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O00391 (QSOX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfhydryl oxidase 1

Short name=hQSOX
EC=1.8.3.2
Alternative name(s):
Quiescin Q6
Gene names
Name:QSOX1
Synonyms:QSCN6
ORF Names:UNQ2520/PRO6013
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length747 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. In fibroblasts, it may have tumor-suppressing capabilities being involved in growth regulation. Ref.2 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13

Catalytic activity

2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2. Ref.13

Cofactor

Binds 1 FAD per subunit. Ref.13 Ref.15

Subunit structure

Monomer. Ref.13 Ref.15

Subcellular location

Isoform 1: Golgi apparatus membrane; Single-pass membrane protein Ref.8 Ref.12.

Isoform 2: Secretedextracellular space. Note: Found in the extracellular medium of quiescent cells but is not found in proliferating cells. Ref.8 Ref.12

Tissue specificity

Expressed in heart, placenta, lung, liver, skeletal muscle, pancreas and very weakly in brain and kidney. Ref.8 Ref.9

Induction

Induced in quiescent cells just as fibroblasts begin to leave the proliferative cycle and enter quiescence. Ref.1 Ref.7 Ref.8

Miscellaneous

'Quiescin Q6' means that it was the sixth clone to be found at a higher level of expression in quiescent fibroblasts.

Sequence similarities

Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.

Contains 1 ERV/ALR sulfhydryl oxidase domain.

Contains 1 thioredoxin domain.

Sequence caution

The sequence BAD92517.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00391-1)

Also known as: a; QSOX-L;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O00391-2)

Also known as: b; QSOX-S;

The sequence of this isoform differs from the canonical sequence as follows:
     603-604: AS → LI
     605-747: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 747718Sulfhydryl oxidase 1
PRO_0000249533

Regions

Transmembrane710 – 73021Helical; Potential
Domain36 – 156121Thioredoxin
Domain396 – 503108ERV/ALR sulfhydryl oxidase
Nucleotide binding478 – 4858FAD

Sites

Active site701Nucleophile Probable
Active site731Nucleophile Probable
Binding site4011FAD
Binding site4081FAD
Binding site4121FAD
Binding site4511FAD
Binding site4551FAD
Binding site5001FAD
Binding site5031FAD

Amino acid modifications

Glycosylation1301N-linked (GlcNAc...) (complex) Ref.11 Ref.14
Glycosylation2431N-linked (GlcNAc...) Potential
Glycosylation5751N-linked (GlcNAc...) Potential
Disulfide bond70 ↔ 73Redox-active Probable
Disulfide bond393 ↔ 405 Ref.15
Disulfide bond449 ↔ 452 Ref.15
Disulfide bond509 ↔ 512 Ref.15

Natural variations

Alternative sequence603 – 6042AS → LI in isoform 2.
VSP_020489
Alternative sequence605 – 747143Missing in isoform 2.
VSP_020490
Natural variant1141N → S.
Corresponds to variant rs3894211 [ dbSNP | Ensembl ].
VAR_027429
Natural variant2001G → A. Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855475 [ dbSNP | Ensembl ].
VAR_027430
Natural variant2561R → M.
Corresponds to variant rs4360492 [ dbSNP | Ensembl ].
VAR_027431
Natural variant2941A → S.
Corresponds to variant rs2278943 [ dbSNP | Ensembl ].
VAR_027432
Natural variant4441H → R. Ref.2
Corresponds to variant rs12371 [ dbSNP | Ensembl ].
VAR_027433
Natural variant5911N → H.
Corresponds to variant rs3738115 [ dbSNP | Ensembl ].
VAR_027434
Natural variant6051R → P.
Corresponds to variant rs16855466 [ dbSNP | Ensembl ].
VAR_053652

Experimental info

Mutagenesis701C → S: Reduces activity by 93%. Ref.13
Mutagenesis731C → S: Reduces activity by 93%. Ref.13
Mutagenesis4491C → S: Reduces activity by 96%. Ref.13
Mutagenesis4521C → S: Loss of activity. Ref.13
Mutagenesis5091C → S: No effect. Reduces activity by 70%; when associated with S-512. Ref.13
Mutagenesis5121C → S: Reduces activity by 40%. Reduces activity by 70%; when associated with S-509. Ref.13

Secondary structure

.................................................................................... 747
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (a) (QSOX-L) [UniParc].

