Full text data of PRDX4
PRDX4
[Confidence: high (present in two of the MS resources)]
Peroxiredoxin-4; 1.11.1.15 (Antioxidant enzyme AOE372; AOE37-2; Peroxiredoxin IV; Prx-IV; Thioredoxin peroxidase AO372; Thioredoxin-dependent peroxide reductase A0372; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Peroxiredoxin-4; 1.11.1.15 (Antioxidant enzyme AOE372; AOE37-2; Peroxiredoxin IV; Prx-IV; Thioredoxin peroxidase AO372; Thioredoxin-dependent peroxide reductase A0372; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q13162
ID PRDX4_HUMAN Reviewed; 271 AA.
AC Q13162; Q6FHT3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Peroxiredoxin-4;
DE EC=1.11.1.15;
DE AltName: Full=Antioxidant enzyme AOE372;
DE Short=AOE37-2;
DE AltName: Full=Peroxiredoxin IV;
DE Short=Prx-IV;
DE AltName: Full=Thioredoxin peroxidase AO372;
DE AltName: Full=Thioredoxin-dependent peroxide reductase A0372;
DE Flags: Precursor;
GN Name=PRDX4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=9388242; DOI=10.1074/jbc.272.49.30952;
RA Jin D.-Y., Chae H.Z., Rhee S.G., Jeang K.-T.;
RT "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB
RT activation.";
RL J. Biol. Chem. 272:30952-30961(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 38-46.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective
RT labeling of protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [5]
RP PROTEIN SEQUENCE OF 46-66; 81-99; 140-164; 174-208; 213-223 AND
RP 231-263, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP OVEROXIDATION AT CYS-124.
RX PubMed=12059788; DOI=10.1042/BJ20020525;
RA Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A.,
RA Leize-Wagner E., Rabilloud T.;
RT "A method for detection of overoxidation of cysteines: peroxiredoxins
RT are oxidized in vivo at the active-site cysteine during oxidative
RT stress.";
RL Biochem. J. 366:777-785(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Probably involved in redox regulation of the cell.
CC Regulates the activation of NF-kappa-B in the cytosol by a
CC modulation of I-kappa-B-alpha phosphorylation.
CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC -!- SUBUNIT: Homodimer or heterodimer with PRDX1; disulfide-linked,
CC upon oxidation (By similarity).
CC -!- INTERACTION:
CC P18428:LBP; NbExp=4; IntAct=EBI-2211957, EBI-3927059;
CC P07237:P4HB; NbExp=2; IntAct=EBI-2211957, EBI-395883;
CC P30101:PDIA3; NbExp=2; IntAct=EBI-2211957, EBI-979862;
CC Q15084:PDIA6; NbExp=2; IntAct=EBI-2211957, EBI-1043087;
CC P21731:TBXA2R; NbExp=3; IntAct=EBI-2211957, EBI-2625082;
CC Q8NBS9:TXNDC5; NbExp=2; IntAct=EBI-2211957, EBI-2510815;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted.
CC -!- MISCELLANEOUS: The active site is the redox-active Cys-124
CC oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-245-SH of the
CC other subunit to form an intermolecular disulfide with a
CC concomitant homodimer formation. The enzyme may be subsequently
CC regenerated by reduction of the disulfide by thioredoxin.
CC -!- MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-
CC 124 (to Cys-SO(3)H) upon oxidative stress.
CC -!- SIMILARITY: Belongs to the AhpC/TSA family.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR EMBL; U25182; AAB95175.1; -; mRNA.
DR EMBL; CR541668; CAG46469.1; -; mRNA.
DR EMBL; CR541705; CAG46506.1; -; mRNA.
DR EMBL; BC003609; AAH03609.1; -; mRNA.
DR EMBL; BC007107; AAH07107.1; -; mRNA.
DR EMBL; BC016770; AAH16770.1; -; mRNA.
DR PIR; G01790; G01790.
DR RefSeq; NP_006397.1; NM_006406.1.
DR UniGene; Hs.83383; -.
DR PDB; 2PN8; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J=84-271.
DR PDB; 3TJB; X-ray; 2.38 A; A/B/C/D/E=38-271.
DR PDB; 3TJF; X-ray; 2.04 A; A/B/C/D/E=38-271.
DR PDB; 3TJG; X-ray; 2.24 A; A/B/C/D/E=38-271.
DR PDB; 3TJJ; X-ray; 1.91 A; A/B/C/D/E=38-271.
