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RB45A_ARATH
ID   RB45A_ARATH             Reviewed;         387 AA.
AC   Q9FPJ8; Q9FFU0;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Polyadenylate-binding protein RBP45A;
DE            Short=Poly(A)-binding protein RBP45A;
DE   AltName: Full=RNA-binding protein 45A;
DE            Short=AtRBP45A;
GN   Name=RBP45A; OrderedLocusNames=At5g54900; ORFNames=MBG8.17;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
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   [7]
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}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in seedlings, and, to a lower
CC       extent, in leaves, stems, and flowers. Present in immature anther
CC       tissues (tapetum cells) and mature pollen grains.
CC       {ECO:0000269|PubMed:11105760, ECO:0000269|PubMed:17159297}.
CC   -!- INDUCTION: By ozone-induced oxidative stress.
CC       {ECO:0000269|PubMed:21120628}.
CC   -!- SIMILARITY: Belongs to the polyadenylate-binding RBP45 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB08769.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB005232; BAB08769.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED96554.1; -; Genomic_DNA.
DR   EMBL; AF324983; AAG40335.1; -; mRNA.
DR   EMBL; BT029545; ABL66801.1; -; mRNA.
DR   RefSeq; NP_568815.1; NM_124872.3.
DR   AlphaFoldDB; Q9FPJ8; -.
DR   SMR; Q9FPJ8; -.
DR   BioGRID; 20825; 4.
DR   IntAct; Q9FPJ8; 3.
DR   STRING; 3702.AT5G54900.1; -.
DR   iPTMnet; Q9FPJ8; -.
DR   MetOSite; Q9FPJ8; -.
DR   PaxDb; Q9FPJ8; -.
DR   PRIDE; Q9FPJ8; -.
DR   ProteomicsDB; 236219; -.
DR   EnsemblPlants; AT5G54900.1; AT5G54900.1; AT5G54900.
DR   GeneID; 835581; -.
DR   Gramene; AT5G54900.1; AT5G54900.1; AT5G54900.
DR   KEGG; ath:AT5G54900; -.
DR   Araport; AT5G54900; -.
DR   TAIR; locus:2160210; AT5G54900.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_016304_2_1_1; -.
DR   InParanoid; Q9FPJ8; -.
DR   OMA; MDENYIM; -.
DR   OrthoDB; 775799at2759; -.
DR   PhylomeDB; Q9FPJ8; -.
DR   PRO; PR:Q9FPJ8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FPJ8; baseline and differential.
DR   Genevisible; Q9FPJ8; AT.
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: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..387
FT                   /note="Polyadenylate-binding protein RBP45A"
FT                   /id="PRO_0000415762"
FT   DOMAIN          60..140
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          154..233
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          260..332
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          329..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  42324 MW;  D6CF4F66DFD78DB0 CRC64;
     MQQPPSNAAG AGQIPSGQQH LWMMMQQQQQ QQQMQLSAAP LGQHQYGIGS QNPGSASDVK
     SLWIGDLQQW MDENYIMSVF AQSGEATSAK VIRNKLTGQS EGYGFIEFVS HSVAERVLQT
     YNGAPMPSTE QTFRLNWAQA GAGEKRFQTE GPDHTIFVGD LAPEVTDYML SDTFKNVYGS
     VKGAKVVLDR TTGRSKGYGF VRFADENEQM RAMTEMNGQY CSTRPMRIGP AANKNALPMQ
     PAMYQNTQGA NAGDNDPNNT TIFVGGLDAN VTDDELKSIF GQFGELLHVK IPPGKRCGFV
     QYANKASAEH ALSVLNGTQL GGQSIRLSWG RSPNKQSDQA QWNGGGYYGY PPQPQGGYGY
     AAQPPTQDPN AYYGGYTGYG NYQQQRQ
 
 
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