Last modified June 1, 2001. Version 3.
Checksum: 52639D09A50E00C5

FASTA74782,578
        10         20         30         40         50         60 
MRRCNSGSGP PPSLLLLLLW LLAVPGANAA PRSALYSPSD PLTLLQADTV RGAVLGSRSA 

        70         80         90        100        110        120 
WAVEFFASWC GHCIAFAPTW KALAEDVKAW RPALYLAALD CAEETNSAVC RDFNIPGFPT 

       130        140        150        160        170        180 
VRFFKAFTKN GSGAVFPVAG ADVQTLRERL IDALESHHDT WPPACPPLEP AKLEEIDGFF 

       190        200        210        220        230        240 
ARNNEEYLAL IFEKGGSYLG REVALDLSQH KGVAVRRVLN TEANVVRKFG VTDFPSCYLL 

       250        260        270        280        290        300 
FRNGSVSRVP VLMESRSFYT AYLQRLSGLT REAAQTTVAP TTANKIAPTV WKLADRSKIY 

       310        320        330        340        350        360 
MADLESALHY ILRIEVGRFP VLEGQRLVAL KKFVAVLAKY FPGRPLVQNF LHSVNEWLKR 

       370        380        390        400        410        420 
QKRNKIPYSF FKTALDDRKE GAVLAKKVNW IGCQGSEPHF RGFPCSLWVL FHFLTVQAAR 

       430        440        450        460        470        480 
QNVDHSQEAA KAKEVLPAIR GYVHYFFGCR DCASHFEQMA AASMHRVGSP NAAVLWLWSS 

       490        500        510        520        530        540 
HNRVNARLAG APSEDPQFPK VQWPPRELCS ACHNERLDVP VWDVEATLNF LKAHFSPSNI 

       550        560        570        580        590        600 
ILDFPAAGSA ARRDVQNVAA APELAMGALE LESRNSTLDP GKPEMMKSPT NTTPHVPAEG 

       610        620        630        640        650        660 
PEASRPPKLH PGLRAAPGQE PPEHMAELQR NEQEQPLGQW HLSKRDTGAA LLAESRAEKN 

       670        680        690        700        710        720 
RLWGPLEVRR VGRSSKQLVD IPEGQLEARA GRGRGQWLQV LGGGFSYLDI SLCVGLYSLS 

       730        740 
FMGLLAMYTY FQAKIRALKG HAGHPAA 

« Hide

Isoform 2 (b) (QSOX-S) [UniParc].

Checksum: B557EE4D1525E7FB
Show »

