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Polyadenylate-binding protein RBP45B (Poly(A)-binding protein RBP45B) (RNA-binding protein 45B) (AtRBP45B)

 RB45B_ARATH             Reviewed;         405 AA.
Q9SAB3; C0Z2Q4; F4I8Z2; Q8LBV8;
22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-APR-2018, entry version 136.
RecName: Full=Polyadenylate-binding protein RBP45B;
Short=Poly(A)-binding protein RBP45B;
AltName: Full=RNA-binding protein 45B;
Short=AtRBP45B;
Name=RBP45B; OrderedLocusNames=At1g11650; ORFNames=F25C20.21;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
PubMed=11105760; DOI=10.1017/S1355838200001163;
Lorkovic Z.J., Wieczorek Kirk D.A., Klahre U., Hemmings-Mieszczak M.,
Filipowicz W.;
"RBP45 and RBP47, two oligouridylate-specific hnRNP-like proteins
interacting with poly(A)+ RNA in nuclei of plant cells.";
RNA 6:1610-1624(2000).
[7]
TISSUE SPECIFICITY.
PubMed=17159297; DOI=10.1266/ggs.81.355;
Park J.-I., Endo M., Kazama T., Saito H., Hakozaki H., Takada Y.,
Kawagishi-Kobayashi M., Watanabe M.;
"Molecular characterization of two anther-specific genes encoding
putative RNA-binding proteins, AtRBP45s, in Arabidopsis thaliana.";
Genes Genet. Syst. 81:355-359(2006).
[8]
INDUCTION BY PATHOGENS, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=cv. Columbia;
PubMed=19053141; DOI=10.1002/pmic.200800293;
Widjaja I., Naumann K., Roth U., Wolf N., Mackey D., Dangl J.L.,
Scheel D., Lee J.;
"Combining subproteome enrichment and Rubisco depletion enables
identification of low abundance proteins differentially regulated
during plant defense.";
Proteomics 9:138-147(2009).
[9]
FUNCTION, SUBUNIT, INDUCTION BY BIOTIC AND ABIOTIC STRESSES, TISSUE
SPECIFICITY, AND GENE FAMILY.
STRAIN=cv. Columbia, and cv. Wassilewskija;
PubMed=21120628; DOI=10.1007/s10059-011-0001-2;
Peal L., Jambunathan N., Mahalingam R.;
"Phylogenetic and expression analysis of RNA-binding proteins with
triple RNA recognition motifs in plants.";
Mol. Cells 31:55-64(2011).
-!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP)-protein
binding the poly(A) tail of mRNA and probably involved in some
steps of pre-mRNA maturation. {ECO:0000269|PubMed:21120628}.
-!- SUBUNIT: Both isoform 1 and isoform 2 interact with poly(A)+ RNA
in nucleus. {ECO:0000269|PubMed:21120628}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9SAB3-1; Sequence=Displayed;
Name=2; Synonyms=AtRBP45b-SV1, AtRBP45b-SV2;
IsoId=Q9SAB3-2; Sequence=VSP_042354;
Note=Derived from EST data. No experimental confirmation
available.;
Name=3;
IsoId=Q9SAB3-3; Sequence=VSP_042352, VSP_042353;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers,
siliques, and seedlings. Present in immature anther tissues
(tapetum cells) and mature pollen grains.
{ECO:0000269|PubMed:11105760, ECO:0000269|PubMed:17159297,
ECO:0000269|PubMed:21120628}.
-!- INDUCTION: By both biotic and abiotic stresses (e.g. ozone,
oxidative chemicals and pathogens such as virulent and avirulent
Pseudomonas syringae). {ECO:0000269|PubMed:19053141,
ECO:0000269|PubMed:21120628}.
-!- SIMILARITY: Belongs to the polyadenylate-binding RBP45 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM64532.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC007296; AAD30259.1; -; Genomic_DNA.
EMBL; CP002684; AEE28764.1; -; Genomic_DNA.
EMBL; CP002684; AEE28765.1; -; Genomic_DNA.
EMBL; AY093201; AAM13200.1; -; mRNA.
EMBL; BT008494; AAP37853.1; -; mRNA.
EMBL; AK318868; BAH56983.1; -; mRNA.
EMBL; AY086969; AAM64532.1; ALT_INIT; mRNA.
PIR; H86249; H86249.
RefSeq; NP_172630.1; NM_101037.4. [Q9SAB3-1]
RefSeq; NP_849641.1; NM_179310.2. [Q9SAB3-2]
UniGene; At.19842; -.
ProteinModelPortal; Q9SAB3; -.
SMR; Q9SAB3; -.
BioGrid; 22948; 12.
IntAct; Q9SAB3; 12.
STRING; 3702.AT1G11650.2; -.
iPTMnet; Q9SAB3; -.
PaxDb; Q9SAB3; -.
PRIDE; Q9SAB3; -.
ProMEX; Q9SAB3; -.
EnsemblPlants; AT1G11650.1; AT1G11650.1; AT1G11650. [Q9SAB3-2]
EnsemblPlants; AT1G11650.2; AT1G11650.2; AT1G11650. [Q9SAB3-1]
GeneID; 837708; -.
Gramene; AT1G11650.1; AT1G11650.1; AT1G11650. [Q9SAB3-2]
Gramene; AT1G11650.2; AT1G11650.2; AT1G11650. [Q9SAB3-1]
KEGG; ath:AT1G11650; -.
Araport; AT1G11650; -.
TAIR; locus:2027372; AT1G11650.
eggNOG; KOG0118; Eukaryota.
eggNOG; COG0724; LUCA.
HOGENOM; HOG000186228; -.
InParanoid; Q9SAB3; -.
OMA; CHSAKIM; -.
OrthoDB; EOG09360FRE; -.
PhylomeDB; Q9SAB3; -.
PRO; PR:Q9SAB3; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9SAB3; baseline and differential.
Genevisible; Q9SAB3; AT.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:TAIR.
GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:TAIR.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0010193; P:response to ozone; IEP:TAIR.
Gene3D; 3.30.70.330; -; 3.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 3.
SMART; SM00360; RRM; 3.
SUPFAM; SSF54928; SSF54928; 3.
PROSITE; PS50102; RRM; 3.
1: Evidence at protein level;
Alternative splicing; Complete proteome; mRNA processing; Nucleus;
Reference proteome; Repeat; RNA-binding; Stress response.
CHAIN 1 405 Polyadenylate-binding protein RBP45B.
/FTId=PRO_0000415763.
DOMAIN 62 143 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 155 234 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 261 333 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 5 55 Pro-rich.
COMPBIAS 382 400 Gln-rich.
VAR_SEQ 263 271 VFVGGLDAS -> ATTAATSRV (in isoform 3).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_042352.
VAR_SEQ 272 405 Missing (in isoform 3).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_042353.
VAR_SEQ 307 405 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_042354.
CONFLICT 190 190 D -> N (in Ref. 5; AAM64532).
{ECO:0000305}.
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


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