QSOX1_CAVPO
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 03-AUG-2022, entry version 116.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 Ensembl; ENSCPOT00000002220; ENSCPOP00000001987; ENSCPOG00000002191.
DR GeneID; 100135609; -.
DR KEGG; cpoc:100135609; -.
DR CTD; 5768; -.
DR eggNOG; KOG1731; Eukaryota.
DR GeneTree; ENSGT00940000159504; -.
DR InParanoid; O08841; -.
DR OrthoDB; 498515at2759; -.
DR BRENDA; 1.8.3.2; 1225.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000002191; Expressed in ovary and 12 other 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:0030173; C:integral component of 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-linked 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 Gene3D; 1.20.120.1960; -; 1.
DR Gene3D; 1.20.120.310; -; 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; PTHR22897; 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; SSF52833; SSF52833; 1.
DR SUPFAM; SSF69000; SSF69000; 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
