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Reviewed, UniProtKB/Swiss-Prot Q3TMX7 (QSOX2_MOUSE)

Last modified June 16, 2009. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sulfhydryl oxidase 2
    EC=1.8.3.2
Alternative name(s):
    Quiescin Q6-like protein 1
Gene names
Name: Qsox2
Synonyms: Qscn6l1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length692 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 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 Potential.

Subcellular location

Membrane; Single-pass membrane protein By similarity.

Sequence similarities

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

Contains 1 ERV/ALR sulfhydryl oxidase domain.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionthiol oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3TMX7-1)

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: Q3TMX7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     574-666: EWEAQGREQE...LCVVLYVASS → SVLRARPWLG...WSVSLRIGPI
     667-692: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q3TMX7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-165: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838 Potential
Chain39 – 692654Sulfhydryl oxidase 2
PRO_0000249539

Regions

Transmembrane656 – 67621 Potential
Domain54 – 172119Thioredoxin
Domain415 – 524110ERV/ALR sulfhydryl oxidase

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 165165Missing in isoform 3.
VSP_020500
Alternative sequence574 – 66693EWEAQ…YVASS → SVLRARPWLGQMARLSHVNL LPHFPVEEVSSLKPGVLCLK TNKPRSSLGVSKDEHSWSVS LRIGPI in isoform 2.
VSP_020501
Alternative sequence667 – 69226Missing in isoform 2.
VSP_020502

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 3BDC7058817484A1

FASTA69277,775
        10         20         30         40         50         60 
MAAARAVARD PGAYARQPPS LRAARLPRLL FLLAVVAAVG PREGGGARLY REGSDAVWLL 

        70         80         90        100        110        120 
DSGSVRSATG NSSAAWLVQF HSSWCGHCIG YAPTWRALAA DVRDWAAAIR VAALDCAEEK 

       130        140        150        160        170        180 
NQDVCRTYDI HFYPTFRYFK AFTKEFTTGE NFKGPDRELR TVRQTMIDFL QNHTEGTWPP 

       190        200        210        220        230        240 
ACPPLDPIQS SDILSFMDSH SGQYHAIVFE SNGSYVGREV ILDLIPYENI MVSRALDTDK 

       250        260        270        280        290        300 
AFLGTLGITS VPSCYLIYPN GSHGLVNVAK PLRSFFSSHL KSLPDVRKKS LFLPEKSNKE 

       310        320        330        340        350        360 
EKSEVVVWKE FDRAKLYTAD LESGLHYLLR VELAAHRSLA GAQLKTFRDF VTVVAKLFPG 

       370        380        390        400        410        420 
RPAVKKLLET LQEWLANLPL DKIPYNAILD LVNNKMQISG IFLTSHVKWV GCQGSRLELR 

       430        440        450        460        470        480 
GYPCSLWKLF HTLTVQASTH PEALAGTGFE GHPQAVLQAI RRYIRTFFGC KECGEHFEEM 

       490        500        510        520        530        540 
AKESMDSVKT PDQAVLWLWR KHNMVNSRLA GHLSEDPKFP KVPWPTPDLC PACHEEIKGL 

       550        560        570        580        590        600 
DSWNEGQVLL FLKQHYSRDN LVDAYSVDQG SPGEWEAQGR EQEEGKGLNP SGKSWRHHDT 

       610        620        630        640        650        660 
GSLRPPHILG PRTDLSKSLH HRLDLRLQSP QGPQALKEAK AVVPFLGVGF SSLDMSLCVV 

       670        680        690 
LYVASSLFLM IMYFFFRVRS KRWKVRLYHP AV 

« Hide

Isoform 2.

Checksum: B61C2ECE6ABC6477
Show »

FASTA63971,477
Isoform 3.

Checksum: 56976D2DF52B8BD2
Show »

FASTA52759,568

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Strain: C57BL/6J.
Tissue: Adipose tissue, Inner ear and Thymus.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: FVB/N.
Tissue: Salivary gland.

Cross-references

Sequence databases

AK042036 mRNA. Translation: BAC31140.1. Sequence problems.
AK140324 mRNA. Translation: BAE24335.1.
AK157992 mRNA. Translation: BAE34304.1.
AK165642 mRNA. Translation: BAE38312.1.
BC030934 mRNA. Translation: AAH30934.1.
IPIIPI00169589.
IPI00474916.
IPI00788406.
UniGeneMm.116769

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ3TMX7.

Genome annotation databases

EnsemblENSMUSG00000036327. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:2387194. Qsox2.

Phylogenomic databases

HOVERGENQ3TMX7.
OMAQ3TMX7. EEMATES.

Enzyme and pathway databases

BRENDA1.8.3.2. 244.

Gene expression databases

BgeeQ3TMX7.
CleanExMM_QSOX2.
GermOnlineENSMUSG00000036327. Mus musculus.

Family and domain databases

InterProIPR017905. ERV/ALR_sulphydryl_oxidase.
IPR006863. Evr1_Alr.
IPR017936. Thioredoxin-like.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:1.20.120.310. Evr1_Alr. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF04777. Evr1_Alr. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
PROSITEPS51324. ERV_ALR. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameQSOX2_MOUSE
AccessionPrimary (citable) accession number: Q3TMX7
Secondary accession number(s): Q3TZA5, Q8C9I4, Q8K0M2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: October 11, 2005
Last modified: June 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents