QSOX2_XENLA
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 03-AUG-2022, entry version 85.
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 DNASU; 447270; -.
DR GeneID; 447270; -.
DR KEGG; xla:447270; -.
DR CTD; 447270; -.
DR Xenbase; XB-GENE-986401; qsox2.S.
DR OrthoDB; 498515at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 447270; Expressed in blastula and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IEA:InterPro.
DR Gene3D; 1.20.120.1960; -; 1.
DR Gene3D; 1.20.120.310; -; 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; PTHR22897; 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; SSF52833; SSF52833; 1.
DR SUPFAM; SSF69000; SSF69000; 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
