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Protein

Sulfhydryl oxidase 1

Gene

QSOX1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei80 – 801NucleophileBy similarity
Active sitei83 – 831NucleophileBy similarity
Binding sitei415 – 4151FADBy similarity
Binding sitei422 – 4221FADBy similarity
Binding sitei426 – 4261FADBy similarity
Binding sitei461 – 4611FADBy similarity
Binding sitei465 – 4651FADBy similarity
Binding sitei510 – 5101FADBy similarity
Binding sitei513 – 5131FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi488 – 4958FADBy similarity

GO - Molecular functioni

  1. flavin-linked sulfhydryl oxidase activity Source: UniProtKB
  2. protein disulfide isomerase activity Source: UniProtKB

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfhydryl oxidase 1 (EC:1.8.3.2)
Alternative name(s):
Quiescin Q6
Gene namesi
Name:QSOX1
Synonyms:QSCN6, QSOX, SOX
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei707 – 72721HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. extracellular vesicular exosome Source: Ensembl
  3. integral component of Golgi membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242Sequence AnalysisAdd
BLAST
Chaini43 – 743701Sulfhydryl oxidase 1PRO_0000249537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi80 ↔ 83Redox-activePROSITE-ProRule annotation
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi407 ↔ 419PROSITE-ProRule annotation
Disulfide bondi459 ↔ 462PROSITE-ProRule annotation
Disulfide bondi519 ↔ 522PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ8JGM4.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

ExpressionAtlasiQ8JGM4. baseline.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi9031.ENSGALP00000006256.

Structurei

3D structure databases

ProteinModelPortaliQ8JGM4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 166124ThioredoxinPROSITE-ProRule annotationAdd
BLAST
Domaini410 – 513104ERV/ALR sulfhydryl oxidasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi578 – 60326Glu-richAdd
BLAST
Compositional biasi680 – 6845Poly-Glu

Sequence similaritiesi

Contains 1 ERV/ALR sulfhydryl oxidase domain.PROSITE-ProRule annotation
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG237986.
HOGENOMiHOG000231631.
HOVERGENiHBG080360.
InParanoidiQ8JGM4.
KOiK10758.
PhylomeDBiQ8JGM4.

Family and domain databases

Gene3Di1.20.120.310. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR017905. ERV/ALR_sulphydryl_oxidase.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF04777. Evr1_Alr. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF69000. SSF69000. 1 hit.
PROSITEiPS51324. ERV_ALR. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8JGM4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWRRRARSGG GGGGGGGGAA PRCRWWPAVL ALLAAALPAA RSRSLYSPSD
60 70 80 90 100
PLELLGADTA ERRLLGSPSA WAVEFFASWC GHCIHFAPTW RALAEDVREW
110 120 130 140 150
RPAVMIAALD CADEANQQVC ADFGITGFPT LKFFRAFSKK AEDGIRIAHP
160 170 180 190 200
TATVADLRRA IITNLEQSGD AWPPACPPLE PASAEEVRSF FHRNTERYLA
210 220 230 240 250
LIFEQSNSFV GREVALDLLQ YENVAVRRVL SSEEELVEKF GVTTFPSAYL
260 270 280 290 300
LLRNGSFSRL PVHAEARSFY TYYLQTLSGV TRGSYRLNVT GSAINETRAL
310 320 330 340 350
QPAQADRSKV YVADLESTVH YTLRVEAGRP AVLAGAQLAA LKCYVATLAK
360 370 380 390 400
YFPGRPSVQT FLQSLDSWLR NWTEPELPRS ALKEAVKNKE DASPAAVLPT
410 420 430 440 450
NVTWVGCRGS EPHFRGYPCG LWTIFHLLTV QAAQGGPDEE LPLEVLNTMR
460 470 480 490 500
CYVKHFFGCQ ECAQHFEAMA AKSMDQVKSR REAVLWLWSH HNEVNARLAG
510 520 530 540 550
GDTEDPQFPK LQWPPPDMCP QCHREERGVH TWDEAAVLSF LKEHFSLGNL
560 570 580 590 600
YLDHAIPIPM AGEEAAASAR LSTAGLREKE EEERKEEEEE GEKETEKPHR
610 620 630 640 650
EGETGRPGSS ELRRPSIVRR NPRLRALGED IVDLDSFSEQ HFKSKALRAA
660 670 680 690 700
GRHRRLSKRD TVALHHDAGW ERLQVPESRE EEEEGGVLRR SPWLRVLGLG
710 720 730 740
FSRLDVSLCI ALYFLSSMCL LGMYTFFRLR TRARKGRPGF PVA
Length:743
Mass (Da):83,079
Last modified:October 1, 2002 - v1
Checksum:i44512B7EBB0B9769
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY112666 mRNA. Translation: AAM44079.1.
RefSeqiNP_989456.1. NM_204125.1.
UniGeneiGga.148.

Genome annotation databases

GeneIDi373914.
KEGGigga:373914.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY112666 mRNA. Translation: AAM44079.1.
RefSeqiNP_989456.1. NM_204125.1.
UniGeneiGga.148.

3D structure databases

ProteinModelPortaliQ8JGM4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000006256.

Proteomic databases

PRIDEiQ8JGM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi373914.
KEGGigga:373914.

Organism-specific databases

CTDi5768.

Phylogenomic databases

eggNOGiNOG237986.
HOGENOMiHOG000231631.
HOVERGENiHBG080360.
InParanoidiQ8JGM4.
KOiK10758.
PhylomeDBiQ8JGM4.

Miscellaneous databases

NextBioi20813446.
PROiQ8JGM4.

Gene expression databases

ExpressionAtlasiQ8JGM4. baseline.

Family and domain databases

Gene3Di1.20.120.310. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR017905. ERV/ALR_sulphydryl_oxidase.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF04777. Evr1_Alr. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF69000. SSF69000. 1 hit.
PROSITEiPS51324. ERV_ALR. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes."
    Thorpe C., Hoober K.L., Raje S., Glynn N.M., Burnside J., Turi G.K., Coppock D.L.
    Arch. Biochem. Biophys. 405:1-12(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY.

Entry informationi

Entry nameiQSOX1_CHICK
AccessioniPrimary (citable) accession number: Q8JGM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: October 1, 2002
Last modified: February 4, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.