NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
DOI=10.1016/S0003-9861(02)00337-5; PubMed=12176051 [NCBI, ExPASy, EBI, Israel, Japan]
Thorpe C., Hoober K.L., Raje S., Glynn N.M., Burnside J., Turi G.K., Coppock D.L.;
"Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes.";
Arch. Biochem. Biophys. 405:1-12(2002).

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: Homodimer.
SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass membrane protein (By similarity).
TISSUE SPECIFICITY: Expressed in testis, placenta, pancreas, lung, ovary, endometrium, but not in brain, liver and kidney tissues. Higher expression in epithelial cells. Highly expressed in the active secretory tissue of the oviduct.
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

AY112666; AAM44079.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_989456.1; -.

UniGene

Gga.148

3D structure databases

HSSP

P09856; 1F9M. [HSSP ENTRY / PDB]

ModBase

Q8JGM4.

Ontologies

GO:0005615;	Cellular component: extracellular space (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).

ProtoNet

Q8JGM4.

Genome annotation databases

Ensembl

ENSGALG00000003933; Gallus gallus. [Contig view]

GeneID

373914; -.

KEGG

gga:373914; -.

Phylogenomic databases

HOVERGEN

Q8JGM4; -.

Other

UniRef

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

Keywords

FAD; Flavoprotein; Glycoprotein; Golgi apparatus; Membrane; Oxidoreductase; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 42`	`42`	`Potential.`
`CHAIN`	`43 743`	`701`	`Sulfhydryl oxidase 1.`	`PRO_0000249537`
`TRANSMEM`	`707 727`	`21`	`Potential.`
`DOMAIN`	`43 166`	`124`	`Thioredoxin.`
`DOMAIN`	`410 513`	`104`	`ERV/ALR sulfhydryl oxidase.`
`COMPBIAS`	`578 603`	`26`	`Glu-rich.`
`COMPBIAS`	`680 684`	`5`	`Poly-Glu.`
`CARBOHYD`	`254 254`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`288 288`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`295 295`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`371 371`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`401 401`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 743 AA [This is the length of the unprocessed precursor]

Molecular weight: 83079 Da [This is the MW of the unprocessed precursor]

CRC64: 44512B7EBB0B9769 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MWRRRARSGG GGGGGGGGAA PRCRWWPAVL ALLAAALPAA RSRSLYSPSD PLELLGADTA 

        70         80         90        100        110        120 
ERRLLGSPSA WAVEFFASWC GHCIHFAPTW RALAEDVREW RPAVMIAALD CADEANQQVC 

       130        140        150        160        170        180 
ADFGITGFPT LKFFRAFSKK AEDGIRIAHP TATVADLRRA IITNLEQSGD AWPPACPPLE 

       190        200        210        220        230        240 
PASAEEVRSF FHRNTERYLA LIFEQSNSFV GREVALDLLQ YENVAVRRVL SSEEELVEKF 

       250        260        270        280        290        300 
GVTTFPSAYL LLRNGSFSRL PVHAEARSFY TYYLQTLSGV TRGSYRLNVT GSAINETRAL 

       310        320        330        340        350        360 
QPAQADRSKV YVADLESTVH YTLRVEAGRP AVLAGAQLAA LKCYVATLAK YFPGRPSVQT 

       370        380        390        400        410        420 
FLQSLDSWLR NWTEPELPRS ALKEAVKNKE DASPAAVLPT NVTWVGCRGS EPHFRGYPCG 

       430        440        450        460        470        480 
LWTIFHLLTV QAAQGGPDEE LPLEVLNTMR CYVKHFFGCQ ECAQHFEAMA AKSMDQVKSR 

       490        500        510        520        530        540 
REAVLWLWSH HNEVNARLAG GDTEDPQFPK LQWPPPDMCP QCHREERGVH TWDEAAVLSF 

       550        560        570        580        590        600 
LKEHFSLGNL YLDHAIPIPM AGEEAAASAR LSTAGLREKE EEERKEEEEE GEKETEKPHR 

       610        620        630        640        650        660 
EGETGRPGSS ELRRPSIVRR NPRLRALGED IVDLDSFSEQ HFKSKALRAA GRHRRLSKRD 

       670        680        690        700        710        720 
TVALHHDAGW ERLQVPESRE EEEEGGVLRR SPWLRVLGLG FSRLDVSLCI ALYFLSSMCL 

       730        740 
LGMYTFFRLR TRARKGRPGF PVA

Q8JGM4 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