GenomeNet

Database: UniProt
Entry: A0A0P7WJH6_SCLFO
LinkDB: A0A0P7WJH6_SCLFO
Original site: A0A0P7WJH6_SCLFO 
ID   A0A0P7WJH6_SCLFO        Unreviewed;       239 AA.
AC   A0A0P7WJH6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Peroxiredoxin-2 {ECO:0000256|ARBA:ARBA00040770};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin 2 {ECO:0000256|ARBA:ARBA00042159};
GN   ORFNames=Z043_117832 {ECO:0000313|EMBL:KPP63870.1};
OS   Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX   NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP63870.1, ECO:0000313|Proteomes:UP000034805};
RN   [1] {ECO:0000313|EMBL:KPP63870.1, ECO:0000313|Proteomes:UP000034805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aro1 {ECO:0000313|EMBL:KPP63870.1};
RA   Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT   "The genome of the Asian arowana (Scleropages formosus).";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC       signaling events. Might participate in the signaling cascades of growth
CC       factors and tumor necrosis factor-alpha by regulating the intracellular
CC       concentrations of H(2)O(2). {ECO:0000256|ARBA:ARBA00037127}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00000280};
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009796}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPP63870.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JARO02007507; KPP63870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7WJH6; -.
DR   STRING; 113540.ENSSFOP00015021813; -.
DR   Proteomes; UP000034805; Unassembled WGS sequence.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF161; PEROXIREDOXIN-2; 1.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 3.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|PIRNR:PIRNR000239};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000239};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR000239};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRNR:PIRNR000239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034805}.
FT   DOMAIN          6..205
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        92
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   239 AA;  26625 MW;  5E3154A9D36A62DE CRC64;
     MSAGNAKIGQ PAPQFKATAV VEGRFRELQL ADYRGDCLSL RLCDTPCPRP RDLDTVGRRV
     SELLRLKGAP FFLRSGKYVV LFFYPLDFTF VCPTEIVAFS DRAEEFRSVG CEVLAASTDS
     HFSHLAWINT ERKQGGLGTM NIPLIADLTK SISQDYGVLK EDEGIAYRGL FVIDDKGILR
     QITINDLPVG RSVDETLRLV QAFQHTDKFG EVCPAGWKPG SDTIIPDVQK SKEFFAKQD
//
DBGET integrated database retrieval system