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NDRP2_ARATH
ID   NDRP2_ARATH             Reviewed;         155 AA.
AC   Q9XI93; Q8LEH5;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 146.
DE   RecName: Full=Nodulin-related protein 2 {ECO:0000305};
GN   OrderedLocusNames=At1g13930 {ECO:0000312|EMBL:AEE29084.1};
GN   ORFNames=F16A14.14 {ECO:0000312|EMBL:AAF79399.1},
GN   F7A19.2 {ECO:0000312|EMBL:AAD39279.1};
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=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   [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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [6]
RP   IDENTIFICATION BY MASS 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).
RN   [7]
RP   INTERACTION WITH DEK3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=cv. Columbia;
RX   PubMed=25387881; DOI=10.1105/tpc.114.129254;
RA   Waidmann S., Kusenda B., Mayerhofer J., Mechtler K., Jonak C.;
RT   "A DEK domain-containing protein modulates chromatin structure and function
RT   in Arabidopsis.";
RL   Plant Cell 26:4328-4344(2014).
CC   -!- FUNCTION: May be a negative regulator of the ABA signaling/synthesis
CC       pathway. {ECO:0000250|UniProtKB:Q9ZQ80}.
CC   -!- SUBUNIT: Interacts with DEK3. {ECO:0000269|PubMed:25387881}.
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DR   EMBL; AC007576; AAD39279.1; -; Genomic_DNA.
DR   EMBL; AC068197; AAF79399.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29084.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29085.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29086.1; -; Genomic_DNA.
DR   EMBL; AY045640; AAK73998.1; -; mRNA.
DR   EMBL; AY058230; AAL15404.1; -; mRNA.
DR   EMBL; AY085412; AAM62639.1; -; mRNA.
DR   PIR; D86272; D86272.
DR   RefSeq; NP_001184989.1; NM_001198060.1.
DR   RefSeq; NP_001184990.1; NM_001198061.1.
DR   RefSeq; NP_563934.1; NM_101259.3.
DR   AlphaFoldDB; Q9XI93; -.
DR   SMR; Q9XI93; -.
DR   IntAct; Q9XI93; 1.
DR   STRING; 3702.AT1G13930.3; -.
DR   MetOSite; Q9XI93; -.
DR   PaxDb; Q9XI93; -.
DR   PRIDE; Q9XI93; -.
DR   ProMEX; Q9XI93; -.
DR   ProteomicsDB; 183657; -.
DR   EnsemblPlants; AT1G13930.1; AT1G13930.1; AT1G13930.
DR   EnsemblPlants; AT1G13930.2; AT1G13930.2; AT1G13930.
DR   EnsemblPlants; AT1G13930.3; AT1G13930.3; AT1G13930.
DR   GeneID; 837953; -.
DR   Gramene; AT1G13930.1; AT1G13930.1; AT1G13930.
DR   Gramene; AT1G13930.2; AT1G13930.2; AT1G13930.
DR   Gramene; AT1G13930.3; AT1G13930.3; AT1G13930.
DR   KEGG; ath:AT1G13930; -.
DR   Araport; AT1G13930; -.
DR   TAIR; locus:2035837; AT1G13930.
DR   eggNOG; ENOG502S1DM; Eukaryota.
DR   HOGENOM; CLU_122604_0_0_1; -.
DR   InParanoid; Q9XI93; -.
DR   OMA; MNFISDQ; -.
DR   OrthoDB; 1519389at2759; -.
DR   PhylomeDB; Q9XI93; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9XI93; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0010115; P:regulation of abscisic acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   InterPro; IPR040294; Nodulin-rel_1/2.
DR   PANTHER; PTHR35098; PTHR35098; 1.
PE   1: Evidence at protein level;
KW   Abscisic acid signaling pathway; Acetylation; Reference proteome.
FT   CHAIN           1..155
FT                   /note="Nodulin-related protein 2"
FT                   /id="PRO_0000453268"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZQ80"
FT   CONFLICT        78
FT                   /note="A -> S (in Ref. 4; AAM62639)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92
FT                   /note="Q -> H (in Ref. 4; AAM62639)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   155 AA;  16164 MW;  B0BFC431A2D8D755 CRC64;
     MNFISDQVKK LSSSTPEEPD HNKPVEGTET ATRPATNAEL MASAKVVAEA AQAAARNESD
     KLDKGKVAGA SADILDAAEK YGKFDEKSST GQYLDKAEKY LNDYESSHST GAGGPPPPTS
     QAEPASQPEP AAKKDDEESG GGLGGYAKMA QGFLK
 
 
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