REHY_ARATH
ID REHY_ARATH Reviewed; 216 AA.
AC O04005; Q42319; Q84WE3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=1-Cys peroxiredoxin PER1;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P30041};
DE AltName: Full=Rehydrin homolog;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
GN Name=PER1; OrderedLocusNames=At1g48130; ORFNames=F21D18.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9580097; DOI=10.1023/a:1005900832440;
RA Haslekas C., Stacy R.A.P., Nygaard V., Culianez-Macia F.A., Aalen R.B.;
RT "The expression of a peroxiredoxin antioxidant gene, AtPer1, in Arabidopsis
RT thaliana is seed-specific and related to dormancy.";
RL Plant Mol. Biol. 36:833-845(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-115.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RA Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14750521; DOI=10.1023/b:plan.0000006937.21343.2a;
RA Haslekas C., Grini P.E., Nordgard S.H., Thorstensen T., Viken M.K.,
RA Nygaard V., Aalen R.B.;
RT "ABI3 mediates expression of the peroxiredoxin antioxidant AtPER1 gene and
RT induction by oxidative stress.";
RL Plant Mol. Biol. 53:313-326(2003).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14526116; DOI=10.1104/pp.103.025916;
RA Haslekas C., Viken M.K., Grini P.E., Nygaard V., Nordgard S.H., Meza T.J.,
RA Aalen R.B.;
RT "Seed 1-cysteine peroxiredoxin antioxidants are not involved in dormancy,
RT but contribute to inhibition of germination during stress.";
RL Plant Physiol. 133:1148-1157(2003).
RN [9]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=15890615; DOI=10.1016/j.freeradbiomed.2004.07.037;
RA Rouhier N., Jacquot J.-P.;
RT "The plant multigenic family of thiol peroxidases.";
RL Free Radic. Biol. Med. 38:1413-1421(2005).
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 (PubMed:14526116).
CC {ECO:0000250|UniProtKB:P30041, ECO:0000269|PubMed:14526116}.
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:14526116}. Cytoplasm
CC {ECO:0000269|PubMed:14526116}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in seed. Expressed in
CC endosperm, embryo and aleurone cells. Also detected in young seedlings,
CC abscission zones, stem branching points. {ECO:0000269|PubMed:14750521,
CC ECO:0000269|PubMed:9580097}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the late globular stage and late
CC torpedo stage of the embryo, and in distinct cells of unfertilized and
CC fertilized ovules. {ECO:0000269|PubMed:14750521}.
CC -!- INDUCTION: By abscisic acid (ABA) and oxidative stress.
CC {ECO:0000269|PubMed:14750521}.
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; Y12089; CAA72804.1; -; Genomic_DNA.
DR EMBL; AC023673; AAF79536.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32252.1; -; Genomic_DNA.
DR EMBL; BT003916; AAO41963.1; -; mRNA.
DR EMBL; BT014873; AAT41856.1; -; mRNA.
DR EMBL; Z37278; CAA85539.1; -; mRNA.
DR RefSeq; NP_175247.1; NM_103709.4.
DR AlphaFoldDB; O04005; -.
DR SMR; O04005; -.
DR STRING; 3702.AT1G48130.1; -.
DR PeroxiBase; 4362; At1CysPrx.
DR PaxDb; O04005; -.
DR PRIDE; O04005; -.
DR ProteomicsDB; 234913; -.
DR EnsemblPlants; AT1G48130.1; AT1G48130.1; AT1G48130.
DR GeneID; 841231; -.
DR Gramene; AT1G48130.1; AT1G48130.1; AT1G48130.
DR KEGG; ath:AT1G48130; -.
DR Araport; AT1G48130; -.
DR TAIR; locus:2023772; AT1G48130.
DR eggNOG; KOG0854; Eukaryota.
DR HOGENOM; CLU_042529_4_1_1; -.
DR OMA; MIDYQDT; -.
DR OrthoDB; 1129256at2759; -.
DR PhylomeDB; O04005; -.
DR BioCyc; ARA:AT1G48130-MON; -.
DR PRO; PR:O04005; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04005; baseline and differential.
DR Genevisible; O04005; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; ISS:TAIR.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0010231; P:maintenance of seed dormancy; TAS:TAIR.
DR GO; GO:0009269; P:response to desiccation; TAS:TAIR.
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; Reference proteome; Stress response.
FT CHAIN 1..216
FT /note="1-Cys peroxiredoxin PER1"
FT /id="PRO_0000135107"
FT DOMAIN 4..159
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 191..214
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"
FT CONFLICT 23
FT /note="K -> T (in Ref. 6; CAA85539)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="S -> T (in Ref. 6; CAA85539)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="I -> N (in Ref. 6; CAA85539)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="H -> R (in Ref. 4; AAT41856 and 5; AAO41963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24081 MW; 60B8ADE9EC8632FB CRC64;
MPGITLGDTV PNLEVETTHD KFKLHDYFAN SWTVLFSHPG DFTPVCTTEL GAMAKYAHEF
DKRGVKLLGL SCDDVQSHKD WIKDIEAFNH GSKVNYPIIA DPNKEIIPQL NMIDPIENGP
SRALHIVGPD SKIKLSFLYP STTGRNMDEV LRALDSLLMA SKHNNKIATP VNWKPDQPVV
ISPAVSDEEA KKMFPQGFKT ADLPSKKGYL RHTEVS
