CP29A_ARATH
ID CP29A_ARATH Reviewed; 342 AA.
AC Q43349; Q94BT1; Q9LFH2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=29 kDa ribonucleoprotein, chloroplastic;
DE AltName: Full=RNA-binding protein CP29A {ECO:0000303|PubMed:23110894};
DE AltName: Full=RNA-binding protein cp29;
DE Flags: Precursor;
GN Name=CP29A {ECO:0000303|PubMed:23110894}; Synonyms=RBP29;
GN OrderedLocusNames=At3g53460; ORFNames=F4P12_160;
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 / MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7894017; DOI=10.1007/bf00019319;
RA Ohta M., Sugita M., Sugiura M.;
RT "Three types of nuclear genes encoding chloroplast RNA-binding proteins
RT (cp29, cp31 and cp33) are present in Arabidopsis thaliana: presence of cp31
RT in chloroplasts and its homologue in nuclei/cytoplasms.";
RL Plant Mol. Biol. 27:529-539(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 1).
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] (ISOFORM 1).
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23110894; DOI=10.1105/tpc.112.103002;
RA Kupsch C., Ruwe H., Gusewski S., Tillich M., Small I.,
RA Schmitz-Linneweber C.;
RT "Arabidopsis chloroplast RNA binding proteins CP31A and CP29A associate
RT with large transcript pools and confer cold stress tolerance by influencing
RT multiple chloroplast RNA processing steps.";
RL Plant Cell 24:4266-4280(2012).
CC -!- FUNCTION: Stabilizes specific chloroplast mRNAs. Required for normal
CC chloroplast development under cold stress conditions by stabilizing
CC transcripts of numerous mRNAs under these conditions.
CC {ECO:0000269|PubMed:23110894}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q43349-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q43349-2; Sequence=VSP_009110;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit increased sensitivity to cold
CC stress. {ECO:0000269|PubMed:23110894}.
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DR EMBL; D31710; BAA06518.1; -; Genomic_DNA.
DR EMBL; D31711; BAA06519.1; -; mRNA.
DR EMBL; AL132966; CAB67653.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79089.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79090.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79091.1; -; Genomic_DNA.
DR EMBL; AY039909; AAK64013.1; -; mRNA.
DR EMBL; AY077674; AAL76152.1; -; mRNA.
DR EMBL; AY087840; AAM65393.1; -; mRNA.
DR PIR; S53490; S53490.
DR PIR; T45886; T45886.
DR RefSeq; NP_001190078.1; NM_001203149.1. [Q43349-1]
DR RefSeq; NP_190914.1; NM_115206.3. [Q43349-1]
DR RefSeq; NP_850692.2; NM_180361.2. [Q43349-1]
DR AlphaFoldDB; Q43349; -.
DR SMR; Q43349; -.
DR BioGRID; 9831; 2.
DR IntAct; Q43349; 1.
DR STRING; 3702.AT3G53460.4; -.
DR iPTMnet; Q43349; -.
DR PRIDE; Q43349; -.
DR ProteomicsDB; 222762; -. [Q43349-1]
DR EnsemblPlants; AT3G53460.1; AT3G53460.1; AT3G53460. [Q43349-1]
DR EnsemblPlants; AT3G53460.2; AT3G53460.2; AT3G53460. [Q43349-1]
DR EnsemblPlants; AT3G53460.3; AT3G53460.3; AT3G53460. [Q43349-1]
DR GeneID; 824514; -.
DR Gramene; AT3G53460.1; AT3G53460.1; AT3G53460. [Q43349-1]
DR Gramene; AT3G53460.2; AT3G53460.2; AT3G53460. [Q43349-1]
DR Gramene; AT3G53460.3; AT3G53460.3; AT3G53460. [Q43349-1]
DR KEGG; ath:AT3G53460; -.
DR Araport; AT3G53460; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_15_1_1; -.
DR InParanoid; Q43349; -.
DR OMA; SNLAWGV; -.
DR PhylomeDB; Q43349; -.
DR PRO; PR:Q43349; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q43349; baseline and differential.
DR Genevisible; Q43349; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1901259; P:chloroplast rRNA processing; IBA:GO_Central.
DR GO; GO:0009631; P:cold acclimation; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043489; P:RNA stabilization; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; mRNA processing; Phosphoprotein;
KW Plastid; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 66..342
FT /note="29 kDa ribonucleoprotein, chloroplastic"
FT /id="PRO_0000031020"
FT DOMAIN 99..177
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 257..335
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 167..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..256
FT /note="Linker (Gly-rich)"
FT COMPBIAS 232..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8RWN5"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03250"
FT VAR_SEQ 220..227
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7894017"
FT /id="VSP_009110"
SQ SEQUENCE 342 AA; 36007 MW; CAC3410B72410988 CRC64;
MSASASSLSA FNPKSLPLCV SRPASVSVLP PSLSFKLHSD HLVSIFASSA LKCSSPAEYP
SRFVRNVAVS SDFEVEEDDM FADGDDSAPV ERNSFSPDLK LFVGNLSFNV DSAQLAQLFE
SAGNVEMVEV IYDKVTGRSR GFGFVTMSTA AEVEAAAQQF NGYEFEGRPL RVNAGPPPPK
REESFSRGPR SGGYGSERGG GYGSERGGGY GSERGGGYGS ERGGGYGSQR SGGGYGGSQR
SSYGSGSGSG SGSGSGNRLY VGNLSWGVDD MALENLFNEQ GKVVEARVIY DRDSGRSKGF
GFVTLSSSQE VQKAINSLNG ADLDGRQIRV SEAEARPPRG QF
