PRDX2_PONAB
ID PRDX2_PONAB Reviewed; 177 AA.
AC Q5RC63;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Peroxiredoxin-2;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P32119};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 2 {ECO:0000305};
GN Name=PRDX2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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:0000250|UniProtKB:P32119}.
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:0000250|UniProtKB:P32119};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC assemble to form a ring-like decamer. Interacts with TIPIN.
CC {ECO:0000250|UniProtKB:P32119}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32119}.
CC -!- PTM: The enzyme can be inactivated by further oxidation of the cysteine
CC sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its
CC condensation to a disulfide bond. It can be reactivated by forming a
CC transient disulfide bond with sulfiredoxin SRXN1, which reduces the
CC cysteine sulfinic acid in an ATP- and Mg-dependent manner.
CC {ECO:0000250|UniProtKB:P32119, ECO:0000250|UniProtKB:Q06830}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000250|UniProtKB:P32119}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR858417; CAH90647.1; -; mRNA.
DR RefSeq; NP_001125349.1; NM_001131877.2.
DR AlphaFoldDB; Q5RC63; -.
DR SMR; Q5RC63; -.
DR STRING; 9601.ENSPPYP00000024125; -.
DR PeroxiBase; 4552; Ppy2CysPrx02.
DR Ensembl; ENSPPYT00000011193; ENSPPYP00000010771; ENSPPYG00000009607.
DR GeneID; 100172251; -.
DR KEGG; pon:100172251; -.
DR CTD; 7001; -.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000155828; -.
DR InParanoid; Q5RC63; -.
DR Proteomes; UP000001595; Chromosome 19.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:Ensembl.
DR GO; GO:0002357; P:defense response to tumor cell; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:Ensembl.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Antioxidant; Cytoplasm; Disulfide bond; Oxidoreductase;
KW Peroxidase; Phosphoprotein; Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT CHAIN 2..177
FT /note="Peroxiredoxin-2"
FT /id="PRO_0000256857"
FT DOMAIN 6..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT DISULFID 51
FT /note="Interchain (with C-173); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT DISULFID 173
FT /note="Interchain (with C-51); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P32119"
SQ SEQUENCE 177 AA; 19430 MW; 6D95970252096370 CRC64;
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN
RAEDFHKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT
DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE GPCFASP
