PRDX1_RAT
ID PRDX1_RAT Reviewed; 199 AA.
AC Q63716;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Peroxiredoxin-1;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q06830};
DE AltName: Full=HBP23;
DE AltName: Full=Heme-binding 23 kDa protein;
DE AltName: Full=Thioredoxin peroxidase 2;
DE AltName: Full=Thioredoxin-dependent peroxide reductase 2;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 1 {ECO:0000305};
GN Name=Prdx1; Synonyms=Tdpx2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7577926; DOI=10.1021/bi00041a017;
RA Iwahara S., Satoh H., Song D.-X., Webb J., Burlingame A.L., Nagae Y.,
RA Mueller-Eberhard U.;
RT "Purification, characterization, and cloning of a heme-binding protein (23
RT kDa) in rat liver cytosol.";
RL Biochemistry 34:13398-13406(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Pituitary;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 17-35 AND 111-190, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN OXIDIZED FORM, AND DISULFIDE
RP BONDS.
RX PubMed=10535922; DOI=10.1073/pnas.96.22.12333;
RA Hirotsu S., Abe Y., Okada K., Nagahara N., Hori H., Nishino T.,
RA Hakoshima T.;
RT "Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding
RT protein 23 kDa/proliferation-associated gene product.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12333-12338(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), DISULFIDE BONDS, AND CATALYTIC
RP ACTIVITY.
RX PubMed=17974571; DOI=10.1074/jbc.m705753200;
RA Matsumura T., Okamoto K., Iwahara S., Hori H., Takahashi Y., Nishino T.,
RA Abe Y.;
RT "Dimer-oligomer interconversion of wild-type and mutant rat 2-Cys
RT peroxiredoxin: disulfide formation at dimer-dimer interfaces is not
RT essential for decamerization.";
RL J. Biol. Chem. 283:284-293(2008).
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) (By similarity). Reduces an intramolecular
CC disulfide bond in GDPD5 that gates the ability to GDPD5 to drive
CC postmitotic motor neuron differentiation (By similarity).
CC {ECO:0000250|UniProtKB:P0CB50, ECO:0000250|UniProtKB:Q06830}.
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:Q06830};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (PubMed:10535922).
CC 5 homodimers assemble to form a ring-like decamer (PubMed:17974571).
CC Interacts with GDPD5; forms a mixed-disulfide with GDPD5 (By
CC similarity). Interacts with SESN1 and SESN2 (By similarity). Interacts
CC with FAM107A (By similarity). {ECO:0000250|UniProtKB:P0CB50,
CC ECO:0000250|UniProtKB:Q06830, ECO:0000269|PubMed:10535922,
CC ECO:0000269|PubMed:17974571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06830}.
CC -!- PTM: Phosphorylated on Thr-90 during the M-phase, which leads to a
CC decrease in enzymatic activity. {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:0000305|PubMed:10535922}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; D30035; BAA06275.1; -; mRNA.
DR EMBL; BC058450; AAH58450.1; -; mRNA.
DR EMBL; BC088118; AAH88118.1; -; mRNA.
DR PIR; I52425; I52425.
DR RefSeq; NP_476455.1; NM_057114.1.
DR PDB; 1QQ2; X-ray; 2.60 A; A/B=1-199.
DR PDB; 2Z9S; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=1-199.
DR PDBsum; 1QQ2; -.
DR PDBsum; 2Z9S; -.
DR AlphaFoldDB; Q63716; -.
DR SMR; Q63716; -.
DR BioGRID; 250701; 7.
DR IntAct; Q63716; 7.
DR MINT; Q63716; -.
DR STRING; 10116.ENSRNOP00000023132; -.
DR PeroxiBase; 4508; Rno2CysPrx01.
DR iPTMnet; Q63716; -.
DR PhosphoSitePlus; Q63716; -.
DR SwissPalm; Q63716; -.
DR World-2DPAGE; 0004:Q63716; -.
DR jPOST; Q63716; -.
DR PaxDb; Q63716; -.
DR PRIDE; Q63716; -.
DR Ensembl; ENSRNOT00000023132; ENSRNOP00000023132; ENSRNOG00000017194.
DR GeneID; 117254; -.
DR KEGG; rno:117254; -.
DR UCSC; RGD:620039; rat.
DR CTD; 5052; -.
DR RGD; 620039; Prdx1.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000154277; -.
DR HOGENOM; CLU_042529_21_1_1; -.
DR InParanoid; Q63716; -.
DR OMA; FWYPKDF; -.
DR OrthoDB; 1326484at2759; -.
DR PhylomeDB; Q63716; -.
DR TreeFam; TF105181; -.
DR BRENDA; 1.11.1.24; 5301.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR EvolutionaryTrace; Q63716; -.
DR PRO; PR:Q63716; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000017194; Expressed in duodenum and 19 other tissues.
DR Genevisible; Q63716; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0000791; C:euchromatin; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:RGD.
DR GO; GO:0020037; F:heme binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0004601; F:peroxidase activity; ISO:RGD.
DR GO; GO:0051920; F:peroxiredoxin activity; IDA:RGD.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034101; P:erythrocyte homeostasis; ISO:RGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:RGD.
DR GO; GO:0045321; P:leukocyte activation; IBA:GO_Central.
DR GO; GO:0030101; P:natural killer cell activation; ISO:RGD.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; ISO:RGD.
DR GO; GO:0019430; P:removal of superoxide radicals; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
DR GO; GO:0000302; P:response to reactive oxygen species; ISO:RGD.
DR DisProt; DP02793; -.
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 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; Acetylation; Antioxidant; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Isopeptide bond; Oxidoreductase;
KW Peroxidase; Phosphoprotein; Redox-active center; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT CHAIN 2..199
FT /note="Peroxiredoxin-1"
FT /id="PRO_0000135078"
FT DOMAIN 6..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 52
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 7
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 35
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 35
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35700"
FT MOD_RES 90
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MOD_RES 136
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35700"
FT DISULFID 52
FT /note="Interchain (with C-173); in linked form"
FT /evidence="ECO:0000269|PubMed:10535922,
FT ECO:0000269|PubMed:17974571, ECO:0007744|PDB:1QQ2"
FT DISULFID 173
FT /note="Interchain (with C-52); in linked form"
FT /evidence="ECO:0000269|PubMed:10535922,
FT ECO:0000269|PubMed:17974571, ECO:0007744|PDB:1QQ2"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:1QQ2"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1QQ2"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:1QQ2"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1QQ2"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1QQ2"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:1QQ2"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:1QQ2"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:1QQ2"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:1QQ2"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1QQ2"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1QQ2"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:1QQ2"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1QQ2"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:1QQ2"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:1QQ2"
FT HELIX 153..168
FT /evidence="ECO:0007829|PDB:1QQ2"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1QQ2"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:2Z9S"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:2Z9S"
SQ SEQUENCE 199 AA; 22109 MW; BDF2D4ABA8A776DA CRC64;
MSSGNAKIGH PAPSFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS
DRAEEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK
ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEILRLV QAFQFTDKHG EVCPAGWKPG
SDTIKPDVNK SKEYFSKQK
