CP31A_ARATH
ID CP31A_ARATH Reviewed; 329 AA.
AC Q04836; P92871; Q03394; Q43350; Q94EH5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 164.
DE RecName: Full=31 kDa ribonucleoprotein, chloroplastic;
DE AltName: Full=RNA-binding protein 1/2/3 {ECO:0000303|PubMed:7972518};
DE Short=AtRBP33;
DE AltName: Full=RNA-binding protein CP31A {ECO:0000303|PubMed:19297624};
DE AltName: Full=RNA-binding protein RNP-T {ECO:0000303|PubMed:1463823};
DE AltName: Full=RNA-binding protein cp31 {ECO:0000303|PubMed:7894017};
DE Flags: Precursor;
GN Name=CP31A {ECO:0000303|PubMed:19297624};
GN Synonyms=RBP31 {ECO:0000303|PubMed:12231822},
GN RNPT {ECO:0000303|PubMed:1463823}; OrderedLocusNames=At4g24770;
GN ORFNames=F22K18.30;
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 [MRNA].
RX PubMed=1463823; DOI=10.1007/bf00027154;
RA Bar-Zvi D., Shagan T., Schindler U., Cashmore A.R.;
RT "RNP-T, a ribonucleoprotein from Arabidopsis thaliana, contains two RNP-80
RT motifs and a novel acidic repeat arranged in an alpha-helix conformation.";
RL Plant Mol. Biol. 20:833-838(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
RX PubMed=12231822; DOI=10.1104/pp.102.1.313;
RA Delisle A.J.;
RT "RNA-binding protein from Arabidopsis.";
RL Plant Physiol. 102:313-314(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7972518; DOI=10.1104/pp.106.1.303;
RA Cheng S.H., Cline K., DeLisle A.J.;
RT "An Arabidopsis chloroplast RNA-binding protein gene encodes multiple mRNAs
RT with different 5' ends.";
RL Plant Physiol. 106:303-311(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=14703514; DOI=10.1074/jbc.m312011200;
RA Kwon C., Chung I.K.;
RT "Interaction of an Arabidopsis RNA-binding protein with plant single-
RT stranded telomeric DNA modulates telomerase activity.";
RL J. Biol. Chem. 279:12812-12818(2004).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-128, AND
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 [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19297624; DOI=10.1073/pnas.0808529106;
RA Tillich M., Hardel S.L., Kupsch C., Armbruster U., Delannoy E.,
RA Gualberto J.M., Lehwark P., Leister D., Small I.D., Schmitz-Linneweber C.;
RT "Chloroplast ribonucleoprotein CP31A is required for editing and stability
RT of specific chloroplast mRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6002-6007(2009).
RN [12]
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: Required for specific RNA editing events in chloroplasts and
CC stabilizes specific chloroplast mRNAs. Associates with the 3'-terminus
CC ndhF mRNAs and protects them against 3'-exonucleolytic degradation
CC (PubMed:19297624, PubMed:23110894). Required for normal chloroplast
CC development under cold stress conditions by stabilizing transcripts of
CC numerous mRNAs under these conditions (PubMed:23110894). May modulate
CC telomere replication through RNA binding domains (PubMed:14703514).
CC {ECO:0000269|PubMed:14703514, ECO:0000269|PubMed:19297624,
CC ECO:0000269|PubMed:23110894}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:17450127}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=1;
CC IsoId=Q04836-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q04836-2; Sequence=VSP_018879;
CC Name=3;
CC IsoId=Q04836-3; Sequence=VSP_018880;
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 -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit multiple specific editing defects
CC in chloroplast transcripts (PubMed:19297624, PubMed:23110894). Mutant
CC plants have increased sensitivity to cold stress (PubMed:23110894).
CC {ECO:0000269|PubMed:19297624, ECO:0000269|PubMed:23110894}.
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DR EMBL; X65255; CAA46347.1; -; mRNA.
DR EMBL; M94554; AAA32860.1; -; mRNA.
DR EMBL; U08467; AAA18378.1; -; Unassigned_RNA.
DR EMBL; U08467; AAA18379.1; -; Unassigned_RNA.
DR EMBL; U08467; AAA18380.1; -; Unassigned_RNA.
DR EMBL; D31712; BAA06520.1; -; Genomic_DNA.
