NRP_ARATH
ID NRP_ARATH Reviewed; 349 AA.
AC Q8RXN8; Q9FHX9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=DCD domain-containing protein NRP {ECO:0000305};
DE AltName: Full=Asparagine-rich protein {ECO:0000303|PubMed:21277785};
DE Short=N-rich protein {ECO:0000303|PubMed:21277785};
DE AltName: Full=GDA1-like protein {ECO:0000303|PubMed:16533544};
GN Name=NRP {ECO:0000303|PubMed:21277785};
GN Synonyms=GDL {ECO:0000303|PubMed:16533544};
GN OrderedLocusNames=At5g42050 {ECO:0000312|Araport:AT5G42050};
GN ORFNames=MJC20.15 {ECO:0000312|EMBL:BAB08438.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION.
RX PubMed=16533544; DOI=10.1016/j.jplph.2005.12.005;
RA Chotikacharoensuk T., Arteca R.N., Arteca J.M.;
RT "Use of differential display for the identification of touch-induced genes
RT from an ethylene-insensitive Arabidopsis mutant and partial
RT characterization of these genes.";
RL J. Plant Physiol. 163:1305-1320(2006).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21277785; DOI=10.1016/j.plaphy.2011.01.005;
RA Hoepflinger M.C., Pieslinger A.M., Tenhaken R.;
RT "Investigations on N-rich protein (NRP) of Arabidopsis thaliana under
RT different stress conditions.";
RL Plant Physiol. Biochem. 49:293-302(2011).
RN [7]
RP FUNCTION, INTERACTION WITH CRY2 AND VERTICILLIUM DAHLIAE PEVD1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28633330; DOI=10.1093/jxb/erx192;
RA Zhou R., Zhu T., Han L., Liu M., Xu M., Liu Y., Han D., Qiu D., Gong Q.,
RA Liu X.;
RT "The asparagine-rich protein NRP interacts with the Verticillium effector
RT PevD1 and regulates the subcellular localization of cryptochrome 2.";
RL J. Exp. Bot. 68:3427-3440(2017).
RN [8]
RP FUNCTION, INTERACTION WITH FYPP3, AND INDUCTION BY ABSCISIC ACID.
RX PubMed=29175650; DOI=10.1016/j.molp.2017.11.006;
RA Zhu T., Wu Y., Yang X., Chen W., Gong Q., Liu X.;
RT "The asparagine-rich protein NRP facilitates the degradation of the PP6-
RT type phosphatase FyPP3 to promote ABA response in Arabidopsis.";
RL Mol. Plant 11:257-268(2018).
CC -!- FUNCTION: Contributes to the initial phase of responses to abiotic and
CC biotic stress signals (Probable). Binds FYPP3 and facilitates FYPP3
CC degradation to promote abscisic acid (ABA) response (PubMed:29175650).
CC {ECO:0000269|PubMed:29175650, ECO:0000305|PubMed:28633330}.
CC -!- SUBUNIT: Interacts with CRY2 in the cytoplasm (PubMed:28633330).
CC Interacts with Verticillium dahliae PevD1 (PubMed:28633330). Interacts
CC with FYPP3 (PubMed:29175650). {ECO:0000269|PubMed:28633330,
CC ECO:0000269|PubMed:29175650}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21277785,
CC ECO:0000269|PubMed:28633330}.
CC -!- TISSUE SPECIFICITY: Highly expressed in sensecent leaves, cauline
CC leaves and sepals (PubMed:21277785). Expressed in the shoot apical
CC meristem, leaf veins, central cylinder, root hair zone, root tips,
CC rosette leaves, flowers and siliques (PubMed:21277785).
CC {ECO:0000269|PubMed:21277785}.
CC -!- INDUCTION: Induced by touch and salt stress (PubMed:16533544,
CC PubMed:21277785). Induced by wounding, calcium, magnesium and methyl
CC jasmonate (PubMed:16533544). Induced by osmotic stress, cycloheximide
CC and ozone (PubMed:21277785). Induced by abscisic acid (ABA)
CC (PubMed:29175650). {ECO:0000269|PubMed:16533544,
CC ECO:0000269|PubMed:21277785, ECO:0000269|PubMed:29175650}.
CC -!- DISRUPTION PHENOTYPE: Reduced length of primary root and increased
CC sensitivity to salt stress. {ECO:0000269|PubMed:21277785}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08438.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB017067; BAB08438.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED94759.1; -; Genomic_DNA.
DR EMBL; AY080773; AAL87257.1; -; mRNA.
DR EMBL; AY114057; AAM45105.1; -; mRNA.
DR EMBL; AY088465; AAM66001.1; -; mRNA.
DR RefSeq; NP_568600.1; NM_123570.4.
DR AlphaFoldDB; Q8RXN8; -.
DR SMR; Q8RXN8; -.
DR STRING; 3702.AT5G42050.1; -.
DR PaxDb; Q8RXN8; -.
DR PRIDE; Q8RXN8; -.
DR ProteomicsDB; 187106; -.
DR EnsemblPlants; AT5G42050.1; AT5G42050.1; AT5G42050.
DR GeneID; 834210; -.
DR Gramene; AT5G42050.1; AT5G42050.1; AT5G42050.
DR KEGG; ath:AT5G42050; -.
DR Araport; AT5G42050; -.
DR TAIR; locus:2165765; AT5G42050.
DR eggNOG; ENOG502QSUM; Eukaryota.
DR HOGENOM; CLU_051751_0_0_1; -.
DR InParanoid; Q8RXN8; -.
DR OMA; GWNSFKP; -.
DR OrthoDB; 1210304at2759; -.
DR PhylomeDB; Q8RXN8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RXN8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0010941; P:regulation of cell death; IGI:TAIR.
DR GO; GO:1904350; P:regulation of protein catabolic process in the vacuole; IGI:TAIR.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IGI:TAIR.
DR GO; GO:1902074; P:response to salt; IMP:UniProtKB.
DR InterPro; IPR013989; Dev_and_cell_death_domain.
DR InterPro; IPR044832; NRP-like.
DR PANTHER; PTHR46034; PTHR46034; 1.
DR Pfam; PF10539; Dev_Cell_Death; 1.
DR SMART; SM00767; DCD; 1.
DR PROSITE; PS51222; DCD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..349
FT /note="DCD domain-containing protein NRP"
FT /id="PRO_0000451105"
FT DOMAIN 214..346
FT /note="DCD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00569"
FT REGION 157..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 39784 MW; 0AB7E8A73159BEA4 CRC64;
MEYNNNNQQS FWQFSDQLRV QTPNLANLSL NDSIWSTNSV FKERRNLDIA ATTDKNNNQI
DYYQKKTTSD NINSNWNWKS SGSNNDMGLG FGPVGSKSTV DLNPIDKFNS PFNDTWKFNS
VNVNVNGYSP SSAVNGDFNK GVYTSMKKYG YNVNLKNNNK NKGIDEDHQI QKGGKKNRKN
QQNNNNQRNE DDKNNGLDKR FKTLPPAEAL PRNETIGGYI FVCNNDTMEE NLKRQLFGLP
PRYRDSVRAI TPGLPLFLYN YSTHQLHGIY EAASFGGTNI ELNAFEDKKC PGESRFPAQV
RAITRKVCLP LEEDSFRPIL HHYDGPKFRL ELSVPEVLSL LDIFADQNP
