ID   QSOX2_XENLA             Reviewed;         661 AA.
AC   Q6AX23;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Sulfhydryl oxidase 2;
DE            EC=1.8.3.2;
DE   AltName: Full=Quiescin Q6-like protein 1;
DE   Flags: Precursor;
GN   Name=qsox2; Synonyms=qscn6l1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) 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. May contribute to disulfide bond formation in a variety of
CC       secreted proteins (By similarity). {ECO:0000250}.
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   -!- 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
CC       {ECO:0000305}.
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DR   EMBL; BC079798; AAH79798.1; -; mRNA.
DR   RefSeq; NP_001087446.1; NM_001093977.1.
DR   AlphaFoldDB; Q6AX23; -.
DR   SMR; Q6AX23; -.
DR   GlyCosmos; Q6AX23; 2 sites, No reported glycans.
DR   DNASU; 447270; -.
DR   GeneID; 447270; -.
DR   KEGG; xla:447270; -.
DR   AGR; Xenbase:XB-GENE-986401; -.
DR   CTD; 447270; -.
DR   Xenbase; XB-GENE-986401; qsox2.S.
DR   OrthoDB; 20090at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 447270; Expressed in blastula and 19 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Membrane; Oxidoreductase;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..661
FT                   /note="Sulfhydryl oxidase 2"
FT                   /id="PRO_0000249540"
FT   TRANSMEM        625..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..155
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          400..509
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   ACT_SITE        67
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        70
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         405
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         412
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         416
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         457
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         461
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   BINDING         484..491
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   BINDING         509
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        67..70
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT                   ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        98..107
FT                   /evidence="ECO:0000250|UniProtKB:O00391"
FT   DISULFID        397..409
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        455..458
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        515..518
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ   SEQUENCE   661 AA;  75121 MW;  6D2CF79098B20188 CRC64;
     MAAFVGLPLR SVPMLLLLLL LVVAGTARGE TLYGPEDSVT ILNKESVARA VFNSSSAWLL
     EFYSSWCGHC INYAPTWKAL ARDVRDWEPA IKIGVLDCAE EDNYGACKDF GVTLYPTFRF
     FKAFTKEFTQ GENYKAVGDR EIQTVRQVII DFLQTSPAES KPQAWPSLEP ISSSEISSLL
     TPKQSHYTAI IFESEESYEG REVILDLIQY SNIVVRRALP SDKPILEKLG IGSVPSCYLI
     QPNGLHGLIN DVKSIRSQLS LHLKALSNVR KLLPSETAHS GLSKGVQQED TTMNQFDRSK
     LYMTDLESGL HYILRAELAN HHTLEGEKLK TFKDFVTILY KLFPGRPHVM KLLETLQEWL
     VSMPLDTIPY DAILDLVNNK MRISGIFLTN HTQWVGCRGS KSNLRGYPCS LWKLFHSLTV
     QAAVKPDALA NTAFEAEPRA VLQTMRRYIR EFFGCRECAK HFEAMAKETV DSVKTPDQAI
     LWLWRKHNVV NNRLSGAPSE DPKFPKVQWP TSDLCSACHS QTGGVHSWNE DEVLAFLKRY
     YGNQEISLEF ADPRKDLSEA ATDNGNKEPH FTKKPQERDY VKKQNPQFLD KLVQKKPEKS
     LDSEAAESSQ SVSFLGIGFS NIDMSLCVIL YVTSSLFLMI MFFFFRFRSK RWKVRYNRPF
     V
//