QSOX2_ARATH
ID QSOX2_ARATH Reviewed; 495 AA.
AC Q9ZU40; Q94C52;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Sulfhydryl oxidase 2;
DE EC=1.8.3.2;
DE AltName: Full=Quiescin-sulfhydryl oxidase 2;
DE Short=AtQSOX2;
DE Flags: Precursor;
GN Name=QSOX2; OrderedLocusNames=At2g01270; ORFNames=F10A8.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and
CC protein thiols to disulfides with the reduction of oxygen to hydrogen
CC peroxide. May contribute to disulfide bond formation in a variety of
CC secreted proteins (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00654};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR EMBL; AC006200; AAD14527.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC05425.1; -; Genomic_DNA.
DR EMBL; AY035175; AAK59679.1; -; mRNA.
DR EMBL; AY090364; AAL91267.1; -; mRNA.
DR EMBL; AY125539; AAM78049.1; -; mRNA.
DR EMBL; BT000880; AAN41280.1; -; mRNA.
DR PIR; F84422; F84422.
DR RefSeq; NP_565258.1; NM_126188.4.
DR AlphaFoldDB; Q9ZU40; -.
DR SMR; Q9ZU40; -.
DR STRING; 3702.AT2G01270.1; -.
DR SwissPalm; Q9ZU40; -.
DR PaxDb; Q9ZU40; -.
DR PRIDE; Q9ZU40; -.
DR ProteomicsDB; 226141; -.
DR EnsemblPlants; AT2G01270.1; AT2G01270.1; AT2G01270.
DR GeneID; 814654; -.
DR Gramene; AT2G01270.1; AT2G01270.1; AT2G01270.
DR KEGG; ath:AT2G01270; -.
DR Araport; AT2G01270; -.
DR TAIR; locus:2038771; AT2G01270.
DR eggNOG; KOG1731; Eukaryota.
DR HOGENOM; CLU_041851_0_0_1; -.
DR InParanoid; Q9ZU40; -.
DR OMA; DVANAFF; -.
DR OrthoDB; 498515at2759; -.
DR PhylomeDB; Q9ZU40; -.
DR BioCyc; ARA:AT2G01270-MON; -.
DR BRENDA; 1.8.3.2; 399.
DR PRO; PR:Q9ZU40; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU40; baseline and differential.
DR Genevisible; Q9ZU40; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 1.20.120.310; -; 1.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR InterPro; IPR039798; Sulfhydryl_oxidase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR22897; PTHR22897; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF69000; SSF69000; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Redox-active center; Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..495
FT /note="Sulfhydryl oxidase 2"
FT /id="PRO_0000400051"
FT DOMAIN 29..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 290..392
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT ACT_SITE 66
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 69
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 363..370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 66..69
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 287..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 334..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 398..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT CONFLICT 85
FT /note="G -> D (in Ref. 3; AAK59679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 55919 MW; 2FBBFA72D9C0A95D CRC64;
MSLVHLLLFA GLVIAASSSS PGSRLILREI SDQKDKAVEL NTTNFDSVLK DTPAKYAVVE
FFAHWCPACR NYKPHYEKVA RLFNGPDAIH PGIVLMTRVD CAMKTNTKLC DKFSVSHYPM
LFWGPPTKFV SGSWEPKKDK SEILVIDDGR TAERLLNWIN KQIGSSYGLD DQKFKNEHAL
SNLTDYNQIS QAVYDVEEAT AEAFDIILAH KAIKSSETSA SFIRFIQLLA AHHLSRRCRK
GAAEILVNYD DLCPSGNCSY EKSGGNDTLG NFPICGKDVP RGYYMFCRGS KNDTRGFSCG
LWVLMHSLSV RIEDGESHFA FTTICDFVNN FFMCDECRLH FNDMCLSVKT PFKKARDFVL
WVWSTHNKVN ERLLKDEASL GTGDPKFPKI IWPPKELCPL CYLSSNQKSI EWDHEHVYKF
LKNYYGPKLV SLYKEKSVSR SKEETVSATE DLTVATNALV VPIGAALAIA IASCAFGALA
CYWRTQQKNR KPRRR
