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Database: UniProt
Entry: Q95QF9_CAEEL
LinkDB: Q95QF9_CAEEL
Original site: Q95QF9_CAEEL 
ID   Q95QF9_CAEEL            Unreviewed;       624 AA.
AC   Q95QF9;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   ORFNames=CELE_F47B7.2 {ECO:0000313|EMBL:CCD70493.1}, F47B7.2
GN   {ECO:0000313|EMBL:CCD70493.1, ECO:0000313|WormBase:F47B7.2c};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD70493.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CCD70493.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD70493.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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|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}.
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DR   EMBL; BX284606; CCD70493.1; -; Genomic_DNA.
DR   RefSeq; NP_508653.1; NM_076252.4.
DR   AlphaFoldDB; Q95QF9; -.
DR   SMR; Q95QF9; -.
DR   EPD; Q95QF9; -.
DR   EnsemblMetazoa; F47B7.2c.1; F47B7.2c.1; WBGene00018533.
DR   GeneID; 180664; -.
DR   UCSC; F47B7.2c; c. elegans.
DR   AGR; WB:WBGene00018533; -.
DR   WormBase; F47B7.2c; CE28395; WBGene00018533; -.
DR   HOGENOM; CLU_020182_0_0_1; -.
DR   OrthoDB; 20090at2759; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00018533; Expressed in embryo and 4 other cell types or tissues.
DR   ExpressionAtlas; Q95QF9; baseline and differential.
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; 1.
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; 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:SF8; SULFHYDRYL OXIDASE; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   Pfam; PF18371; FAD_SOX; 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   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|EPD:Q95QF9,
KW   ECO:0007829|PeptideAtlas:Q95QF9};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   Transmembrane {ECO:0000256|RuleBase:RU371123};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU371123"
FT   DOMAIN          24..164
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          410..517
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
SQ   SEQUENCE   624 AA;  70048 MW;  A72E1B3AC5A92E90 CRC64;
     MNEKEPGVAK SLCIAAVITG VFMLFILVVI LAFSAGGSSG ESLYDKDDPI LELDVDTFSA
     AIYGSKKAHF IEFYSSWCGA CIGYAPTFKK FAKQLEKWAP LVQVTVVNCA DDKNMPLCRE
     HSVSSYPSLR YFKYNSHNKD DGMKYSGDKY DINKLAHDIA GLAQADAQKQ NPESWPTFLP
     LSDTTTLEEV FKSIGTTSYL AIVVQDSPSV IAWANLINYH GNNGVKVAYV TQNHPIATKF
     FSDGGVHALL FSNGNQEPLW KSSSPVDKWV DVQDKIDELI GDKIAASGPT VHPINAAPVI
     AAPSNPLNNQ YEVQLVDLKS AMSYMLYKEI PRREEIRDEP MAVLKQWMHT LKKYAPGTTP
     MRRLFFRLDE WIQLQSVVTA NEWITKVDEI QQALGNPLPK EITWMACAGS KPNLRGYTCG
     LWTLAHTITV EAYKQEKHNT AFKPVIDVLE PFRAFIFHFL SCSECAQNFT KEAEKNQLHL
     VTRPEDVYAW LWRVHNFVNK RLSGSLTDDP SFKKQQFPPK SLCADCYDAN GDIDEAKALP
     FVFKYYSNIK TDSTDNLPGY KVVEYKEGKT LSAGQRHLNP KFQVHAGKVD QLEANDKVKN
     VLDASPQRTW KDIDGYGVLG VPHR
//
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