CP29B_ARATH
ID CP29B_ARATH Reviewed; 289 AA.
AC Q9ZUU4; Q7GA50; Q8L941;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=RNA-binding protein CP29B, chloroplastic {ECO:0000305};
DE AltName: Full=Ribonucleoprotein At2g37220;
DE Flags: Precursor;
GN Name=CP29B {ECO:0000305}; OrderedLocusNames=At2g37220; ORFNames=F3G5.1;
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].
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, SUBCELLULAR LOCATION, AND
RP ADP-RIBOSYLATION.
RX PubMed=17450127; DOI=10.1038/nature05737;
RA Fu Z.Q., Guo M., Jeong B.R., Tian F., Elthon T.E., Cerny R.L., Staiger D.,
RA Alfano J.R.;
RT "A type III effector ADP-ribosylates RNA-binding proteins and quells plant
RT immunity.";
RL Nature 447:284-288(2007).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=18768909; DOI=10.1104/pp.108.124594;
RA Ghelis T., Bolbach G., Clodic G., Habricot Y., Miginiac E., Sotta B.,
RA Jeannette E.;
RT "Protein tyrosine kinases and protein tyrosine phosphatases are involved in
RT abscisic acid-dependent processes in Arabidopsis seeds and suspension
RT cells.";
RL Plant Physiol. 148:1668-1680(2008).
RN [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-63, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ASN-62, 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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-6 AND
RP SER-12.
RX PubMed=26452715; DOI=10.1016/j.febslet.2015.09.025;
RA Kim D., Ntui V.O., Zhang N., Xiong L.;
RT "Arabidopsis Yak1 protein (AtYak1) is a dual specificity protein kinase.";
RL FEBS Lett. 589:3321-3327(2015).
CC -!- FUNCTION: Could be involved in splicing and/or processing of
CC chloroplast RNA's. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:17450127}.
CC -!- PTM: ADP-ribosylated by the Pseudomonas syringae type III effector
CC HopU1. ADP-ribosylation reduces the ability of the protein to bind RNA.
CC {ECO:0000269|PubMed:17450127}.
CC -!- PTM: Phosphorylated on tyrosine residues after treatment with abscisic
CC acid (ABA). Phosphorylation may reduce the ability of the protein to
CC bind RNA. {ECO:0000269|PubMed:18768909}.
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DR EMBL; AC005896; AAC98043.1; -; Genomic_DNA.
DR EMBL; AC006260; AAM15222.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09369.1; -; Genomic_DNA.
DR EMBL; AF370167; AAK43982.1; -; mRNA.
DR EMBL; AY048251; AAK82513.1; -; mRNA.
DR EMBL; AY059129; AAL15235.1; -; mRNA.
DR EMBL; AY088648; AAM66970.1; -; mRNA.
DR PIR; A84790; A84790.
DR RefSeq; NP_181259.1; NM_129278.4.
DR AlphaFoldDB; Q9ZUU4; -.
DR SMR; Q9ZUU4; -.
DR BioGRID; 3643; 2.
DR IntAct; Q9ZUU4; 2.
DR MINT; Q9ZUU4; -.
DR STRING; 3702.AT2G37220.1; -.
DR iPTMnet; Q9ZUU4; -.
DR SWISS-2DPAGE; Q9ZUU4; -.
DR PaxDb; Q9ZUU4; -.
DR PRIDE; Q9ZUU4; -.
DR ProteomicsDB; 220549; -.
DR EnsemblPlants; AT2G37220.1; AT2G37220.1; AT2G37220.
DR GeneID; 818299; -.
DR Gramene; AT2G37220.1; AT2G37220.1; AT2G37220.
DR KEGG; ath:AT2G37220; -.
DR Araport; AT2G37220; -.
DR TAIR; locus:2049721; AT2G37220.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_15_1_1; -.
DR InParanoid; Q9ZUU4; -.
DR OMA; GVFKAYK; -.
DR OrthoDB; 1202220at2759; -.
DR PhylomeDB; Q9ZUU4; -.
DR PRO; PR:Q9ZUU4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUU4; baseline and differential.
DR Genevisible; Q9ZUU4; AT.
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:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:TAIR.
DR GO; GO:1901259; P:chloroplast rRNA processing; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IDA:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Chloroplast; mRNA processing; Phosphoprotein; Plastid;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 63..289
FT /note="RNA-binding protein CP29B, chloroplastic"
FT /id="PRO_0000031019"
FT DOMAIN 91..169
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 204..282
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 158..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..203
FT /note="Linker (Gly-rich)"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 63
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 60
FT /note="A -> V (in Ref. 4; AAM66970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 30718 MW; E500C3C0518369AD CRC64;
MAASASSLAL SSFNPKSLPF GVSRPASVSL LSPSLSFKLN SDSVSFSIAA KWNSPASRFA
RNVAITSEFE VEEDGFADVA PPKEQSFSAD LKLFVGNLPF NVDSAQLAQL FESAGNVEMV
EVIYDKITGR SRGFGFVTMS SVSEVEAAAQ QFNGYELDGR PLRVNAGPPP PKREDGFSRG
PRSSFGSSGS GYGGGGGSGA GSGNRVYVGN LSWGVDDMAL ESLFSEQGKV VEARVIYDRD
SGRSKGFGFV TYDSSQEVQN AIKSLDGADL DGRQIRVSEA EARPPRRQY
