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Peroxiredoxin-4 (EC 1.11.1.15) (Antioxidant enzyme AOE372) (Peroxiredoxin IV) (Prx-IV) (Thioredoxin peroxidase AO372) (Thioredoxin-dependent peroxide reductase A0372)

 PRDX4_RAT               Reviewed;         273 AA.
Q9Z0V5;
19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 121.
RecName: Full=Peroxiredoxin-4;
EC=1.11.1.15;
AltName: Full=Antioxidant enzyme AOE372;
AltName: Full=Peroxiredoxin IV;
Short=Prx-IV;
AltName: Full=Thioredoxin peroxidase AO372;
AltName: Full=Thioredoxin-dependent peroxide reductase A0372;
Flags: Precursor;
Name=Prdx4; Synonyms=Rno2CysPrx04;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=10025941; DOI=10.1016/S0014-5793(98)01736-0;
Matsumoto A., Okado A., Fujii T., Fujii J., Egashira M., Niikawa N.,
Taniguchi N.;
"Cloning of the peroxiredoxin gene family in rats and characterization
of the fourth member.";
FEBS Lett. 443:246-250(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10731722; DOI=10.1093/oxfordjournals.jbchem.a022632;
Okado-Matsumoto A., Matsumoto A., Fujii J., Taniguchi N.;
"Peroxiredoxin IV is a secretable protein with heparin-binding
properties under reduced conditions.";
J. Biochem. 127:493-501(2000).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides and as sensor of
hydrogen peroxide-mediated signaling events. Regulates the
activation of NF-kappa-B in the cytosol by a modulation of I-
kappa-B-alpha phosphorylation. {ECO:0000250|UniProtKB:Q13162}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000250|UniProtKB:Q13162}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
assemble to form a ring-like decamer.
{ECO:0000250|UniProtKB:Q13162}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13162}.
Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13162}. Secreted
{ECO:0000269|PubMed:10025941, ECO:0000269|PubMed:10731722}.
-!- PTM: The enzyme can be inactivated by further oxidation of the
cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H)
and sulphonic acid (C(P)-SO3H) instead of its condensation to a
disulfide bond. {ECO:0000250|UniProtKB:Q13162}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by
the other dimeric subunit to form an intersubunit disulfide. The
disulfide is subsequently reduced by thioredoxin.
{ECO:0000250|UniProtKB:Q13162}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF106945; AAD17993.1; -; mRNA.
EMBL; BC059122; AAH59122.1; -; mRNA.
RefSeq; NP_445964.1; NM_053512.2.
UniGene; Rn.17958; -.
ProteinModelPortal; Q9Z0V5; -.
SMR; Q9Z0V5; -.
IntAct; Q9Z0V5; 2.
STRING; 10116.ENSRNOP00000005014; -.
PeroxiBase; 4533; Rno2CysPrx04.
iPTMnet; Q9Z0V5; -.
PhosphoSitePlus; Q9Z0V5; -.
PaxDb; Q9Z0V5; -.
PRIDE; Q9Z0V5; -.
Ensembl; ENSRNOT00000005014; ENSRNOP00000005014; ENSRNOG00000003763.
GeneID; 85274; -.
KEGG; rno:85274; -.
CTD; 10549; -.
RGD; 620043; Prdx4.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00390000004653; -.
HOGENOM; HOG000022343; -.
HOVERGEN; HBG000286; -.
InParanoid; Q9Z0V5; -.
KO; K03386; -.
OMA; GWKPGQD; -.
OrthoDB; EOG091G0IE5; -.
PhylomeDB; Q9Z0V5; -.
TreeFam; TF105181; -.
BRENDA; 1.11.1.15; 5301.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:Q9Z0V5; -.
Proteomes; UP000002494; Chromosome X.
Bgee; ENSRNOG00000003763; -.
Genevisible; Q9Z0V5; RN.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0019471; P:4-hydroxyproline metabolic process; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:2000255; P:negative regulation of male germ cell proliferation; IEA:Ensembl.
GO; GO:0022417; P:protein maturation by protein folding; IEA:Ensembl.
GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
2: Evidence at transcript level;
Antioxidant; Complete proteome; Cytoplasm; Disulfide bond;
Endoplasmic reticulum; Oxidoreductase; Peroxidase;
Redox-active center; Reference proteome; Secreted; Signal.
SIGNAL 1 40 {ECO:0000250}.
CHAIN 41 273 Peroxiredoxin-4.
/FTId=PRO_0000390877.
DOMAIN 81 239 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 126 126 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:Q13162}.
MOD_RES 101 101 N6-succinyllysine.
{ECO:0000250|UniProtKB:P20108}.
DISULFID 126 126 Interchain (with C-247); in linked form.
{ECO:0000250|UniProtKB:Q13162}.
DISULFID 247 247 Interchain (with C-126); in linked form.
{ECO:0000250|UniProtKB:Q13162}.
SEQUENCE 273 AA; 31007 MW; 09E614794F1DC6C2 CRC64;
METWSKLLDG TTPSRRWRKL VLLLPPLLLF LLQTEALQGL ESDDRFRTRE NECHFYAGGQ
VYPGEVSRVS VADHSLHLSK AKISKPAPYW EGTAVINGEF KELKLTDYRG KYLVFFFYPL
DFTFVCPTEI IAFGDRIEEF KSINTEVVAC SVDSQFTHLA WINTPRRQGG LGPIRIPLLS
DLNHQISKDY GVYLEDSGHT LRGLFIIDDK GVLRQITLND LPVGRSVDET LRLVQAFQYT
DKHGEVCPAG WKPGSETIIP DPAGKLKYFD KLN


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