-like.
IPR013766; Thioredoxin_dom.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.120.310; Evr1_Alr; 1.
G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF04777; Evr1_Alr; 1.
PF00085; Thioredoxin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00421; THIOREDOXIN.

PROSITE

PS51324; ERV_ALR; 1.
PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

Phylogenomic databases

HOVERGEN

O08841; -.

Other

ProtoNet

O08841.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 30`	`30`	`Potential.`
`CHAIN`	`31 613`	`583`	`Sulfhydryl oxidase 1.`	`PRO_0000249536`
`DOMAIN`	`37 157`	`121`	`Thioredoxin.`
`DOMAIN`	`397 504`	`108`	`ERV/ALR sulfhydryl oxidase.`
`CARBOHYD`	`131 131`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`244 244`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 613 AA [This is the length of the unprocessed precursor]

Molecular weight: 68595 Da [This is the MW of the unprocessed precursor]

CRC64: 34105EF608CA7B55 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTGCGRRSGW LPPLRLLLLP LLLGGPGVGA AQLAALYSAS DPLTLLQADT VRSTVLNSPS 

        70         80         90        100        110        120 
AWAVEFFASW CGHCIAFAPT WKALAKDIKD WRPALNLAAL NCADETNNAV CRDFNIAGFP 

       130        140        150        160        170        180 
SVRFFKAFSK NSTGTTLPVA GANVQMLRER LIDALESHHD TWPSACPPLE PVKPKEIDTF 

       190        200        210        220        230        240 
FARNNQEYLV LIFEQENSYL GREVTLDLSQ HHDLVVRRVL STEANVVRKF GVADFPSCYL 

       250        260        270        280        290        300 
LFRNGSVSRV PVLVESRRFY TAYLQRLSEV TREGTPTPAV PTISDQIAPT VWKFADRSKI 

       310        320        330        340        350        360 
YMADLESALH YILRVEVGRF SVLEGQRLMA LKKFVTVLTK YFPGQPLVRN FLQSTNEWLK 

       370        380        390        400        410        420 
RQHKKKMPYS FFKTAMDSRN EEAVITKEVN WVGCQGSESH FRGFPCSLWI LFHFLTVQAS 

       430        440        450        460        470        480 
QKNAESSQKP ANGQEVLQAI RNYVRFFFGC RDCANHFEQM AAGSMHRVKS PNDAVLWLWT 

       490        500        510        520        530        540 
SHNRVNARLA GAPSEDPQFP KVQWPPPELC SACHNELSGE PVWDVDATLR FLKTHFSPSN 

       550        560        570        580        590        600 
IVLNFPPAEP ASRSSVHSWG ATPHLELDAL GLVTRNSALA LERAEISESP GSNAMPNIPA 

       610 
ERPELFEALS HSR

O08841 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools