ID   QSOX1_CHICK             Reviewed;         743 AA.
AC   Q8JGM4;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 41.
DE   RecName: Full=Sulfhydryl oxidase 1;
DE            EC=1.8.3.2;
DE   AltName: Full=Quiescin Q6;
DE   Flags: Precursor;
GN   Name=QSOX1; Synonyms=QSCN6, QSOX, SOX;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX   PubMed=12176051; DOI=10.1016/S0003-9861(02)00337-5;
RA   Thorpe C., Hoober K.L., Raje S., Glynn N.M., Burnside J., Turi G.K.,
RA   Coppock D.L.;
RT   "Sulfhydryl oxidases: emerging catalysts of protein disulfide bond
RT   formation in eukaryotes.";
RL   Arch. Biochem. Biophys. 405:1-12(2002).
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: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass
CC       membrane protein (By similarity).
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. Highly expressed in the
CC       active secretory tissue of the oviduct.
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; AY112666; AAM44079.1; -; mRNA.
DR   IPI; IPI00571581; -.
DR   RefSeq; NP_989456.1; -.
DR   UniGene; Gga.148; -.
DR   HSSP; P09856; 1F9M.
DR   PRIDE; Q8JGM4; -.
DR   Ensembl; ENSGALG00000003933; Gallus gallus.
DR   GeneID; 373914; -.
DR   KEGG; gga:373914; -.
DR   HOVERGEN; Q8JGM4; -.
DR   BRENDA; 1.8.3.2; 4.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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; IPR010747; DUF1321.
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; PF07031; DUF1321; 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   1: Evidence at protein level;
KW   FAD; Flavoprotein; Glycoprotein; Golgi apparatus; Membrane;
KW   Oxidoreductase; Signal; Transmembrane.
FT   SIGNAL        1     42       Potential.
FT   CHAIN        43    743       Sulfhydryl oxidase 1.
FT                                /FTId=PRO_0000249537.
FT   TRANSMEM    707    727       Potential.
FT   DOMAIN       43    166       Thioredoxin.
FT   DOMAIN      410    513       ERV/ALR sulfhydryl oxidase.
FT   COMPBIAS    578    603       Glu-rich.
FT   COMPBIAS    680    684       Poly-Glu.
FT   CARBOHYD    254    254       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    288    288       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    295    295       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    371    371       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    401    401       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   743 AA;  83079 MW;  44512B7EBB0B9769 CRC64;
     MWRRRARSGG GGGGGGGGAA PRCRWWPAVL ALLAAALPAA RSRSLYSPSD PLELLGADTA
     ERRLLGSPSA WAVEFFASWC GHCIHFAPTW RALAEDVREW RPAVMIAALD CADEANQQVC
     ADFGITGFPT LKFFRAFSKK AEDGIRIAHP TATVADLRRA IITNLEQSGD AWPPACPPLE
     PASAEEVRSF FHRNTERYLA LIFEQSNSFV GREVALDLLQ YENVAVRRVL SSEEELVEKF
     GVTTFPSAYL LLRNGSFSRL PVHAEARSFY TYYLQTLSGV TRGSYRLNVT GSAINETRAL
     QPAQADRSKV YVADLESTVH YTLRVEAGRP AVLAGAQLAA LKCYVATLAK YFPGRPSVQT
     FLQSLDSWLR NWTEPELPRS ALKEAVKNKE DASPAAVLPT NVTWVGCRGS EPHFRGYPCG
     LWTIFHLLTV QAAQGGPDEE LPLEVLNTMR CYVKHFFGCQ ECAQHFEAMA AKSMDQVKSR
     REAVLWLWSH HNEVNARLAG GDTEDPQFPK LQWPPPDMCP QCHREERGVH TWDEAAVLSF
     LKEHFSLGNL YLDHAIPIPM AGEEAAASAR LSTAGLREKE EEERKEEEEE GEKETEKPHR
     EGETGRPGSS ELRRPSIVRR NPRLRALGED IVDLDSFSEQ HFKSKALRAA GRHRRLSKRD
     TVALHHDAGW ERLQVPESRE EEEEGGVLRR SPWLRVLGLG FSRLDVSLCI ALYFLSSMCL
     LGMYTFFRLR TRARKGRPGF PVA
//