RB47A_ARATH
ID RB47A_ARATH Reviewed; 445 AA.
AC F4I3B3; Q9FX88;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Polyadenylate-binding protein RBP47A;
DE Short=Poly(A)-binding protein RBP47A;
DE AltName: Full=RNA-binding protein 47A;
DE Short=AtRBP47A;
GN Name=RBP47A; OrderedLocusNames=At1g49600; ORFNames=F14J22.16;
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 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 [4]
RP INDUCTION BY OZONE, 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:0000250}.
CC -!- SUBUNIT: Interacts with the poly(A) tail of mRNA in nucleus.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasmic granule
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers, and seedlings.
CC {ECO:0000269|PubMed:11105760}.
CC -!- INDUCTION: Repressed by ozone-induced oxidative stress.
CC {ECO:0000269|PubMed:21120628}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding RBP47 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG13046.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC011807; AAG13046.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32448.1; -; Genomic_DNA.
DR PIR; F96532; F96532.
DR RefSeq; NP_175383.1; NM_103848.3.
DR AlphaFoldDB; F4I3B3; -.
DR SMR; F4I3B3; -.
DR BioGRID; 26609; 1.
DR IntAct; F4I3B3; 1.
DR STRING; 3702.AT1G49600.1; -.
DR iPTMnet; F4I3B3; -.
DR PaxDb; F4I3B3; -.
DR PRIDE; F4I3B3; -.
DR ProteomicsDB; 236210; -.
DR EnsemblPlants; AT1G49600.1; AT1G49600.1; AT1G49600.
DR GeneID; 841384; -.
DR Gramene; AT1G49600.1; AT1G49600.1; AT1G49600.
DR KEGG; ath:AT1G49600; -.
DR Araport; AT1G49600; -.
DR TAIR; locus:2012211; AT1G49600.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_016304_2_1_1; -.
DR InParanoid; F4I3B3; -.
DR OMA; GSEWCIF; -.
DR PRO; PR:F4I3B3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I3B3; baseline and differential.
DR Genevisible; F4I3B3; AT.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0034605; P:cellular response to heat; 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..445
FT /note="Polyadenylate-binding protein RBP47A"
FT /id="PRO_0000415766"
FT DOMAIN 119..199
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 213..292
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 327..399
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 48483 MW; 8C17FFB737675954 CRC64;
MQTPNNNGST DSVLPPTSAG TTPPPPLQQS TPPPQQQQQQ QWQQQQQWMA AMQQYPAAAM
AMMQQQQMMM YPHPQYAPYN QAAYQQHPQF QYAAYQQQQQ QHHQSQQQPR GGSGGDDVKT
LWVGDLLHWM DETYLHTCFS HTNEVSSVKV IRNKQTCQSE GYGFVEFLSR SAAEEALQSF
SGVTMPNAEQ PFRLNWASFS TGEKRASENG PDLSIFVGDL APDVSDAVLL ETFAGRYPSV
KGAKVVIDSN TGRSKGYGFV RFGDENERSR AMTEMNGAFC SSRQMRVGIA TPKRAAAYGQ
QNGSQALTLA GGHGGNGSMS DGESNNSTIF VGGLDADVTE EDLMQPFSDF GEVVSVKIPV
GKGCGFVQFA NRQSAEEAIG NLNGTVIGKN TVRLSWGRSP NKQWRSDSGN QWNGGYSRGQ
GYNNGYANQD SNMYATAAAA VPGAS
