PRDX1_MYOLU
ID PRDX1_MYOLU Reviewed; 199 AA.
AC Q6B4U9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Peroxiredoxin-1;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q06830};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 1 {ECO:0000305};
GN Name=PRDX1; Synonyms=PAG;
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY,
RP AND INDUCTION.
RC TISSUE=Heart;
RX PubMed=15680912; DOI=10.1016/j.abb.2004.11.020;
RA Eddy S.F., McNally J.D., Storey K.B.;
RT "Up-regulation of a thioredoxin peroxidase-like protein, proliferation-
RT associated gene, in hibernating bats.";
RL Arch. Biochem. Biophys. 435:103-111(2005).
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. 5 homodimers
CC assemble to form a ring-like decamer (By similarity). Interacts with
CC GDPD5; forms a mixed-disulfide with GDPD5 (By similarity). Interacts
CC with SESN1 and SESN2 (By similarity). Interacts with FAM107A (By
CC similarity). {ECO:0000250|UniProtKB:P0CB50,
CC ECO:0000250|UniProtKB:Q06830}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06830}.
CC -!- TISSUE SPECIFICITY: Detected in heart and skeletal muscle (at protein
CC level). {ECO:0000269|PubMed:15680912}.
CC -!- INDUCTION: Up-regulated in hearts from hiberbating bats.
CC {ECO:0000269|PubMed:15680912}.
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:0000250|UniProtKB:Q06830}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY680839; AAT79401.1; -; mRNA.
DR RefSeq; NP_001273946.1; NM_001287017.1.
DR RefSeq; XP_014319263.1; XM_014463777.1.
DR AlphaFoldDB; Q6B4U9; -.
DR SMR; Q6B4U9; -.
DR STRING; 59463.ENSMLUP00000005182; -.
DR PRIDE; Q6B4U9; -.
DR Ensembl; ENSMLUT00000005672; ENSMLUP00000005182; ENSMLUG00000005673.
DR GeneID; 102430863; -.
DR KEGG; mlf:102430863; -.
DR CTD; 5052; -.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000154277; -.
DR HOGENOM; CLU_042529_21_1_1; -.
DR InParanoid; Q6B4U9; -.
DR OMA; FWYPKDF; -.
DR OrthoDB; 1326484at2759; -.
DR TreeFam; TF105181; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:Ensembl.
DR GO; GO:0034101; P:erythrocyte homeostasis; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:Ensembl.
DR GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; 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; 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 Acetylation; Antioxidant; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Isopeptide bond; Oxidoreductase; Peroxidase;
KW Phosphoprotein; Redox-active center; Reference proteome; 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_0000256853"
FT DOMAIN 6..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 176..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 52
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
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:0000250|UniProtKB:Q06830"
FT DISULFID 173
FT /note="Interchain (with C-52); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
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"
SQ SEQUENCE 199 AA; 22124 MW; A75F3D21C40322CD CRC64;
MSSGNAKIGH PAPNFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS
DRAEEFKKIN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK
ADEGISFRGL FIIDDKGILR QITVNDLPVG RSVDETLRLV QAFQFTDKHG EVCPAGWKPG
SDTIKPDVQK SKEYFSKQK
