ID A0A2K6RE13_RHIRO Unreviewed; 747 AA.
AC A0A2K6RE13;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN Name=QSOX1 {ECO:0000313|Ensembl:ENSRROP00000039288.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000039288.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000039288.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU371123}.
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:0000256|ARBA:ARBA00000999,
CC ECO:0000256|RuleBase:RU371123};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU371123};
CC -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
CC {ECO:0000256|ARBA:ARBA00006041, ECO:0000256|RuleBase:RU371123}.
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DR AlphaFoldDB; A0A2K6RE13; -.
DR Ensembl; ENSRROT00000063767.1; ENSRROP00000039288.1; ENSRROG00000042952.1.
DR GeneTree; ENSGT00940000159504; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro.
DR CDD; cd02992; PDI_a_QSOX; 1.
DR Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR Gene3D; 1.20.120.1960; QSOX sulfhydryl oxidase domain; 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; QUIESCIN Q6-RELATED SULFHYDRYL OXIDASE; 1.
DR PANTHER; PTHR22897:SF6; SULFHYDRYL OXIDASE 1; 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; SSF69000; FAD-dependent thiol oxidase; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU371123};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU371123}; Membrane {ECO:0000256|RuleBase:RU371123};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU371123};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|RuleBase:RU371123};
KW Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..747
FT /note="Sulfhydryl oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014478070"
FT TRANSMEM 714..731
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT DOMAIN 36..156
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 396..503
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
FT REGION 573..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 82508 MW; D7AEE21E0B7C78FE CRC64;
MGRCGRGSEP LPSLLLLLLL LLAVPGAGAA PRSALYSPSD PLTLLQADTV RGAVLGSRGA
WAVEFFASWC GHCIAFAPTW KALAEDVKAW RPALNLAALD CAEETNSAVC RDFNIPGFPT
VRVSALLTPC SRLCSFTVAG ADVQTLRERL IDALESHHDT WPPACPPLEP AKLEEIDGFF
ARNKEEYLAL IFEKGGSYLG REVALDLSQH KGVMVRRVLN TEADVVRKFG VTDFPSCYLL
FRNGSVSRVP VLMESRSFYT AYLQRLSGLT REAAQTTVAP TTANKIAPTV WKFADRSKIY
MADLESALHY ILRIEVGRFP VLEGQRLVAL KKFVAVLAKY FPGRPLVQNF LHSVNEWLKR
QKRNKIPYSF FKTALDDRKE GAVLAKKVNW IGCQGSEPHF RGFPCSLWVL FHFLTVQAAR
QNVDHSQEAA KAQEVLPAIR GYVHYFFGCR DCAGHFEQMA AASMHRVGSP NAAVLWLWSS
HNRVNARLAG APSEDPQFPK VQWPPRELCS ACHNERLDVP VWDVEATLRF LKAHFSPSNI
ILDFPAAGSA ARREAQNVAA APELAMGSLE LEGRNSTLDP GKPEMMKSPA NTTPDVPVER
PEASRPPKLR PGLGAAPGQE PPEHMAELQR KEREQPRGQW HLSKRDTGAA LLAESRAEKN
HLWGPSEVRR VGRSSKQLVD IPEGQLEARA GRGRGQWLQV LGGGFSHLDI SLCVGLYSLS
FMGLLAMYTY FRAKIRALKG HVGHPAA
//
