RP45C_ARATH
ID RP45C_ARATH Reviewed; 415 AA.
AC Q93W34; Q9SZ39;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Polyadenylate-binding protein RBP45C;
DE Short=Poly(A)-binding protein RBP45C;
DE AltName: Full=RNA-binding protein 45C;
DE Short=AtRBP45C;
GN Name=RBP45C; OrderedLocusNames=At4g27000; ORFNames=F10M23.340;
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=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 [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 TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11105760; DOI=10.1017/s1355838200001163;
RA Lorkovic Z.J., Wieczorek Kirk D.A., Klahre U., Hemmings-Mieszczak M.,
RA Filipowicz W.;
RT "RBP45 and RBP47, two oligouridylate-specific hnRNP-like proteins
RT interacting with poly(A)+ RNA in nuclei of plant cells.";
RL RNA 6:1610-1624(2000).
RN [5]
RP GENE FAMILY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=21120628; DOI=10.1007/s10059-011-0001-2;
RA Peal L., Jambunathan N., Mahalingam R.;
RT "Phylogenetic and expression analysis of RNA-binding proteins with triple
RT RNA recognition motifs in plants.";
RL Mol. Cells 31:55-64(2011).
CC -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP)-protein
CC binding the poly(A) tail of mRNA and probably involved in some steps of
CC pre-mRNA maturation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the poly(A) tail of mRNA in nucleus.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in seedlings and stems, and, to a
CC lower extent, in leaves and flowers. {ECO:0000269|PubMed:11105760}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding RBP45 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36546.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79555.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035440; CAB36546.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161566; CAB79555.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85282.1; -; Genomic_DNA.
DR EMBL; AF370339; AAK44154.1; -; mRNA.
DR EMBL; AY054487; AAK96678.1; -; mRNA.
DR EMBL; AY062999; AAL34173.1; -; mRNA.
DR EMBL; AY093292; AAM13291.1; -; mRNA.
DR PIR; T04823; T04823.
DR RefSeq; NP_567764.1; NM_118834.4.
DR AlphaFoldDB; Q93W34; -.
DR SMR; Q93W34; -.
DR BioGRID; 14095; 3.
DR IntAct; Q93W34; 3.
DR STRING; 3702.AT4G27000.1; -.
DR iPTMnet; Q93W34; -.
DR PaxDb; Q93W34; -.
DR PRIDE; Q93W34; -.
DR ProteomicsDB; 226812; -.
DR EnsemblPlants; AT4G27000.1; AT4G27000.1; AT4G27000.
DR GeneID; 828808; -.
DR Gramene; AT4G27000.1; AT4G27000.1; AT4G27000.
DR KEGG; ath:AT4G27000; -.
DR Araport; AT4G27000; -.
DR TAIR; locus:2116322; AT4G27000.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_016304_2_1_1; -.
DR InParanoid; Q93W34; -.
DR OMA; YPSCHSA; -.
DR OrthoDB; 775799at2759; -.
DR PRO; PR:Q93W34; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93W34; baseline and differential.
DR Genevisible; Q93W34; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 3.
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; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 2: Evidence at transcript level;
KW mRNA processing; Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..415
FT /note="Polyadenylate-binding protein RBP45C"
FT /id="PRO_0000415764"
FT DOMAIN 80..160
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 173..252
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 278..350
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 44972 MW; 5C375776B7BE7AF5 CRC64;
MMQQPPPASN GAATGPGQIP SDQQAYLQQQ QSWMMQHQQQ QQGQPPAGWN QQSAPSSGQP
QQQQYGGGGS QNPGSAGEIR SLWIGDLQPW MDENYLMNVF GLTGEATAAK VIRNKQNGYS
EGYGFIEFVN HATAERNLQT YNGAPMPSSE QAFRLNWAQL GAGERRQAEG PEHTVFVGDL
APDVTDHMLT ETFKAVYSSV KGAKVVNDRT TGRSKGYGFV RFADESEQIR AMTEMNGQYC
SSRPMRTGPA ANKKPLTMQP ASYQNTQGNS GESDPTNTTI FVGAVDQSVT EDDLKSVFGQ
FGELVHVKIP AGKRCGFVQY ANRACAEQAL SVLNGTQLGG QSIRLSWGRS PSNKQTQPDQ
AQYGGGGGYY GYPPQGYEAY GYAPPPQDPN AYYGGYAGGG YGNYQQPGGY QQQQQ
