ID B0UXN0_DANRE Unreviewed; 778 AA.
AC B0UXN0; A0A8M1NHY3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 104.
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:ENSDARP00000057644,
GN ECO:0000313|RefSeq:NP_001121836.1,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-7019};
GN Synonyms=fk65c10 {ECO:0000313|RefSeq:NP_001121836.1}, im:6793551
GN {ECO:0000313|RefSeq:NP_001121836.1}, sb:cb840
GN {ECO:0000313|RefSeq:NP_001121836.1}, si:dkey-39n1.2
GN {ECO:0000313|RefSeq:NP_001121836.1}, wu:fc30g09
GN {ECO:0000313|RefSeq:NP_001121836.1}, wu:fk65c10
GN {ECO:0000313|RefSeq:NP_001121836.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000057644};
RN [1] {ECO:0000313|RefSeq:NP_001121836.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001121836.1};
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.D., Sun X.J., Deng M., Zhang G.W., Zhou Y., Wu X.Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.L., Fan H.Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2] {ECO:0000313|Ensembl:ENSDARP00000057644, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000057644};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000057644}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000057644};
RG Ensembl;
RL Submitted (AUG-2013) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:NP_001121836.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001121836.1};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [5] {ECO:0000313|RefSeq:NP_001121836.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001121836.1};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU371123}.
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DR EMBL; CR381643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001121836.1; NM_001128364.1.
DR STRING; 7955.ENSDARP00000057644; -.
DR PaxDb; 7955-ENSDARP00000057644; -.
DR PeptideAtlas; B0UXN0; -.
DR Ensembl; ENSDART00000057645; ENSDARP00000057644; ENSDARG00000039459.
DR Ensembl; ENSDART00000057645.6; ENSDARP00000057644.5; ENSDARG00000039459.7.
DR GeneID; 100004382; -.
DR KEGG; dre:100004382; -.
DR AGR; ZFIN:ZDB-GENE-030131-7019; -.
DR CTD; 5768; -.
DR ZFIN; ZDB-GENE-030131-7019; qsox1.
DR eggNOG; KOG1731; Eukaryota.
DR HOGENOM; CLU_020182_1_0_1; -.
DR OMA; RYFPFND; -.
DR OrthoDB; 20090at2759; -.
DR PhylomeDB; B0UXN0; -.
DR TreeFam; TF316749; -.
DR BRENDA; 1.8.3.2; 928.
DR Reactome; R-DRE-114608; Platelet degranulation.
DR Reactome; R-DRE-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000000437; Chromosome 8.
DR Bgee; ENSDARG00000039459; Expressed in liver and 29 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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:UP000000437};
KW Transmembrane {ECO:0000256|RuleBase:RU371123};
KW Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT TRANSMEM 747..764
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT DOMAIN 44..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 407..510
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
FT REGION 569..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..612
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 88047 MW; 9895990B3802EF79 CRC64;
MARRGCGATS CYTTKTKLNS FYSFLCAFIT CVSLCPVLCE AGLYTASDQV IVLTPENVDS
TLFNNTAALL VEFYATWCGH CIAFSPVWKS LARDIKEWKP AVDLAAIDCA NESNRKVCTN
FGITGYPSIK FFHAYSSIGS RGLEVRGFSR DVRGLRQYII ENLELHTEAW PPACPPLETA
SEAEVHHFFP ANNVKYLALV FENKKSYVGR EVTLDLLQYE NIAVRRVLDT ETNLVSRFGV
TEFPSCYLYD SSGNITRLKV LKEARTFYSY ALQRLPGVVR TGKHQTPITE LIKNSTLQEW
RPFNKSRVYM SDLESALHYS LRVELSSHTS ISGDDLIALK KYINVLAKYF PGRPSVKSAL
QAVDSWLQSQ KGTEIKYSDF RDVLDNVVQT SDAVLPEGVQ WVGCQGSQAR YRGYPCAVWT
LFHVLTVQAK EMGSTVSEPQ EVLLAMRGYV SSFFGCRPCA THFEAMAAES MDQVNSLSGA
VIWLWSRHNR VNNRLAGDLS EDPHFPKIQW PSPELCPSCH GVTIIGDHNW IKDEVPQFLQ
NYFSSSRILN DYLQDETQAL IQQRNRLTAA RMEKEAGRGA DRRARDIFDN NPADEPQEEE
EEEEEEEPTF EEQAVEPYPA GLEGAPGADQ APWEKPQPLS SQRKPKIVGM KLREAQEDIV
DLDYFVSQHY KAKALRAAAM SGVVRRRSLQ KKEDVEDLQF EGGWRVKRDL GSQEENFGIE
PYPRAQSKHW MSLLSVGFSR LDVSLCVLLY LLSTMCLLAM YMYFKLRIKL RSAKVSLP
//
