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NDRP1_ARATH
ID   NDRP1_ARATH             Reviewed;         187 AA.
AC   Q9ZQ80; Q84VZ7;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Nodulin-related protein 1 {ECO:0000303|PubMed:20016941};
DE            Short=AtNRP1 {ECO:0000303|PubMed:20016941};
DE   AltName: Full=RPS2-interacting protein 11 {ECO:0000303|Ref.5};
GN   Name=NRP1 {ECO:0000303|PubMed:20016941};
GN   Synonyms=RPI-11 {ECO:0000303|Ref.5};
GN   OrderedLocusNames=At2g03440 {ECO:0000312|Araport:AT2G03440};
GN   ORFNames=T4M8.13 {ECO:0000312|EMBL:AAD17432.1};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RPS2.
RC   STRAIN=cv. Columbia;
RX   DOI=10.1016/j.pmpp.2005.02.006;
RA   Quirino B.F., Genger R., Ham J.H., Zabala G., Bent A.F.;
RT   "Identification and functional analysis of Arabidopsis proteins that
RT   interact with resistance gene product RPS2 in yeast.";
RL   Physiol. Mol. Plant Pathol. 65:257-267(2004).
RN   [6]
RP   INDUCTION BY PSEUDOMONAS SYRINGAE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17899171; DOI=10.1007/s00425-007-0628-6;
RA   Jung H.W., Lim C.W., Lee S.C., Choi H.W., Hwang C.H., Hwang B.K.;
RT   "Distinct roles of the pepper hypersensitive induced reaction protein gene
RT   CaHIR1 in disease and osmotic stress, as determined by comparative
RT   transcriptome and proteome analyses.";
RL   Planta 227:409-425(2008).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, INDUCTION BY COLD, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=20016941; DOI=10.1007/s10059-010-0005-3;
RA   Fu Q., Li S., Yu D.;
RT   "Identification of an Arabidopsis Nodulin-related protein in heat stress.";
RL   Mol. Cells 29:77-84(2010).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Prevents accumulation of abscisic acid (ABA) after heat
CC       treatment, thus reducing thermotolerance. May be a negative regulator
CC       of the ABA signaling/synthesis pathway (PubMed:20016941). Required for
CC       defense responses against avirulent bacteria such as P.syringae pv.
CC       tomato DC3000 (avrRpt2) (Ref.5). {ECO:0000269|PubMed:20016941,
CC       ECO:0000269|Ref.5}.
CC   -!- SUBUNIT: Interacts with RPS2. {ECO:0000269|Ref.5}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques.
CC       {ECO:0000269|PubMed:20016941}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates in meristematic tissues such as shoot
CC       apex and root tips, young leaf veins, stamens and stigmas of flowers,
CC       and abscission layers of young siliques. In young seedlings, present in
CC       root tips and junctions of roots and hypocotyls. Highest levels are
CC       reached in ten days old seedlings. In adult plants, confined to
CC       vasculature and hydathodes in leaves, and meristems. Also observed in
CC       floral developing organs. {ECO:0000269|PubMed:20016941}.
CC   -!- INDUCTION: Induced by P.syringae pv. tomato (PubMed:17899171).
CC       Repressed by heat stress (42 degrees Celsius) but induced by low
CC       temperature (4 degrees Celsius). Slightly repressed by NaCl
CC       (PubMed:20016941). {ECO:0000269|PubMed:17899171,
CC       ECO:0000269|PubMed:20016941}.
CC   -!- DISRUPTION PHENOTYPE: No obvious phenotype under heat stress
CC       (PubMed:20016941). Impaired resistance to avirulent bacteria P.syringae
CC       pv. tomato DC3000 (avrRpt2) (Ref.5). {ECO:0000269|PubMed:20016941,
CC       ECO:0000269|Ref.5}.
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DR   EMBL; AC006284; AAD17432.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05700.1; -; Genomic_DNA.
DR   EMBL; AY136477; AAM97142.1; -; mRNA.
DR   EMBL; BT004586; AAO42832.1; -; mRNA.
DR   EMBL; AK227483; BAE99484.1; -; mRNA.
DR   PIR; E84448; E84448.
DR   RefSeq; NP_178443.1; NM_126395.3.
DR   AlphaFoldDB; Q9ZQ80; -.
DR   SMR; Q9ZQ80; -.
DR   STRING; 3702.AT2G03440.1; -.
DR   iPTMnet; Q9ZQ80; -.
DR   PaxDb; Q9ZQ80; -.
DR   PRIDE; Q9ZQ80; -.
DR   ProMEX; Q9ZQ80; -.
DR   ProteomicsDB; 236818; -.
DR   EnsemblPlants; AT2G03440.1; AT2G03440.1; AT2G03440.
DR   GeneID; 814873; -.
DR   Gramene; AT2G03440.1; AT2G03440.1; AT2G03440.
DR   KEGG; ath:AT2G03440; -.
DR   Araport; AT2G03440; -.
DR   TAIR; locus:2063788; AT2G03440.
DR   eggNOG; ENOG502S1DM; Eukaryota.
DR   HOGENOM; CLU_122604_0_0_1; -.
DR   OMA; HAGPTTH; -.
DR   OrthoDB; 1519389at2759; -.
DR   PRO; PR:Q9ZQ80; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZQ80; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR   GO; GO:0010115; P:regulation of abscisic acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0009408; P:response to heat; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR   InterPro; IPR040294; Nodulin-rel_1/2.
DR   PANTHER; PTHR35098; PTHR35098; 1.
PE   1: Evidence at protein level;
KW   Abscisic acid signaling pathway; Acetylation; Plant defense;
KW   Reference proteome.
FT   CHAIN           1..187
FT                   /note="Nodulin-related protein 1"
FT                   /id="PRO_0000437190"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CONFLICT        75
FT                   /note="V -> I (in Ref. 3; AAO42832 and 4; BAE99484)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   187 AA;  19701 MW;  2AA0886BB5031B75 CRC64;
     MDFFTDQVKK KFSDKKPESS DPEPNHNKNK PGHTEPTTHK PGHGEPTTHK PVSNTDPTTH
     RPATNAELMA SAKIVAEAAQ AAARHESDKL DKAKVAGATA DILDAASRYG KLDEKSGVGQ
     YLEKAEQYLH KYETSHSHSS TGGTGSHGNV GGHGGGAGAP AAKKEDEKSG GGHGFGDYAK
     MAQGFMK
 
 
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