DR PDB; 3TJK; X-ray; 2.09 A; A/B/C/D/E=38-271.
DR PDB; 3TKP; X-ray; 2.49 A; A/B/C/D/E=38-271.
DR PDB; 3TKQ; X-ray; 2.22 A; A/B/C/D/E=38-271.
DR PDB; 3TKR; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=38-271.
DR PDB; 3TKS; X-ray; 2.40 A; A/B/C/D/E=38-271.
DR PDBsum; 2PN8; -.
DR PDBsum; 3TJB; -.
DR PDBsum; 3TJF; -.
DR PDBsum; 3TJG; -.
DR PDBsum; 3TJJ; -.
DR PDBsum; 3TJK; -.
DR PDBsum; 3TKP; -.
DR PDBsum; 3TKQ; -.
DR PDBsum; 3TKR; -.
DR PDBsum; 3TKS; -.
DR ProteinModelPortal; Q13162; -.
DR SMR; Q13162; 74-269.
DR IntAct; Q13162; 43.
DR MINT; MINT-3027265; -.
DR STRING; 9606.ENSP00000368646; -.
DR PeroxiBase; 4530; Hs2CysPrx04.
DR PhosphoSite; Q13162; -.
DR DMDM; 3024727; -.
DR OGP; Q13162; -.
DR REPRODUCTION-2DPAGE; IPI00011937; -.
DR UCD-2DPAGE; Q13162; -.
DR PaxDb; Q13162; -.
DR PeptideAtlas; Q13162; -.
DR PRIDE; Q13162; -.
DR DNASU; 10549; -.
DR Ensembl; ENST00000379341; ENSP00000368646; ENSG00000123131.
DR GeneID; 10549; -.
DR KEGG; hsa:10549; -.
DR UCSC; uc004dam.3; human.
DR CTD; 10549; -.
DR GeneCards; GC0XP023592; -.
DR HGNC; HGNC:17169; PRDX4.
DR HPA; CAB008659; -.
DR HPA; CAB027389; -.
DR MIM; 606506; gene.
DR neXtProt; NX_Q13162; -.
DR PharmGKB; PA33725; -.
DR eggNOG; COG0450; -.
DR HOGENOM; HOG000022343; -.
DR HOVERGEN; HBG000286; -.
DR InParanoid; Q13162; -.
DR KO; K03386; -.
DR OMA; GKINYYM; -.
DR PhylomeDB; Q13162; -.
DR EvolutionaryTrace; Q13162; -.
DR GeneWiki; PRDX4; -.
DR GenomeRNAi; 10549; -.
DR NextBio; 40013; -.
DR PRO; PR:Q13162; -.
DR ArrayExpress; Q13162; -.
DR Bgee; Q13162; -.
DR CleanEx; HS_PRDX4; -.
DR Genevestigator; Q13162; -.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; TAS:ProtInc.
DR GO; GO:0007252; P:I-kappaB phosphorylation; TAS:ProtInc.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome; Secreted; Signal.
FT SIGNAL 1 37
FT CHAIN 38 271 Peroxiredoxin-4.
FT /FTId=PRO_0000135098.
FT DOMAIN 79 237 Thioredoxin.
FT ACT_SITE 124 124 Cysteine sulfenic acid (-SOH)
FT intermediate (By similarity).
FT DISULFID 124 124 Interchain (with C-245); in linked form
FT (By similarity).
FT DISULFID 245 245 Interchain (with C-124); in linked form
FT (By similarity).
FT CONFLICT 12 12 P -> S (in Ref. 3; CAG46469).
FT CONFLICT 51 51 C -> Y (in Ref. 3; CAG46469).
FT STRAND 75 78
FT STRAND 89 94
FT STRAND 97 102
FT HELIX 103 106
FT STRAND 109 115
FT HELIX 123 133
FT HELIX 135 139
FT TURN 140 142
FT STRAND 143 151
FT HELIX 153 160
FT HELIX 164 166
FT STRAND 176 178
FT HELIX 183 187
FT TURN 193 195
FT STRAND 196 198
FT STRAND 200 205
FT STRAND 209 217
FT HELIX 225 241
FT TURN 260 262
FT HELIX 263 267
FT TURN 268 270
SQ 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
//
ID PRDX4_HUMAN Reviewed; 271 AA.
