UniProt: A0A1S3PRE8

Database: UniProt
Entry: A0A1S3PRE8_SALSA

LinkDB:  A0A1S3PRE8_SALSA 
Original site:  A0A1S3PRE8_SALSA

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (4)   
   PROSITE (2)   
All databases (19)   

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ID   A0A1S3PRE8_SALSA        Unreviewed;       668 AA.
AC   A0A1S3PRE8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   Name=qsox2 {ECO:0000313|RefSeq:XP_014030206.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014030206.1};
RN   [1] {ECO:0000313|RefSeq:XP_014030206.1}
RP   IDENTIFICATION.
RG   RefSeq;
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_014030206.1; XM_014174731.1.
DR   AlphaFoldDB; A0A1S3PRE8; -.
DR   STRING; 8030.ENSSSAP00000034321; -.
DR   PaxDb; 8030-ENSSSAP00000034321; -.
DR   KEGG; sasa:106586968; -.
DR   OrthoDB; 20090at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa26.
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:UP000087266};
KW   Transmembrane {ECO:0000256|RuleBase:RU371123};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT   TRANSMEM        635..652
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU371123"
FT   DOMAIN          39..159
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          408..517
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
FT   REGION          558..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  75534 MW;  14A8C4685375661D CRC64;
     MATLCVDDCP SLRKTGFLLF KTSIIFVFLF NPSLTTRLYS EEDSVVILTS ATVEQTLLNS
     STAWLVQFYS SWCGHCIQYS PTWKALAGDV KDWEHAIRIG VLDCAQENNF DICKEFGIHF
     YPTFRYFKAR GPTFDVGKTY RGADRELQTV RQLMVNFLQN HTRQDWPVSC PPLEPYSSAD
     ILPLIGQKSN QYTAVIVENE DSYVGREVIL DLMMYQGLTV KRALSSEKSL TEKLGINSFP
     SAYLLHPNGT HAILHVQKRL RFFFSSFLKL LLGVHRKLST SGAPQKPLLE GPRGPGTAEA
     LKDFEKSKVY MADLESGLHY LLRVELATHQ TLEGEELKTF KDFVTVVAKL FPGRQSVVKL
     LETLLEWLVS LPLEKIPFDA ILDLVNNKMR ISGMFLSDQL QWVGCQGSRV GLRGYPCSLW
     TLFHVLTVQA ASRPDALANT GLEENPKAVL QTMRKYIVNF FGCQECGKHF EEMAVASLPQ
     VKSVDQAVLW LWRKHNQVNG RLAGTMSEDP HFPKTQWPSP DLCPTCHEEQ DGIHVWNEDK
     VLMFLKQHYG AANISPKHMY SSQHEPNQEA LGSPDNKPIK ATQEKTVAPE SSLLHAKQSD
     VEGAGQAGTG AHRETRPGVS FLGLGFSSVD MSLCVVLYAF SCVFLMVMFF FFRVRSKRWK
     IRYNRPYV
//

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