QSOX1_CHICK
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 03-AUG-2022, entry version 118.
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 Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND REVIEW.
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).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=10542195; DOI=10.1074/jbc.274.45.31759;
RA Hoober K.L., Glynn N.M., Burnside J., Coppock D.L., Thorpe C.;
RT "Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a
RT new class of flavin-linked sulfhydryl oxidases.";
RL J. Biol. Chem. 274:31759-31762(1999).
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 -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O00391}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O00391}. Secreted
CC {ECO:0000250|UniProtKB:O00391}. Note=A small proportion is secreted,
CC probably via a proteolytic cleavage that removes the membrane anchor.
CC {ECO:0000250|UniProtKB:O00391}.
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; AY112666; AAM44079.1; -; mRNA.
DR RefSeq; NP_989456.1; NM_204125.1.
DR AlphaFoldDB; Q8JGM4; -.
DR SMR; Q8JGM4; -.
DR STRING; 9031.ENSGALP00000006256; -.
DR Ensembl; ENSGALT00000099189; ENSGALP00000065414; ENSGALG00000003933.
DR GeneID; 373914; -.
DR KEGG; gga:373914; -.
DR CTD; 5768; -.
DR VEuPathDB; HostDB:geneid_373914; -.
DR eggNOG; KOG1731; Eukaryota.
DR GeneTree; ENSGT00940000159504; -.
DR HOGENOM; CLU_020182_1_0_1; -.
DR InParanoid; Q8JGM4; -.
DR OMA; YLWKAHN; -.
DR OrthoDB; 498515at2759; -.
DR PhylomeDB; Q8JGM4; -.
DR BRENDA; 1.8.3.2; 1306.
DR PRO; PR:Q8JGM4; -.
DR Proteomes; UP000000539; Chromosome 8.
DR Bgee; ENSGALG00000003933; Expressed in ovary and 14 other tissues.
DR ExpressionAtlas; Q8JGM4; baseline and differential.
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; IBA:GO_Central.
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:0006457; P:protein folding; IBA:GO_Central.
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 Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW Golgi apparatus; Membrane; Oxidoreductase; Reference proteome; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..743
FT /note="Sulfhydryl oxidase 1"
FT /id="PRO_0000249537"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 43..166
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 410..513
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT REGION 567..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 422
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 426
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 461
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 465
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 488..495
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 510
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 513
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..83
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 111..120
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT DISULFID 407..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 459..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 519..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
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
