QSOX1_ARATH
ID QSOX1_ARATH Reviewed; 528 AA.
AC Q8W4J3; Q3EDC3; Q9M9Q3;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Sulfhydryl oxidase 1;
DE EC=1.8.3.2;
DE AltName: Full=Quiescin-sulfhydryl oxidase 1;
DE Short=AtQSOX1;
DE Flags: Precursor;
GN Name=QSOX1; Synonyms=QSO2; OrderedLocusNames=At1g15020; ORFNames=T15D22.7;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORM 1).
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).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17568770; DOI=10.1038/sj.emboj.7601757;
RA Alejandro S., Rodriguez P.L., Belles J.M., Yenush L., Garcia-Sanchez M.J.,
RA Fernandez J.A., Serrano R.;
RT "An Arabidopsis quiescin-sulfhydryl oxidase regulates cation homeostasis at
RT the root symplast-xylem interface.";
RL EMBO J. 26:3203-3215(2007).
CC -!- FUNCTION: Sulfhydryl oxidase involved in the regulation of cation
CC homeostasis. Positively regulates shoot accumulation of K(+) and
CC inhibits accumulation of toxic cations. Acts at the level of root K(+)
CC efflux systems involved in xylem loading (root symplast-xylem
CC interface). {ECO:0000269|PubMed:17568770}.
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, cell wall
CC {ECO:0000269|PubMed:17568770}. Note=Associated with the cell wall.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8W4J3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8W4J3-2; Sequence=VSP_039985;
CC -!- TISSUE SPECIFICITY: Highly expressed in roots.
CC {ECO:0000269|PubMed:17568770}.
CC -!- INDUCTION: By salt and norspermidine treatments and phosphate
CC starvation. {ECO:0000269|PubMed:17568770}.
CC -!- MISCELLANEOUS: Plants lacking QSOX1 display more sensitivity to the
CC toxic cations lithium and sodium than wild-type plants.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF31025.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012189; AAF31025.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29255.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29256.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59589.1; -; Genomic_DNA.
DR EMBL; AY062528; AAL32606.1; -; mRNA.
DR EMBL; BT001218; AAN65105.1; -; mRNA.
DR PIR; G86283; G86283.
DR RefSeq; NP_001321934.1; NM_001332143.1. [Q8W4J3-2]
DR RefSeq; NP_172955.1; NM_101371.5. [Q8W4J3-1]
DR RefSeq; NP_849664.1; NM_179333.2. [Q8W4J3-2]
DR AlphaFoldDB; Q8W4J3; -.
DR SMR; Q8W4J3; -.
DR STRING; 3702.AT1G15020.2; -.
DR PaxDb; Q8W4J3; -.
DR PRIDE; Q8W4J3; -.
DR ProteomicsDB; 236516; -. [Q8W4J3-1]
DR EnsemblPlants; AT1G15020.1; AT1G15020.1; AT1G15020. [Q8W4J3-2]
DR EnsemblPlants; AT1G15020.2; AT1G15020.2; AT1G15020. [Q8W4J3-1]
DR EnsemblPlants; AT1G15020.3; AT1G15020.3; AT1G15020. [Q8W4J3-2]
DR GeneID; 838067; -.
DR Gramene; AT1G15020.1; AT1G15020.1; AT1G15020. [Q8W4J3-2]
DR Gramene; AT1G15020.2; AT1G15020.2; AT1G15020. [Q8W4J3-1]
DR Gramene; AT1G15020.3; AT1G15020.3; AT1G15020. [Q8W4J3-2]
DR KEGG; ath:AT1G15020; -.
DR Araport; AT1G15020; -.
DR TAIR; locus:2196209; AT1G15020.
DR eggNOG; KOG1731; Eukaryota.
DR InParanoid; Q8W4J3; -.
DR OMA; ILVVEEW; -.
DR OrthoDB; 498515at2759; -.
DR PhylomeDB; Q8W4J3; -.
DR BioCyc; ARA:AT1G15020-MON; -.
DR BRENDA; 1.8.3.2; 399.
DR PRO; PR:Q8W4J3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W4J3; baseline and differential.
DR Genevisible; Q8W4J3; AT.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0000137; C:Golgi cis cisterna; HDA:TAIR.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
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:0016972; F:thiol oxidase activity; TAS:UniProtKB.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0043157; P:response to cation stress; IMP:TAIR.
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 Alternative splicing; Cell wall; Disulfide bond; FAD; Flavoprotein;
KW Glycoprotein; Oxidoreductase; Redox-active center; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..528
FT /note="Sulfhydryl oxidase 1"
FT /id="PRO_0000400050"
FT DOMAIN 35..170
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 295..397
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT ACT_SITE 72
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 75
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 368..375
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..75
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 292..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 339..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 403..406
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT VAR_SEQ 497..527
FT /note="YNYNPHYLKRYNSNYMVMNTFSNTESEREKE -> QQIQR (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039985"
SQ SEQUENCE 528 AA; 60087 MW; 99D1E9B46492F976 CRC64;
MSLIHLFLLL GLLSLEAAAS FSPGSRSILR DIGSNVADQK DNAIELNATN FDSVFQDSPA
KYAVLEFFAH WCPACRNYKP HYEKVARLFN GADAVYPGVV LMTRVDCAIK MNVKLCDKFS
INHYPMLFWA PPKRFVGGSW GPKQEKNEIS VVNEWRTADL LLNWINKQIG SSYGLDDQKL
GNLLSNISDQ EQISQAIFDI EEATEEAFDI ILAHKAIKSS ETSASFIRFL QLLVAHHPSR
RCRTGSAEIL VNFDDICPSG ECSYDQESGA KDSLRNFHIC GKDVPRGYYR FCRGSKNETR
GFSCGLWVLM HSLSVRIEDG ESQFAFTAIC DFINNFFMCD DCRRHFHDMC LSVKTPFKKA
RDIALWLWST HNKVNERLKK DEDSLGTGDP KFPKMIWPPK QLCPSCYLSS TEKNIDWDHD
QVYKFLKKYY GQKLVSVYKK NGESVSKEEV IAAAEEMAVP TNALVVPVGA ALAIALASCA
FGALACYWRT QQKNRKYNYN PHYLKRYNSN YMVMNTFSNT ESEREKER