DR EMBL; D31713; BAA06521.1; -; mRNA.
DR EMBL; AL035356; CAA22986.1; -; Genomic_DNA.
DR EMBL; AL161562; CAB79387.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84954.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66089.1; -; Genomic_DNA.
DR EMBL; AF410318; AAK95304.1; -; mRNA.
DR EMBL; AY143865; AAN28804.1; -; mRNA.
DR PIR; S28057; S28057.
DR PIR; S53492; S53492.
DR RefSeq; NP_001328008.1; NM_001341706.1. [Q04836-1]
DR RefSeq; NP_194208.1; NM_118610.4. [Q04836-1]
DR AlphaFoldDB; Q04836; -.
DR SMR; Q04836; -.
DR BioGRID; 13868; 2.
DR STRING; 3702.AT4G24770.1; -.
DR iPTMnet; Q04836; -.
DR PaxDb; Q04836; -.
DR PRIDE; Q04836; -.
DR ProteomicsDB; 220408; -. [Q04836-1]
DR EnsemblPlants; AT4G24770.1; AT4G24770.1; AT4G24770. [Q04836-1]
DR EnsemblPlants; AT4G24770.2; AT4G24770.2; AT4G24770. [Q04836-1]
DR GeneID; 828579; -.
DR Gramene; AT4G24770.1; AT4G24770.1; AT4G24770. [Q04836-1]
DR Gramene; AT4G24770.2; AT4G24770.2; AT4G24770. [Q04836-1]
DR KEGG; ath:AT4G24770; -.
DR Araport; AT4G24770; -.
DR TAIR; locus:2122009; AT4G24770.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_15_1_1; -.
DR InParanoid; Q04836; -.
DR OMA; KWENDDS; -.
DR PhylomeDB; Q04836; -.
DR PRO; PR:Q04836; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q04836; baseline and differential.
DR Genevisible; Q04836; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA: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:0003723; F:RNA binding; IDA:TAIR.
DR GO; GO:0016553; P:base conversion or substitution editing; IMP:TAIR.
DR GO; GO:1901259; P:chloroplast rRNA processing; IBA:GO_Central.
DR GO; GO:0009631; P:cold acclimation; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; IDA:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0009451; P:RNA modification; IMP:TAIR.
DR GO; GO:0006396; P:RNA processing; TAS:TAIR.
DR GO; GO:0043489; P:RNA stabilization; IMP: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 Alternative initiation; Chloroplast; mRNA processing; Phosphoprotein;
KW Plastid; Reference proteome; Repeat; Ribonucleoprotein; RNA editing;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..77
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 78..329
FT /note="31 kDa ribonucleoprotein, chloroplastic"
FT /id="PRO_0000031021"
FT REPEAT 108..112
FT /note="1"
FT REPEAT 113..117
FT /note="2"
FT REPEAT 118..122
FT /note="3"
FT REPEAT 123..127
FT /note="4"
FT REPEAT 128..132
FT /note="5"
FT REPEAT 133..137
FT /note="6"
FT DOMAIN 152..228
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 244..322
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 87..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..137
FT /note="6 X 5 AA approximate tandem repeats of S-E-G-D-X"
FT COMPBIAS 102..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 1..167
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018880"
FT VAR_SEQ 1..14
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018879"
FT CONFLICT 109..123
FT /note="Missing (in Ref. 4; BAA06520/BAA06521)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="R -> H (in Ref. 7; AAK95304/AAN28804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 35787 MW; 4FD02DA48600A593 CRC64;
MASSIVTSSL KPLAMADSSS STIFSHPSIS STISSSRIRS SSVSLLTGRI NLPLSFSRVS
LSLKTKTHLK KSPFVSFVAQ TSDWAEEGGE GSVAVEETEN SLESQDVSEG DESEGDASEG
DVSEGDESEG DVSEGAVSER AEFPEPSEEA KLFVGNLAYD VNSQALAMLF EQAGTVEIAE
VIYNRETDQS RGFGFVTMSS VDEAETAVEK FNRYDLNGRL LTVNKAAPRG SRPERAPRVY
EPAFRVYVGN LPWDVDNGRL EQLFSEHGKV VEARVVYDRE TGRSRGFGFV TMSDVDELNE
AISALDGQNL EGRAIRVNVA EERPPRRGY
