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Peroxiredoxin-4 (EC 1.11.1.15) (Antioxidant enzyme AOE372) (AOE37-2) (Peroxiredoxin IV) (Prx-IV) (Thioredoxin peroxidase AO372) (Thioredoxin-dependent peroxide reductase A0372)

 PRDX4_HUMAN             Reviewed;         271 AA.
Q13162; Q6FHT3;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 176.
RecName: Full=Peroxiredoxin-4;
EC=1.11.1.15 {ECO:0000269|PubMed:21916849, ECO:0000269|PubMed:9388242};
AltName: Full=Antioxidant enzyme AOE372;
Short=AOE37-2;
AltName: Full=Peroxiredoxin IV;
Short=Prx-IV;
AltName: Full=Thioredoxin peroxidase AO372;
AltName: Full=Thioredoxin-dependent peroxide reductase A0372;
Flags: Precursor;
Name=PRDX4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, AND SUBUNIT.
PubMed=9388242; DOI=10.1074/jbc.272.49.30952;
Jin D.-Y., Chae H.Z., Rhee S.G., Jeang K.-T.;
"Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB
activation.";
J. Biol. Chem. 272:30952-30961(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[4]
PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 38-46.
TISSUE=Leukemic T-cell;
PubMed=19892738; DOI=10.1073/pnas.0908958106;
Xu G., Shin S.B., Jaffrey S.R.;
"Global profiling of protease cleavage sites by chemoselective
labeling of protein N-termini.";
Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
[5]
PROTEIN SEQUENCE OF 46-66; 81-99; 140-164; 174-208; 213-223 AND
231-263, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[6]
OVEROXIDATION AT CYS-124.
PubMed=12059788; DOI=10.1042/BJ20020525;
Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A.,
Leize-Wagner E., Rabilloud T.;
"A method for detection of overoxidation of cysteines: peroxiredoxins
are oxidized in vivo at the active-site cysteine during oxidative
stress.";
Biochem. J. 366:777-785(2002).
[7]
SUBCELLULAR LOCATION.
PubMed=18052930; DOI=10.1042/BJ20071428;
Tavender T.J., Sheppard A.M., Bulleid N.J.;
"Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming
oligomeric complexes in human cells.";
Biochem. J. 411:191-199(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-37, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[11]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS), AND DISULFIDE BONDS.
PubMed=21994946; DOI=10.1074/jbc.M111.298810;
Cao Z., Tavender T.J., Roszak A.W., Cogdell R.J., Bulleid N.J.;
"Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme
reveals a stable oxidized decamer and a non-disulfide-bonded
intermediate in the catalytic cycle.";
J. Biol. Chem. 286:42257-42266(2011).
[12]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND CATALYTIC ACTIVITY.
PubMed=21916849; DOI=10.1042/BJ20110380;
Wang X., Wang L., Wang X., Sun F., Wang C.C.;
"Structural insights into the peroxidase activity and inactivation of
human peroxiredoxin 4.";
Biochem. J. 441:113-118(2012).
-!- 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:0000269|PubMed:9388242}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:21916849, ECO:0000269|PubMed:9388242}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation
(PubMed:9388242). 5 homodimers assemble to form a ring-like
decamer (PubMed:21994946). Can form heterodimers with PRDX1
(PubMed:9388242). {ECO:0000269|PubMed:21994946,
ECO:0000269|PubMed:9388242}.
-!- INTERACTION:
P18428:LBP; NbExp=4; IntAct=EBI-2211957, EBI-3927059;
P07237:P4HB; NbExp=2; IntAct=EBI-2211957, EBI-395883;
P30101:PDIA3; NbExp=2; IntAct=EBI-2211957, EBI-979862;
Q15084:PDIA6; NbExp=2; IntAct=EBI-2211957, EBI-1043087;
P21731:TBXA2R; NbExp=3; IntAct=EBI-2211957, EBI-2625082;
Q8NBS9:TXNDC5; NbExp=2; IntAct=EBI-2211957, EBI-2510815;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18052930,
ECO:0000269|PubMed:9388242}. Endoplasmic reticulum
{ECO:0000269|PubMed:18052930}. Note=Cotranslationally translocated
to and retained within the endoplasmic reticulum. A small fraction
of the protein is cytoplasmic. {ECO:0000269|PubMed:18052930}.
