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Q9ZU40 (QSOX2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sulfhydryl oxidase 2

EC=1.8.3.2
Alternative name(s):
Quiescin-sulfhydryl oxidase 2
Short name=AtQSOX2
Gene names
Name:QSOX2
Ordered Locus Names:At2g01270
ORF Names:F10A8.15
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length495 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

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

Cofactor

FAD By similarity.

Subcellular location

Secreted By similarity.

Sequence similarities

Contains 1 ERV/ALR sulfhydryl oxidase domain.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – 495480Sulfhydryl oxidase 2
PRO_0000400051

Regions

Domain29 – 164136Thioredoxin
Domain290 – 392103ERV/ALR sulfhydryl oxidase
Nucleotide binding363 – 3708FAD By similarity

Sites

Active site661Nucleophile By similarity
Active site691Nucleophile By similarity
Binding site2951FAD By similarity
Binding site3021FAD By similarity
Binding site3061FAD By similarity
Binding site3361FAD By similarity
Binding site3401FAD By similarity
Binding site3891FAD By similarity
Binding site3921FAD By similarity

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation2571N-linked (GlcNAc...) Potential
Glycosylation2661N-linked (GlcNAc...) Potential
Glycosylation2921N-linked (GlcNAc...) Potential
Disulfide bond66 ↔ 69Redox-active By similarity
Disulfide bond287 ↔ 299 By similarity
Disulfide bond334 ↔ 337 By similarity
Disulfide bond398 ↔ 401 By similarity

Experimental info

Sequence conflict851G → D in AAK59679. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9ZU40 [UniParc].

Last modified June 1, 2002. Version 2.
Checksum: 2FBBFA72D9C0A95D

FASTA49555,919
        10         20         30         40         50         60 
MSLVHLLLFA GLVIAASSSS PGSRLILREI SDQKDKAVEL NTTNFDSVLK DTPAKYAVVE 

        70         80         90        100        110        120 
FFAHWCPACR NYKPHYEKVA RLFNGPDAIH PGIVLMTRVD CAMKTNTKLC DKFSVSHYPM 

       130        140        150        160        170        180 
LFWGPPTKFV SGSWEPKKDK SEILVIDDGR TAERLLNWIN KQIGSSYGLD DQKFKNEHAL 

       190        200        210        220        230        240 
SNLTDYNQIS QAVYDVEEAT AEAFDIILAH KAIKSSETSA SFIRFIQLLA AHHLSRRCRK 

       250        260        270        280        290        300 
GAAEILVNYD DLCPSGNCSY EKSGGNDTLG NFPICGKDVP RGYYMFCRGS KNDTRGFSCG 

       310        320        330        340        350        360 
LWVLMHSLSV RIEDGESHFA FTTICDFVNN FFMCDECRLH FNDMCLSVKT PFKKARDFVL 

       370        380        390        400        410        420 
WVWSTHNKVN ERLLKDEASL GTGDPKFPKI IWPPKELCPL CYLSSNQKSI EWDHEHVYKF 

       430        440        450        460        470        480 
LKNYYGPKLV SLYKEKSVSR SKEETVSATE DLTVATNALV VPIGAALAIA IASCAFGALA 

       490 
CYWRTQQKNR KPRRR 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC006200 Genomic DNA. Translation: AAD14527.2.
CP002685 Genomic DNA. Translation: AEC05425.1.
AY035175 mRNA. Translation: AAK59679.1.
AY090364 mRNA. Translation: AAL91267.1.
AY125539 mRNA. Translation: AAM78049.1.
BT000880 mRNA. Translation: AAN41280.1.
PIRF84422.
RefSeqNP_565258.1. NM_126188.3.
UniGeneAt.20100.

3D structure databases

ProteinModelPortalQ9ZU40.
SMRQ9ZU40. Positions 38-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G01270.1-P.

Proteomic databases

PaxDbQ9ZU40.
PRIDEQ9ZU40.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G01270.1; AT2G01270.1; AT2G01270.
GeneID814654.
KEGGath:AT2G01270.

Organism-specific databases

TAIRAT2G01270.

Phylogenomic databases

eggNOGNOG237986.
HOGENOMHOG000029909.
InParanoidQ9ZU40.
OMASGSWEPK.
PhylomeDBQ9ZU40.

Enzyme and pathway databases

BioCycARA:AT2G01270-MONOMER.

Gene expression databases

GenevestigatorQ9ZU40.

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.
IPR017937. Thioredoxin_CS.
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.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQSOX2_ARATH
AccessionPrimary (citable) accession number: Q9ZU40
Secondary accession number(s): Q94C52
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: June 1, 2002
Last modified: May 14, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names