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   16-JUN-2009, entry version 51.
DE   RecName: Full=Sulfhydryl oxidase 1;
DE            EC=1.8.3.2;
DE   AltName: Full=Quiescin Q6;
DE   AltName: Full=FAD-dependent sulfhydryl oxidase-3;
DE            Short=SOx-3;
DE   AltName: Full=Glandular epithelial cells protein 3;
DE   Flags: Precursor;
GN   Name=QSOX1; Synonyms=GEC3, QSCN6, SOX3;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricognathi; Caviidae; Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=21433478; 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
RT   during the 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
CC       and protein thiols to disulfides with the reduction of oxygen to
CC       hydrogen peroxide. May contribute to disulfide bond formation in a
CC       variety of secreted proteins (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4 R'C(R)SH + O(2) = 2 R'C(R)S-S(R)CR' + 2
CC       H(2)O.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Found in the extracellular
CC       medium.
CC   -!- TISSUE SPECIFICITY: Expressed in testis, placenta, pancreas, lung,
CC       ovary, endometrium, but not in brain, liver and kidney tissues.
CC       Higher expression in epithelial cells.
CC   -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX)
CC       family.
CC   -!- SIMILARITY: Contains 1 ERV/ALR sulfhydryl oxidase domain.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; U82982; AAB58401.2; -; mRNA.
DR   PIR; JC7762; JC7762.
DR   Ensembl; ENSCPOG00000002191; Cavia porcellus.
DR   HOVERGEN; O08841; -.
DR   BRENDA; 1.8.3.2; 44.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0030173; C:integral to Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; ISS:UniProtKB.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006467; P:protein thiol-disulfide exchange; ISS:UniProtKB.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR006863; Evr1_Alr.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:1.20.120.310; Evr1_Alr; 1.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Signal.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    613       Sulfhydryl oxidase 1.
FT                                /FTId=PRO_0000249536.
FT   DOMAIN       37    157       Thioredoxin.
FT   DOMAIN      397    504       ERV/ALR sulfhydryl oxidase.
FT   CARBOHYD    131    131       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    244    244       N-linked (GlcNAc...) (Potential).
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
//