-!- 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:0000269|PubMed:12059788,
ECO:0000269|PubMed:21916849}.
-!- 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:0000305|PubMed:21994946}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
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EMBL; U25182; AAB95175.1; -; mRNA.
EMBL; CR541668; CAG46469.1; -; mRNA.
EMBL; CR541705; CAG46506.1; -; mRNA.
EMBL; BC003609; AAH03609.1; -; mRNA.
EMBL; BC007107; AAH07107.1; -; mRNA.
EMBL; BC016770; AAH16770.1; -; mRNA.
CCDS; CCDS14206.1; -.
PIR; G01790; G01790.
RefSeq; NP_006397.1; NM_006406.1.
UniGene; Hs.83383; -.
PDB; 2PN8; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J=84-271.
PDB; 3TJB; X-ray; 2.38 A; A/B/C/D/E=38-271.
PDB; 3TJF; X-ray; 2.04 A; A/B/C/D/E=38-271.
PDB; 3TJG; X-ray; 2.24 A; A/B/C/D/E=38-271.
PDB; 3TJJ; X-ray; 1.91 A; A/B/C/D/E=38-271.
PDB; 3TJK; X-ray; 2.09 A; A/B/C/D/E=38-271.
PDB; 3TKP; X-ray; 2.49 A; A/B/C/D/E=38-271.
PDB; 3TKQ; X-ray; 2.22 A; A/B/C/D/E=38-271.
PDB; 3TKR; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=38-271.
PDB; 3TKS; X-ray; 2.40 A; A/B/C/D/E=38-271.
PDB; 4RQX; X-ray; 2.26 A; A/B/C/D/E=79-271.
PDB; 5HQP; X-ray; 2.60 A; A/B=38-271.
PDBsum; 2PN8; -.
PDBsum; 3TJB; -.
PDBsum; 3TJF; -.
PDBsum; 3TJG; -.
PDBsum; 3TJJ; -.
PDBsum; 3TJK; -.
PDBsum; 3TKP; -.
PDBsum; 3TKQ; -.
PDBsum; 3TKR; -.
PDBsum; 3TKS; -.
PDBsum; 4RQX; -.
PDBsum; 5HQP; -.
ProteinModelPortal; Q13162; -.
SMR; Q13162; -.
BioGrid; 115800; 58.
IntAct; Q13162; 50.
MINT; MINT-3027265; -.
STRING; 9606.ENSP00000368646; -.
PeroxiBase; 4530; Hs2CysPrx04.
iPTMnet; Q13162; -.
PhosphoSitePlus; Q13162; -.
SwissPalm; Q13162; -.
BioMuta; PRDX4; -.
DMDM; 3024727; -.
OGP; Q13162; -.
REPRODUCTION-2DPAGE; IPI00011937; -.
UCD-2DPAGE; Q13162; -.
EPD; Q13162; -.
PaxDb; Q13162; -.
PeptideAtlas; Q13162; -.
PRIDE; Q13162; -.
TopDownProteomics; Q13162; -.
DNASU; 10549; -.
Ensembl; ENST00000379341; ENSP00000368646; ENSG00000123131.
GeneID; 10549; -.
KEGG; hsa:10549; -.
CTD; 10549; -.
DisGeNET; 10549; -.
EuPathDB; HostDB:ENSG00000123131.12; -.
GeneCards; PRDX4; -.
HGNC; HGNC:17169; PRDX4.
HPA; CAB008659; -.
HPA; CAB027389; -.
HPA; CAB047362; -.
MIM; 300927; gene.
neXtProt; NX_Q13162; -.
OpenTargets; ENSG00000123131; -.
PharmGKB; PA33725; -.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00390000004653; -.
HOGENOM; HOG000022343; -.
HOVERGEN; HBG000286; -.
InParanoid; Q13162; -.
KO; K03386; -.
OMA; GWKPGQD; -.
OrthoDB; EOG091G0IE5; -.
PhylomeDB; Q13162; -.
TreeFam; TF105181; -.