AC Q13162; Q6FHT3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Peroxiredoxin-4;
DE EC=1.11.1.15;
DE AltName: Full=Antioxidant enzyme AOE372;
DE Short=AOE37-2;
DE AltName: Full=Peroxiredoxin IV;
DE Short=Prx-IV;
DE AltName: Full=Thioredoxin peroxidase AO372;
DE AltName: Full=Thioredoxin-dependent peroxide reductase A0372;
DE Flags: Precursor;
GN Name=PRDX4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=9388242; DOI=10.1074/jbc.272.49.30952;
RA Jin D.-Y., Chae H.Z., Rhee S.G., Jeang K.-T.;
RT "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB
RT activation.";
RL J. Biol. Chem. 272:30952-30961(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 38-46.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective
RT labeling of protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [5]
RP PROTEIN SEQUENCE OF 46-66; 81-99; 140-164; 174-208; 213-223 AND
RP 231-263, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP OVEROXIDATION AT CYS-124.
RX PubMed=12059788; DOI=10.1042/BJ20020525;
RA Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A.,
RA Leize-Wagner E., Rabilloud T.;
RT "A method for detection of overoxidation of cysteines: peroxiredoxins
RT are oxidized in vivo at the active-site cysteine during oxidative
RT stress.";
RL Biochem. J. 366:777-785(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Probably involved in redox regulation of the cell.
CC Regulates the activation of NF-kappa-B in the cytosol by a
CC modulation of I-kappa-B-alpha phosphorylation.
CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC -!- SUBUNIT: Homodimer or heterodimer with PRDX1; disulfide-linked,
CC upon oxidation (By similarity).
CC -!- INTERACTION:
CC P18428:LBP; NbExp=4; IntAct=EBI-2211957, EBI-3927059;
CC P07237:P4HB; NbExp=2; IntAct=EBI-2211957, EBI-395883;
CC P30101:PDIA3; NbExp=2; IntAct=EBI-2211957, EBI-979862;
CC Q15084:PDIA6; NbExp=2; IntAct=EBI-2211957, EBI-1043087;
CC P21731:TBXA2R; NbExp=3; IntAct=EBI-2211957, EBI-2625082;
CC Q8NBS9:TXNDC5; NbExp=2; IntAct=EBI-2211957, EBI-2510815;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted.
CC -!- MISCELLANEOUS: The active site is the redox-active Cys-124
CC oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-245-SH of the
CC other subunit to form an intermolecular disulfide with a
CC concomitant homodimer formation. The enzyme may be subsequently
CC regenerated by reduction of the disulfide by thioredoxin.
CC -!- MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-
CC 124 (to Cys-SO(3)H) upon oxidative stress.
CC -!- SIMILARITY: Belongs to the AhpC/TSA family.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U25182; AAB95175.1; -; mRNA.
DR EMBL; CR541668; CAG46469.1; -; mRNA.
DR EMBL; CR541705; CAG46506.1; -; mRNA.
DR EMBL; BC003609; AAH03609.1; -; mRNA.
DR EMBL; BC007107; AAH07107.1; -; mRNA.
DR EMBL; BC016770; AAH16770.1; -; mRNA.
DR PIR; G01790; G01790.
DR RefSeq; NP_006397.1; NM_006406.1.
DR UniGene; Hs.83383; -.
DR PDB; 2PN8; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J=84-271.
DR PDB; 3TJB; X-ray; 2.38 A; A/B/C/D/E=38-271.
DR PDB; 3TJF; X-ray; 2.04 A; A/B/C/D/E=38-271.
DR PDB; 3TJG; X-ray; 2.24 A; A/B/C/D/E=38-271.
DR PDB; 3TJJ; X-ray; 1.91 A; A/B/C/D/E=38-271.
DR PDB; 3TJK; X-ray; 2.09 A; A/B/C/D/E=38-271.
DR PDB; 3TKP; X-ray; 2.49 A; A/B/C/D/E=38-271.
DR PDB; 3TKQ; X-ray; 2.22 A; A/B/C/D/E=38-271.
DR PDB; 3TKR; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=38-271.
DR PDB; 3TKS; X-ray; 2.40 A; A/B/C/D/E=38-271.
DR PDBsum; 2PN8; -.
DR PDBsum; 3TJB; -.
DR PDBsum; 3TJF; -.
DR PDBsum; 3TJG; -.
DR PDBsum; 3TJJ; -.
DR PDBsum; 3TJK; -.
