ID A0A3Q2FL06_CYPVA Unreviewed; 637 AA.
AC A0A3Q2FL06;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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=QSOX2 {ECO:0000313|Ensembl:ENSCVAP00000005390.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000005390.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000005390.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_015250723.1; XM_015395237.1.
DR AlphaFoldDB; A0A3Q2FL06; -.
DR STRING; 28743.ENSCVAP00000005390; -.
DR Ensembl; ENSCVAT00000006770.1; ENSCVAP00000005390.1; ENSCVAG00000006750.1.
DR GeneID; 107097899; -.
DR KEGG; cvg:107097899; -.
DR CTD; 169714; -.
DR GeneTree; ENSGT00940000159734; -.
DR OMA; DSWDEGH; -.
DR OrthoDB; 20090at2759; -.
DR Proteomes; UP000265020; Unplaced.
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:SF7; SULFHYDRYL OXIDASE 2; 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:UP000265020};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|RuleBase:RU371123};
KW Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..637
FT /note="Sulfhydryl oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018640289"
FT TRANSMEM 604..621
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT DOMAIN 29..147
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 391..500
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
FT REGION 548..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 71399 MW; 4380FC5A7ED7C0FF CRC64;
MFRLWLQAAG FLWLCRGSLG ASGRLYSEED PLVILSSDSL KPTVTNSSSA WLLQFYSSWC
GHCIQYSSTW RALAHDVKDW QGAIGLAVLD CAQEENFDVC KEFGIKFYPT FKYFRAHGEP
TDRGTIYRGA DREVRSVRQL MIDILQNHTA LDRPESCPPL EPFSSAQLLP LLGQRSDHYT
AIILEEPDSF VGREVILDLL QFSGVLVRRA LSSDLPLLDA LNIAAFPSIY LLHPNGSHAQ
MHSEKRLRFF FSSLLRTLPG VQRRRRSEAA QMGALQDRQP SEPWRDFDRS KVYTADLESA
LHYLLRVELA AHSSLEGEEL QVFKEFVTVV AKLYPGRGSV VKLMETLSDW LLSLPLQQIP
YQAVMDLVDN KMKISGVFLG AELRWVGCQG SRPGLRGYPC SLWTLFHVLT VQHEATPTAL
DGTGLEAQAA PVLQVMRRYI RTFFGCRECA RHFEQAAAAG MEQVKSREEE VLWLWNQHNR
VNARLAGSLS DDPLFPKAPW PSPALCPACH EENNGVHVWN QDNVLQFLRH HYGAANLSPR
YSLLPPPLPA APGPTRAPQQ EPPAAAGGGG RAGEQKEEVV SGGGGGGVWI LALGFNSVDM
SLCVVLYVCS CLVLMLLFFF FKVRSRRWKT RHSRLHV
//