BRENDA; 1.11.1.15; 2681.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; PRDX4; human.
EvolutionaryTrace; Q13162; -.
GeneWiki; PRDX4; -.
GenomeRNAi; 10549; -.
PRO; PR:Q13162; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000123131; -.
CleanEx; HS_PRDX4; -.
ExpressionAtlas; Q13162; baseline and differential.
Genevisible; Q13162; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0008379; F:thioredoxin peroxidase activity; TAS:ProtInc.
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:0007252; P:I-kappaB phosphorylation; TAS:ProtInc.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:2000255; P:negative regulation of male germ cell proliferation; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
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.
1: Evidence at protein level;
3D-structure; Antioxidant; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Oxidoreductase; Peroxidase; Redox-active center; Reference proteome;
Signal.
SIGNAL 1 37 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:19892738}.
CHAIN 38 271 Peroxiredoxin-4.
/FTId=PRO_0000135098.
DOMAIN 79 237 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 124 124 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000305|PubMed:12059788,
ECO:0000305|PubMed:21916849}.
MOD_RES 99 99 N6-succinyllysine.
{ECO:0000250|UniProtKB:P20108}.
DISULFID 124 124 Interchain (with C-245); in linked form.
{ECO:0000244|PDB:3TJB,
ECO:0000244|PDB:3TJG,
ECO:0000269|PubMed:21994946}.
DISULFID 245 245 Interchain (with C-124); in linked form.
{ECO:0000244|PDB:3TJB,
ECO:0000244|PDB:3TJG,
ECO:0000269|PubMed:21994946}.
CONFLICT 12 12 P -> S (in Ref. 3; CAG46469).
{ECO:0000305}.
CONFLICT 51 51 C -> Y (in Ref. 3; CAG46469).
{ECO:0000305}.
STRAND 75 78 {ECO:0000244|PDB:3TJK}.
STRAND 89 94 {ECO:0000244|PDB:2PN8}.
STRAND 97 102 {ECO:0000244|PDB:2PN8}.
HELIX 103 106 {ECO:0000244|PDB:2PN8}.
STRAND 109 115 {ECO:0000244|PDB:2PN8}.
HELIX 123 133 {ECO:0000244|PDB:2PN8}.
HELIX 135 139 {ECO:0000244|PDB:2PN8}.
TURN 140 142 {ECO:0000244|PDB:2PN8}.
STRAND 143 151 {ECO:0000244|PDB:2PN8}.
HELIX 153 160 {ECO:0000244|PDB:2PN8}.
HELIX 164 166 {ECO:0000244|PDB:2PN8}.
STRAND 176 178 {ECO:0000244|PDB:2PN8}.
STRAND 180 182 {ECO:0000244|PDB:5HQP}.
HELIX 183 187 {ECO:0000244|PDB:2PN8}.
TURN 193 195 {ECO:0000244|PDB:2PN8}.
STRAND 196 198 {ECO:0000244|PDB:2PN8}.
STRAND 200 205 {ECO:0000244|PDB:2PN8}.
STRAND 209 217 {ECO:0000244|PDB:2PN8}.
HELIX 225 241 {ECO:0000244|PDB:2PN8}.
TURN 260 262 {ECO:0000244|PDB:2PN8}.
HELIX 263 267 {ECO:0000244|PDB:2PN8}.
TURN 268 270 {ECO:0000244|PDB:3TKS}.
SEQUENCE 271 AA; 30540 MW; 7E56B580049FC60F CRC64;
MEALPLLAAT TPDHGRHRRL LLLPLLLFLL PAGAVQGWET EERPRTREEE CHFYAGGQVY
PGEASRVSVA DHSLHLSKAK ISKPAPYWEG TAVIDGEFKE LKLTDYRGKY LVFFFYPLDF
TFVCPTEIIA FGDRLEEFRS INTEVVACSV DSQFTHLAWI NTPRRQGGLG PIRIPLLSDL
THQISKDYGV YLEDSGHTLR GLFIIDDKGI LRQITLNDLP VGRSVDETLR LVQAFQYTDK
HGEVCPAGWK PGSETIIPDP AGKLKYFDKL N


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