ID   QSOX1_ORYSJ             Reviewed;         513 AA.
AC   Q6AUC6; A0A0P0WQM2; Q0DG53;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   RecName: Full=Sulfhydryl oxidase 1;
DE            EC=1.8.3.2;
DE   AltName: Full=Quiescin-sulfhydryl oxidase 1;
DE            Short=OsQSOX1;
DE   Flags: Precursor;
GN   Name=QSOX1; OrderedLocusNames=Os05g0552500, LOC_Os05g47930;
GN   ORFNames=OsJ_19470, OSJNBa0079H23.16;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00654};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF18170.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC129717; AAT85195.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF18170.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014961; BAS95229.1; -; Genomic_DNA.
DR   EMBL; CM000142; EEE64618.1; -; Genomic_DNA.
DR   EMBL; AK121660; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015640480.1; XM_015784994.1.
DR   AlphaFoldDB; Q6AUC6; -.
DR   SMR; Q6AUC6; -.
DR   STRING; 39947.Q6AUC6; -.
DR   GlyCosmos; Q6AUC6; 3 sites, No reported glycans.
DR   PaxDb; 39947-Q6AUC6; -.
DR   EnsemblPlants; Os05t0552500-02; Os05t0552500-02; Os05g0552500.
DR   GeneID; 4339541; -.
DR   Gramene; Os05t0552500-02; Os05t0552500-02; Os05g0552500.
DR   KEGG; osa:4339541; -.
DR   eggNOG; KOG1731; Eukaryota.
DR   HOGENOM; CLU_041851_0_0_1; -.
DR   InParanoid; Q6AUC6; -.
DR   OMA; FASAKWD; -.
DR   OrthoDB; 20090at2759; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000007752; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   ExpressionAtlas; Q6AUC6; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016971; F:flavin-dependent 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   CDD; cd02992; PDI_a_QSOX; 1.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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; QUIESCIN Q6-RELATED SULFHYDRYL OXIDASE; 1.
DR   PANTHER; PTHR22897:SF8; SULFHYDRYL OXIDASE; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   Genevisible; Q6AUC6; OS.
PE   2: Evidence at transcript level;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW   Redox-active center; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..513
FT                   /note="Sulfhydryl oxidase 1"
FT                   /id="PRO_0000400052"
FT   DOMAIN          31..174
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          304..406
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   ACT_SITE        76
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        79
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         377..384
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         403
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         406
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..79
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT                   ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        301..313
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        348..351
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        412..415
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   CONFLICT        160
FT                   /note="R -> G (in Ref. 6; AK121660)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        361
FT                   /note="S -> G (in Ref. 6; AK121660)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   513 AA;  57849 MW;  B891D5944EDC38A4 CRC64;
     MAAAAVARRV VLVLVLAAAS LAAAPRGAAA RSLGGREGPG EVDADAAVDL NATNFDAFLK
     ASLEPWAVVE FFAHWCPACR NYKPHYEKVA KLFNGRDAAH PGLILMARVD CASKVNIDLC
     NRFSVDHYPF LLWGPPTKFA SAKWDPKQEN NEIKLIDDGR TAERLLKWIN NQMKSSFSLE
     DKKYENENML PKNASDPEQI VQAIYDVEEA TAQALQIILE RKTIKPKNRD SLIRFLQILV
     ARHPSKRCRR GSAELLINFD DHWSSNLSLS SQEGSKLLES VAEENHWICG KEVPRGYWLF
     CRGSKSETRG FSCGLWVLMH SLTVRIGDGE SQSTFTSICD FIHNFFICEE CRKHFYEMCS
     SVSAPFRTAR ELSLWLWSTH NKVNMRLMKE EKDMGTGDPL FPKVTWPPNQ LCPSCYRSSK
     VTDGAVDWNE DAVYQFLVNY YGKKLVSSYK ETYMESLQQQ EKKIVSEDSS ISNAASVPIG
     AALGVAIASC TFGALACFWR AQQKNRKQRK NWN
//