DR PDBsum; 3TKP; -.
DR PDBsum; 3TKQ; -.
DR PDBsum; 3TKR; -.
DR PDBsum; 3TKS; -.
DR ProteinModelPortal; Q13162; -.
DR SMR; Q13162; 74-269.
DR IntAct; Q13162; 43.
DR MINT; MINT-3027265; -.
DR STRING; 9606.ENSP00000368646; -.
DR PeroxiBase; 4530; Hs2CysPrx04.
DR PhosphoSite; Q13162; -.
DR DMDM; 3024727; -.
DR OGP; Q13162; -.
DR REPRODUCTION-2DPAGE; IPI00011937; -.
DR UCD-2DPAGE; Q13162; -.
DR PaxDb; Q13162; -.
DR PeptideAtlas; Q13162; -.
DR PRIDE; Q13162; -.
DR DNASU; 10549; -.
DR Ensembl; ENST00000379341; ENSP00000368646; ENSG00000123131.
DR GeneID; 10549; -.
DR KEGG; hsa:10549; -.
DR UCSC; uc004dam.3; human.
DR CTD; 10549; -.
DR GeneCards; GC0XP023592; -.
DR HGNC; HGNC:17169; PRDX4.
DR HPA; CAB008659; -.
DR HPA; CAB027389; -.
DR MIM; 606506; gene.
DR neXtProt; NX_Q13162; -.
DR PharmGKB; PA33725; -.
DR eggNOG; COG0450; -.
DR HOGENOM; HOG000022343; -.
DR HOVERGEN; HBG000286; -.
DR InParanoid; Q13162; -.
DR KO; K03386; -.
DR OMA; GKINYYM; -.
DR PhylomeDB; Q13162; -.
DR EvolutionaryTrace; Q13162; -.
DR GeneWiki; PRDX4; -.
DR GenomeRNAi; 10549; -.
DR NextBio; 40013; -.
DR PRO; PR:Q13162; -.
DR ArrayExpress; Q13162; -.
DR Bgee; Q13162; -.
DR CleanEx; HS_PRDX4; -.
DR Genevestigator; Q13162; -.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; TAS:ProtInc.
DR GO; GO:0007252; P:I-kappaB phosphorylation; TAS:ProtInc.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome; Secreted; Signal.
FT SIGNAL 1 37
FT CHAIN 38 271 Peroxiredoxin-4.
FT /FTId=PRO_0000135098.
FT DOMAIN 79 237 Thioredoxin.
FT ACT_SITE 124 124 Cysteine sulfenic acid (-SOH)
FT intermediate (By similarity).
FT DISULFID 124 124 Interchain (with C-245); in linked form
FT (By similarity).
FT DISULFID 245 245 Interchain (with C-124); in linked form
FT (By similarity).
FT CONFLICT 12 12 P -> S (in Ref. 3; CAG46469).
FT CONFLICT 51 51 C -> Y (in Ref. 3; CAG46469).
FT STRAND 75 78
FT STRAND 89 94
FT STRAND 97 102
FT HELIX 103 106
FT STRAND 109 115
FT HELIX 123 133
FT HELIX 135 139
FT TURN 140 142
FT STRAND 143 151
FT HELIX 153 160
FT HELIX 164 166
FT STRAND 176 178
FT HELIX 183 187
FT TURN 193 195
FT STRAND 196 198
FT STRAND 200 205
FT STRAND 209 217
FT HELIX 225 241
FT TURN 260 262
FT HELIX 263 267
FT TURN 268 270
SQ 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
//
MIM
606506
*RECORD*
*FIELD* NO
606506
*FIELD* TI
*606506 PEROXIREDOXIN 4; PRDX4
;;ANTIOXIDANT ENZYME 372; AOE372
*FIELD* TX
Antioxidants govern intracellular reduction-oxidation (redox) status,
read morewhich plays a critical role in NFKB (see 164011) transcription factor
activation. Different antioxidants are selective for redox regulation of
certain transcription factors.
