ID   QSOX1_CAVPO             Reviewed;         613 AA.
AC   O08841;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   24-JAN-2024, entry version 121.
DE   RecName: Full=Sulfhydryl oxidase 1;
DE            EC=1.8.3.2;
DE   AltName: Full=FAD-dependent sulfhydryl oxidase-3 {ECO:0000303|PubMed:11549257};
DE            Short=SOx-3 {ECO:0000303|PubMed:11549257};
DE   AltName: Full=Glandular epithelial cells protein 3;
DE   AltName: Full=Quiescin Q6;
DE   Flags: Precursor;
GN   Name=QSOX1; Synonyms=GEC3, QSCN6, SOX3;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=11549257; DOI=10.1006/bbrc.2001.5440;
RA   Musard J.-F., Sallot M., Dulieu P., Fraichard A., Ordener C.,
RA   Remy-Martin J.-P., Jouvenot M., Adami P.;
RT   "Identification and expression of a new sulfhydryl oxidase SOx-3 during the
RT   cell cycle and the estrus cycle in uterine cells.";
RL   Biochem. Biophys. Res. Commun. 287:83-91(2001).
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. Plays a role in disulfide bond formation in a variety of
CC       extracellular proteins. In fibroblasts, required for normal
CC       incorporation of laminin into the extracellular matrix, and thereby for
CC       normal cell-cell adhesion and cell migration.
CC       {ECO:0000250|UniProtKB:O00391}.
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         Evidence={ECO:0000250|UniProtKB:O00391};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:O00391};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O00391};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6IUU3}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected in endometrium and in uterus glandular
CC       epithelial cells (at protein level). Expressed in testis, placenta,
CC       pancreas, lung, ovary, endometrium, but not in brain, liver and kidney
CC       tissues. Higher expression in epithelial cells.
CC       {ECO:0000269|PubMed:11549257}.
CC   -!- PTM: N-glycosylated. O-glycosylated on Thr and Ser residues.
CC       {ECO:0000250|UniProtKB:O00391}.
CC   -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
CC       {ECO:0000305}.
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DR   EMBL; U82982; AAB58401.2; -; mRNA.
DR   PIR; JC7762; JC7762.
DR   RefSeq; NP_001166479.1; NM_001173008.2.
DR   AlphaFoldDB; O08841; -.
DR   SMR; O08841; -.
DR   STRING; 10141.ENSCPOP00000001987; -.
DR   GlyCosmos; O08841; 2 sites, No reported glycans.
DR   Ensembl; ENSCPOT00000002220.3; ENSCPOP00000001987.3; ENSCPOG00000002191.4.
DR   GeneID; 100135609; -.
DR   KEGG; cpoc:100135609; -.
DR   CTD; 5768; -.
DR   VEuPathDB; HostDB:ENSCPOG00000002191; -.
DR   eggNOG; KOG1731; Eukaryota.
DR   GeneTree; ENSGT00940000159504; -.
DR   InParanoid; O08841; -.
DR   OMA; SDMDMRM; -.
DR   OrthoDB; 20090at2759; -.
DR   BRENDA; 1.8.3.2; 1225.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000002191; Expressed in ovary and 12 other cell types or tissues.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR   GO; GO:0071949; F:FAD binding; IEA:Ensembl.
DR   GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; ISS:UniProtKB.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB.
DR   GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR   GO; GO:0016242; P:negative regulation of macroautophagy; IEA:Ensembl.
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; 2.
DR   Gene3D; 1.20.120.1960; QSOX sulfhydryl oxidase domain; 1.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR040986; QSOX_FAD-bd_dom.
DR   InterPro; IPR042568; QSOX_FAD-bd_sf.
DR   InterPro; IPR041269; QSOX_Trx1.
DR   InterPro; IPR039798; Sulfhydryl_oxidase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR22897; QUIESCIN Q6-RELATED SULFHYDRYL OXIDASE; 1.
DR   PANTHER; PTHR22897:SF6; SULFHYDRYL OXIDASE 1; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   Pfam; PF18371; FAD_SOX; 1.
DR   Pfam; PF18108; QSOX_Trx1; 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; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..613
FT                   /note="Sulfhydryl oxidase 1"
FT                   /id="PRO_0000249536"
FT   DOMAIN          37..157
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          397..504
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   ACT_SITE        71
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        74
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         402
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         409
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         413
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         452
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         456
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         479..486
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         501
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         504
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        71..74
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT                   ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        102..111
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   DISULFID        394..406
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        450..453
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        510..513
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ   SEQUENCE   613 AA;  68595 MW;  34105EF608CA7B55 CRC64;
     MTGCGRRSGW LPPLRLLLLP LLLGGPGVGA AQLAALYSAS DPLTLLQADT VRSTVLNSPS
     AWAVEFFASW CGHCIAFAPT WKALAKDIKD WRPALNLAAL NCADETNNAV CRDFNIAGFP
     SVRFFKAFSK NSTGTTLPVA GANVQMLRER LIDALESHHD TWPSACPPLE PVKPKEIDTF
     FARNNQEYLV LIFEQENSYL GREVTLDLSQ HHDLVVRRVL STEANVVRKF GVADFPSCYL
     LFRNGSVSRV PVLVESRRFY TAYLQRLSEV TREGTPTPAV PTISDQIAPT VWKFADRSKI
     YMADLESALH YILRVEVGRF SVLEGQRLMA LKKFVTVLTK YFPGQPLVRN FLQSTNEWLK
     RQHKKKMPYS FFKTAMDSRN EEAVITKEVN WVGCQGSESH FRGFPCSLWI LFHFLTVQAS
     QKNAESSQKP ANGQEVLQAI RNYVRFFFGC RDCANHFEQM AAGSMHRVKS PNDAVLWLWT
     SHNRVNARLA GAPSEDPQFP KVQWPPPELC SACHNELSGE PVWDVDATLR FLKTHFSPSN
     IVLNFPPAEP ASRSSVHSWG ATPHLELDAL GLVTRNSALA LERAEISESP GSNAMPNIPA
     ERPELFEALS HSR
//