QSOX1_PONAB
ID QSOX1_PONAB Reviewed; 750 AA.
AC H2N4I1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 03-AUG-2022, entry version 56.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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: 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; ABGA01039131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABGA01039132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002809780.2; XM_002809734.3.
DR AlphaFoldDB; H2N4I1; -.
DR SMR; H2N4I1; -.
DR STRING; 9601.ENSPPYP00000000519; -.
DR PRIDE; H2N4I1; -.
DR GeneID; 100461175; -.
DR KEGG; pon:100461175; -.
DR CTD; 5768; -.
DR eggNOG; KOG1731; Eukaryota.
DR HOGENOM; CLU_020182_1_0_1; -.
DR InParanoid; H2N4I1; -.
DR OrthoDB; 498515at2759; -.
DR TreeFam; TF316749; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IEA:InterPro.
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 3: Inferred from homology;
KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Golgi apparatus; Membrane;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..750
FT /note="Sulfhydryl oxidase 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000428724"
FT TRANSMEM 713..733
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 39..159
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 399..506
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT REGION 578..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 76
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 411
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 415
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 454
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 458
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 481..488
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 503
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 506
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..76
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 104..113
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT DISULFID 396..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 452..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 512..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ SEQUENCE 750 AA; 82804 MW; 0219DCEF33714B92 CRC64;
MGRCNRGSGP PSSLLLLLLL LLWLLAVPGA SAAPRSALYS PSDPLTLLQA DTVRGAVLGS
RSAWAVEFFA SWCGHCIAFA PTWKALAEDV KAWRPALNLA ALDCAEETNS AVCRDFNIPG
FPTVRFFKAF TKNGSGAVFP VAGADVQTLR ERLIDALESH HDTWPPACPP LEPARLEEID
GFFARNNEEY LALIFEKGGS YLGREVALDL SQHKGVAVRR VLNTEANVVR KFGVTDFPSC
YLLFRNGSVS RVPVLMESRS FYTAYLQRLS GLTREAAQTT VAPTTANKIA PTVWKFADRS
KIYMADLESA LHYILRIEVG RFPVLEGQCL VALKKFVAVL AKYFPGRPLV QNFLHSVNEW
LKRQKRNKIP YSFFKTALDD RKEGAVLAKK VNWIGCQGSE PHFRGFPCSL WVLFHFLTVQ
AARQNIDRSQ EAAKAKEVLP AIRGYVHYFF GCRDCASHFE QMAAASMHRV RSPNAAVLWL
WSSHNRVNAR LAGAPSEDPQ FPKVQWPPRE LCSACHNERL DVPVWDVEAT LNFLKAHFSP
SNIILDFAAA GSAAQREAQN VAAAPELAMG ALELESRNST VDLGKPEMMK SSTNTTPDVP
AERPEASRPP KLRPGLGAAP GQEPPEHMAE LQTNEREQPR GQWHLSKRDT GAALLAESRA
EKNHLWGPSE VRRVGRSSKQ LVDIPEGQLE AQAGRGRGQW LQVLGGGFSY LDISLCVGLY
SLSFMGLLAM YAYFRAKIRA LKGHAGHPAA