CLONING
Using a yeast 2-hybrid screen of a HeLa cell cDNA library with PAG
(PRDX1; 176763) as bait, followed by 5-prime RACE, Jin et al. (1997)
isolated cDNAs encoding PRDX4, which they termed 'antioxidant enzyme
AOE372.' Sequence analysis predicted that the 271-amino acid protein,
70% identical to a yeast thiol-specific antioxidant, contains a signal
peptide and 2 peroxide catalysis cysteine motifs conserved in all human
peroxiredoxins. Functional analysis showed that PRDX4 protects glutamine
synthetase (GLUL; 138290) from inactivation. Northern blot analysis
revealed ubiquitous expression of a 1.0-kb transcript in numerous cell
lines and variable expression in tissues, with highest expression in
pancreas and none detected in peripheral blood leukocytes. Western blot
analysis showed expression of a 23-kD protein with highest levels in
pancreas, followed by liver, heart, spleen, and thymus. Confocal
microscopy as well as immunoblotting demonstrated predominant
cytoplasmic expression. Yeast 2-hybrid, immunoprecipitation, and
immunoblot analyses indicated that PRDX4 and PRDX1 are capable of
homodimerization and heterodimerization with each other but not with the
mitochondrial PRDX3 (604769). Gel mobility shift and immunoblot analysis
found that PRDX4 depletes NFKB binding activity together with a
reduction in the amounts of p50, p65 (RELA; 164014), and phosphorylated
IKBA (164008), as well as a reduction in the expression of HIV-1 viral
proteins. Expression of PRDX4, alone or with PRDX1, increased the
resistance of yeast cells to oxidant-induced toxicity. Jin et al. (1997)
suggested PRDX4 modulates IKBA phosphorylation in the cytoplasm and thus
affects a peroxiredoxin-dependent redox step.
*FIELD* RF
1. Jin, D.-Y; Chae, H. Z; Rhee, S. G; Jeang, K.-T: Regulatory role
for a novel human thioredoxin peroxidase in NF-kappa-B activation. J.
Biol. Chem. 272: 30952-30961, 1997.
*FIELD* CD
Paul J. Converse: 11/27/2001
*FIELD* ED
alopez: 11/27/2001
*RECORD*
*FIELD* NO
606506
*FIELD* TI
*606506 PEROXIREDOXIN 4; PRDX4
;;ANTIOXIDANT ENZYME 372; AOE372
*FIELD* TX
Antioxidants govern intracellular reduction-oxidation (redox) status,
read morewhich plays a critical role in NFKB (see 164011) transcription factor
activation. Different antioxidants are selective for redox regulation of
certain transcription factors.
CLONING
Using a yeast 2-hybrid screen of a HeLa cell cDNA library with PAG
(PRDX1; 176763) as bait, followed by 5-prime RACE, Jin et al. (1997)
isolated cDNAs encoding PRDX4, which they termed 'antioxidant enzyme
AOE372.' Sequence analysis predicted that the 271-amino acid protein,
70% identical to a yeast thiol-specific antioxidant, contains a signal
peptide and 2 peroxide catalysis cysteine motifs conserved in all human
peroxiredoxins. Functional analysis showed that PRDX4 protects glutamine
synthetase (GLUL; 138290) from inactivation. Northern blot analysis
revealed ubiquitous expression of a 1.0-kb transcript in numerous cell
lines and variable expression in tissues, with highest expression in
pancreas and none detected in peripheral blood leukocytes. Western blot
analysis showed expression of a 23-kD protein with highest levels in
pancreas, followed by liver, heart, spleen, and thymus. Confocal
microscopy as well as immunoblotting demonstrated predominant
cytoplasmic expression. Yeast 2-hybrid, immunoprecipitation, and
immunoblot analyses indicated that PRDX4 and PRDX1 are capable of
homodimerization and heterodimerization with each other but not with the
mitochondrial PRDX3 (604769). Gel mobility shift and immunoblot analysis
found that PRDX4 depletes NFKB binding activity together with a
reduction in the amounts of p50, p65 (RELA; 164014), and phosphorylated
IKBA (164008), as well as a reduction in the expression of HIV-1 viral
proteins. Expression of PRDX4, alone or with PRDX1, increased the
resistance of yeast cells to oxidant-induced toxicity. Jin et al. (1997)
suggested PRDX4 modulates IKBA phosphorylation in the cytoplasm and thus
affects a peroxiredoxin-dependent redox step.
*FIELD* RF
1. Jin, D.-Y; Chae, H. Z; Rhee, S. G; Jeang, K.-T: Regulatory role
for a novel human thioredoxin peroxidase in NF-kappa-B activation. J.
Biol. Chem. 272: 30952-30961, 1997.
*FIELD* CD
Paul J. Converse: 11/27/2001
*FIELD* ED
alopez: 11/27/2001