RB45B_ARATH
ID RB45B_ARATH Reviewed; 405 AA.
AC Q9SAB3; C0Z2Q4; F4I8Z2; Q8LBV8;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Polyadenylate-binding protein RBP45B;
DE Short=Poly(A)-binding protein RBP45B;
DE AltName: Full=RNA-binding protein 45B;
DE Short=AtRBP45B;
GN Name=RBP45B; OrderedLocusNames=At1g11650; ORFNames=F25C20.21;
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] (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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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 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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=17159297; DOI=10.1266/ggs.81.355;
RA Park J.-I., Endo M., Kazama T., Saito H., Hakozaki H., Takada Y.,
RA Kawagishi-Kobayashi M., Watanabe M.;
RT "Molecular characterization of two anther-specific genes encoding putative
RT RNA-binding proteins, AtRBP45s, in Arabidopsis thaliana.";
RL Genes Genet. Syst. 81:355-359(2006).
RN [8]
RP INDUCTION BY PATHOGENS, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=19053141; DOI=10.1002/pmic.200800293;
RA Widjaja I., Naumann K., Roth U., Wolf N., Mackey D., Dangl J.L., Scheel D.,
RA Lee J.;
RT "Combining subproteome enrichment and Rubisco depletion enables
RT identification of low abundance proteins differentially regulated during
RT plant defense.";
RL Proteomics 9:138-147(2009).
RN [9]
RP FUNCTION, SUBUNIT, INDUCTION BY BIOTIC AND ABIOTIC STRESSES, TISSUE
RP SPECIFICITY, AND 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:0000269|PubMed:21120628}.
CC -!- SUBUNIT: Both isoform 1 and isoform 2 interact with poly(A)+ RNA in
CC nucleus. {ECO:0000269|PubMed:21120628}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9SAB3-1; Sequence=Displayed;
CC Name=2; Synonyms=AtRBP45b-SV1, AtRBP45b-SV2;
CC IsoId=Q9SAB3-2; Sequence=VSP_042354;
CC Name=3;
CC IsoId=Q9SAB3-3; Sequence=VSP_042352, VSP_042353;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers,
CC siliques, and seedlings. Present in immature anther tissues (tapetum
CC cells) and mature pollen grains. {ECO:0000269|PubMed:11105760,
CC ECO:0000269|PubMed:17159297, ECO:0000269|PubMed:21120628}.
CC -!- INDUCTION: By both biotic and abiotic stresses (e.g. ozone, oxidative
CC chemicals and pathogens such as virulent and avirulent Pseudomonas
CC syringae). {ECO:0000269|PubMed:19053141, ECO:0000269|PubMed:21120628}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding RBP45 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM64532.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007296; AAD30259.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28764.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28765.1; -; Genomic_DNA.
DR EMBL; AY093201; AAM13200.1; -; mRNA.
DR EMBL; BT008494; AAP37853.1; -; mRNA.
DR EMBL; AK318868; BAH56983.1; -; mRNA.
DR EMBL; AY086969; AAM64532.1; ALT_INIT; mRNA.
DR PIR; H86249; H86249.
DR RefSeq; NP_172630.1; NM_101037.4. [Q9SAB3-1]
DR RefSeq; NP_849641.1; NM_179310.2. [Q9SAB3-2]
DR AlphaFoldDB; Q9SAB3; -.
DR SMR; Q9SAB3; -.
DR BioGRID; 22948; 12.
DR IntAct; Q9SAB3; 12.
DR STRING; 3702.AT1G11650.2; -.
DR iPTMnet; Q9SAB3; -.
DR PaxDb; Q9SAB3; -.
DR PRIDE; Q9SAB3; -.
DR ProMEX; Q9SAB3; -.
DR ProteomicsDB; 236504; -. [Q9SAB3-1]
DR EnsemblPlants; AT1G11650.1; AT1G11650.1; AT1G11650. [Q9SAB3-2]
DR EnsemblPlants; AT1G11650.2; AT1G11650.2; AT1G11650. [Q9SAB3-1]
DR GeneID; 837708; -.
DR Gramene; AT1G11650.1; AT1G11650.1; AT1G11650. [Q9SAB3-2]
DR Gramene; AT1G11650.2; AT1G11650.2; AT1G11650. [Q9SAB3-1]
DR KEGG; ath:AT1G11650; -.
DR Araport; AT1G11650; -.
DR TAIR; locus:2027372; AT1G11650.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_016304_2_1_1; -.
DR InParanoid; Q9SAB3; -.
DR OMA; WMEETYL; -.
DR PhylomeDB; Q9SAB3; -.
DR PRO; PR:Q9SAB3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAB3; baseline and differential.
DR Genevisible; Q9SAB3; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; 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:0003723; F:RNA binding; IDA:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0010193; P:response to ozone; IEP:TAIR.
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; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Stress response.
FT CHAIN 1..405
FT /note="Polyadenylate-binding protein RBP45B"
FT /id="PRO_0000415763"
FT DOMAIN 62..143
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 155..234
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 261..333
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 263..271
FT /note="VFVGGLDAS -> ATTAATSRV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_042352"
FT VAR_SEQ 272..405
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_042353"
FT VAR_SEQ 307..405
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042354"
FT CONFLICT 190
FT /note="D -> N (in Ref. 5; AAM64532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 44115 MW; A13CB769F7B601E0 CRC64;
MMQQPPPGGI LPHHAPPPSA QQQYGYQQPY GIAGAAPPPP QMWNPQAAAP PSVQPTTADE
IRTLWIGDLQ YWMDENFLYG CFAHTGEMVS AKVIRNKQTG QVEGYGFIEF ASHAAAERVL
QTFNNAPIPS FPDQLFRLNW ASLSSGDKRD DSPDYTIFVG DLAADVTDYI LLETFRASYP
SVKGAKVVID RVTGRTKGYG FVRFSDESEQ IRAMTEMNGV PCSTRPMRIG PAASKKGVTG
QRDSYQSSAA GVTTDNDPNN TTVFVGGLDA SVTDDHLKNV FSQYGEIVHV KIPAGKRCGF
VQFSEKSCAE EALRMLNGVQ LGGTTVRLSW GRSPSNKQSG DPSQFYYGGY GQGQEQYGYT
MPQDPNAYYG GYSGGGYSGG YQQTPQAGQQ PPQQPPQQQQ VGFSY