FASTA60466,861

References

« Hide 'large scale' references
[1]"The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1."
Coppock D.L., Cina-Poppe D., Gilleran S.
Genomics 54:460-468(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
Tissue: Lung.
[2]"Identification and expression of a new splicing variant of FAD-sulfhydryl oxidase in adult rat brain."
Radom J., Colin D., Thiebault F., Dognin-Bergeret M.J., Mairet-Coello G., Esnard-Feve A., Fellmann D., Jouvenot M.
Biochim. Biophys. Acta 1759:225-233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, VARIANTS ALA-200 AND ARG-444.
Tissue: Placenta.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-200.
Tissue: Brain.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ALA-200.
Tissue: Chondrosarcoma and Kidney.
[7]"Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases."
Hoober K.L., Glynn N.M., Burnside J., Coppock D.L., Thorpe C.
J. Biol. Chem. 274:31759-31762(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Regulation of the quiescence-induced genes: quiescin Q6, decorin, and ribosomal protein S29."
Coppock D.L., Kopman C., Gudas J., Cina-Poppe D.A.
Biochem. Biophys. Res. Commun. 269:604-610(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"The distribution and specificity of expression of quiescin Q6 (Q6) in Human tissues is associated with both endocrine and non-endocrine protein secretion."
Turi G.K.
Proc. Annu. Meet. Am. Assoc. Cancer Res. 42:397-397(2001)
Cited for: TISSUE SPECIFICITY.
[10]"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: FUNCTION, NOMENCLATURE, ALTERNATIVE SPLICING.
[11]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130.
Tissue: Plasma.
[12]"Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1."
Chakravarthi S., Jessop C.E., Willer M., Stirling C.J., Bulleid N.J.
Biochem. J. 404:403-411(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]"Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis."
Heckler E.J., Alon A., Fass D., Thorpe C.
Biochemistry 47:4955-4963(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, MUTAGENESIS OF CYS-70; CYS-73; CYS-449; CYS-452; CYS-509 AND CYS-512, ACTIVE SITE.
[14]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-130.
[15]"QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains."
Alon A., Heckler E.J., Thorpe C., Fass D.
FEBS Lett. 584:1521-1525(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 286-546 IN COMPLEX WITH FAD, SUBUNIT, COFACTOR, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U97276 mRNA. Translation: AAC09010.2.
AF361868 mRNA. Translation: AAM00263.1.
AY358941 mRNA. Translation: AAQ89300.1.
AB209280 mRNA. Translation: BAD92517.1. Different initiation.
AL390718 Genomic DNA. Translation: CAI14838.1.
AL390718 Genomic DNA. Translation: CAI14839.1.
BC017692 mRNA. Translation: AAH17692.1.
BC100023 mRNA. Translation: AAI00024.1.
RefSeqNP_001004128.1. NM_001004128.2.
NP_002817.2. NM_002826.4.
UniGeneHs.744925.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LLIX-ray2.05A286-546[»]
3LLKX-ray2.00A/B/C286-546[»]
3Q6OX-ray2.05A33-272[»]
4IJ3X-ray2.70A33-272[»]
ProteinModelPortalO00391.
SMRO00391. Positions 33-544.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111734. 4 interactions.
IntActO00391. 1 interaction.
MINTMINT-2862351.
STRING9606.ENSP00000356574.

PTM databases

PhosphoSiteO00391.

Proteomic databases

PaxDbO00391.
PeptideAtlasO00391.
PRIDEO00391.

Protocols and materials databases

DNASU5768.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367600; ENSP00000356572; ENSG00000116260. [O00391-2]
ENST00000367602; ENSP00000356574; ENSG00000116260. [O00391-1]
GeneID5768.
KEGGhsa:5768.
UCSCuc001gny.3. human. [O00391-2]
uc001gnz.3. human. [O00391-1]

Organism-specific databases

CTD5768.
GeneCardsGC01P180123.
HGNCHGNC:9756. QSOX1.
HPAHPA042127.
MIM603120. gene.
neXtProtNX_O00391.
PharmGKBPA162400559.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000231631.
HOVERGENHBG080360.
InParanoidO00391.
KOK10758.
OMASHNRVNA.
OrthoDBEOG73RB9X.
PhylomeDBO00391.
TreeFamTF316749.

Enzyme and pathway databases

BRENDA1.8.3.2. 2681.

Gene expression databases

ArrayExpressO00391.
BgeeO00391.
CleanExHS_QSOX1.
GenevestigatorO00391.

Family and domain databases

Gene3D1.20.120.310. 1 hit.
3.40.30.10. 1 hit.
InterProIPR017905. ERV/ALR_sulphydryl_oxidase.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF04777. Evr1_Alr. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
SSF69000. SSF69000. 1 hit.
PROSITEPS51324. ERV_ALR. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSQSOX1. human.
EvolutionaryTraceO00391.
GeneWikiQSOX1.
GenomeRNAi5768.
NextBio22434.
PROO00391.
SOURCESearch...

Entry information

Entry nameQSOX1_HUMAN
AccessionPrimary (citable) accession number: O00391
Secondary accession number(s): Q59G29 expand/collapse secondary AC list , Q5T2X0, Q8TDL6, Q8WVP4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM