REHY_HORVU
ID REHY_HORVU Reviewed; 218 AA.
AC P52572;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=1-Cys peroxiredoxin PER1;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P30041};
DE AltName: Full=B15C;
DE AltName: Full=Rehydrin homolog;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
GN Name=PER1;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=cv. Bomi; TISSUE=Aleurone;
RX PubMed=8180622; DOI=10.1111/j.1365-313x.1994.00385.x;
RA Aalen R.B., Opsahl-Ferstad H.G., Linnestad C., Olsen O.A.;
RT "Transcripts encoding an oleosin and a dormancy-related protein are present
RT in both the aleurone layer and the embryo of developing barley (Hordeum
RT vulgare L.) seeds.";
RL Plant J. 5:385-396(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Bomi;
RX PubMed=8914536; DOI=10.1007/bf00040837;
RA Stacy R.A.P., Munthe E., Steinum T., Sharma B., Aalen R.B.;
RT "A peroxiredoxin antioxidant is encoded by a dormancy-related gene, Per1,
RT expressed during late development in the aleurone and embryo of barley
RT grains.";
RL Plant Mol. Biol. 31:1205-1216(1996).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10417721; DOI=10.1046/j.1365-313x.1999.00488.x;
RA Stacy R.A.P., Nordeng T.W., Culianez-Macia F.A., Aalen R.B.;
RT "The dormancy-related peroxiredoxin anti-oxidant, PER1, is localized to the
RT nucleus of barley embryo and aleurone cells.";
RL Plant J. 19:1-8(1999).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively (By similarity). Seems to contribute to the inhibition of
CC germination during stress (By similarity).
CC {ECO:0000250|UniProtKB:O04005, ECO:0000250|UniProtKB:P30041}.
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:P30041};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10417721}. Cytoplasm
CC {ECO:0000250|UniProtKB:O04005}.
CC -!- TISSUE SPECIFICITY: Embryo and aleurone cells.
CC {ECO:0000269|PubMed:10417721}.
CC -!- DEVELOPMENTAL STAGE: Expressed during late development in the aleurone
CC and embryo. {ECO:0000269|PubMed:8180622}.
CC -!- INDUCTION: By abscisic acid (ABA). {ECO:0000269|PubMed:8180622}.
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 1-Cys
CC peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC with a cysteine from another protein or with a small thiol molecule.
CC {ECO:0000250|UniProtKB:O35244}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000305}.
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DR EMBL; X76605; CAA54066.1; -; mRNA.
DR EMBL; X96551; CAA65387.1; -; Genomic_DNA.
DR PIR; S60285; S60285.
DR AlphaFoldDB; P52572; -.
DR SMR; P52572; -.
DR Allergome; 9882; Hor v 32.
DR PeroxiBase; 4413; Hv1CysPrx.
DR EnsemblPlants; HORVU.MOREX.r2.2HG0099570.1; HORVU.MOREX.r2.2HG0099570.1; HORVU.MOREX.r2.2HG0099570.
DR EnsemblPlants; HORVU.MOREX.r2.2HG0099570.1.mrna1; HORVU.MOREX.r2.2HG0099570.1.mrna1; HORVU.MOREX.r2.2HG0099570.1.
DR Gramene; HORVU.MOREX.r2.2HG0099570.1; HORVU.MOREX.r2.2HG0099570.1; HORVU.MOREX.r2.2HG0099570.
DR Gramene; HORVU.MOREX.r2.2HG0099570.1.mrna1; HORVU.MOREX.r2.2HG0099570.1.mrna1; HORVU.MOREX.r2.2HG0099570.1.
DR ExpressionAtlas; P52572; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR CDD; cd03016; PRX_1cys; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR045020; PRX_1cys.
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 2: Evidence at transcript level;
KW Antioxidant; Cytoplasm; Nucleus; Oxidoreductase; Peroxidase;
KW Redox-active center.
FT CHAIN 1..218
FT /note="1-Cys peroxiredoxin PER1"
FT /id="PRO_0000135109"
FT DOMAIN 4..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 194..217
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 46
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P30041"
SQ SEQUENCE 218 AA; 23963 MW; 3895329545D6BC6A CRC64;
MPGLTIGDTV PNLELDSTHG KIRIHDYVGN GYVILFSHPG DFTPVCTTEL AAMANYAKEF
EKRGVKLLGI SCDDVQSHKE WTKDIEAYKP GSKVTYPIMA DPDRSAIKQL NMVDPDEKDA
QGQLPSRTLH IVGPDKVVKL SFLYPSCTGR NMDEVVRAVD SLLTAAKHKV ATPANWKPGE
CVVIAPGVSD EEAKKMFPQG FETADLPSKK GYLRFTKV
