PABP2_ARATH
ID PABP2_ARATH Reviewed; 629 AA.
AC P42731; Q8RXR5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Polyadenylate-binding protein 2;
DE Short=PABP-2;
DE Short=Poly(A)-binding protein 2;
GN Name=PAB2; OrderedLocusNames=At4g34110; ORFNames=F28A23.130;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Shoot;
RX PubMed=8029336; DOI=10.1104/pp.103.2.525;
RA Hilson P., Carroll K.L., Masson P.H.;
RT "Molecular characterization of PAB2, a member of the multigene family
RT coding for poly(A)-binding proteins in Arabidopsis thaliana.";
RL Plant Physiol. 103:525-533(1993).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH EIF-ISO4G.
RX PubMed=10849337; DOI=10.1046/j.1365-313x.2000.00721.x;
RA Palanivelu R., Belostotsky D.A., Meagher R.B.;
RT "Arabidopsis thaliana poly (A) binding protein 2 (PAB2) functions in yeast
RT translational and mRNA decay processes.";
RL Plant J. 22:187-198(2000).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=10849338; DOI=10.1046/j.1365-313x.2000.00720.x;
RA Palanivelu R., Belostotsky D.A., Meagher R.B.;
RT "Conserved expression of Arabidopsis thaliana poly (A) binding protein 2
RT (PAB2) in distinct vegetative and reproductive tissues.";
RL Plant J. 22:199-210(2000).
RN [7]
RP GENE FAMILY.
RX PubMed=12586718; DOI=10.1093/genetics/163.1.311;
RA Belostotsky D.A.;
RT "Unexpected complexity of poly(A)-binding protein gene families in
RT flowering plants: three conserved lineages that are at least 200 million
RT years old and possible auto- and cross-regulation.";
RL Genetics 163:311-319(2003).
RN [8]
RP INTERACTION WITH VIRAL VPG-PRO.
RX PubMed=15039548; DOI=10.1099/vir.0.19706-0;
RA Leonard S., Viel C., Beauchemin C., Daigneault N., Fortin M.G.,
RA Laliberte J.F.;
RT "Interaction of VPg-Pro of turnip mosaic virus with the translation
RT initiation factor 4E and the poly(A)-binding protein in planta.";
RL J. Gen. Virol. 85:1055-1063(2004).
RN [9]
RP INTERACTION WITH CID1/ERD15 AND CID7, AND TISSUE SPECIFICITY.
RX PubMed=15650869; DOI=10.1007/s00438-004-1090-9;
RA Bravo J., Aguilar-Henonin L., Olmedo G., Guzman P.;
RT "Four distinct classes of proteins as interaction partners of the PABC
RT domain of Arabidopsis thaliana Poly(A)-binding proteins.";
RL Mol. Genet. Genomics 272:651-665(2005).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=17670821; DOI=10.1128/jvi.01243-07;
RA Beauchemin C., Laliberte J.F.;
RT "The poly(A) binding protein is internalized in virus-induced vesicles or
RT redistributed to the nucleolus during turnip mosaic virus infection.";
RL J. Virol. 81:10905-10913(2007).
RN [11]
RP FUNCTION, INDUCTION, INTERACTION WITH VIRAL VPG-PRO AND RDRP, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18753244; DOI=10.1099/vir.0.2008/002139-0;
RA Dufresne P.J., Ubalijoro E., Fortin M.G., Laliberte J.F.;
RT "Arabidopsis thaliana class II poly(A)-binding proteins are required for
RT efficient multiplication of turnip mosaic virus.";
RL J. Gen. Virol. 89:2339-2348(2008).
RN [12]
RP INTERACTION WITH VIRAL RDRP, AND FUNCTION.
RX PubMed=18222516; DOI=10.1016/j.virol.2007.12.014;
RA Dufresne P.J., Thivierge K., Cotton S., Beauchemin C., Ide C.,
RA Ubalijoro E., Laliberte J.F., Fortin M.G.;
RT "Heat shock 70 protein interaction with Turnip mosaic virus RNA-dependent
RT RNA polymerase within virus-induced membrane vesicles.";
RL Virology 374:217-227(2008).
RN [13]
RP INTERACTION WITH ERD15/CID1.
RX PubMed=22118612; DOI=10.1016/j.plantsci.2011.08.009;
RA Aalto M.K., Helenius E., Kariola T., Pennanen V., Heino P., Horak H.,
RA Puzorjova I., Kollist H., Palva E.T.;
RT "ERD15--an attenuator of plant ABA responses and stomatal aperture.";
RL Plant Sci. 182:19-28(2012).
RN [14]
RP FUNCTION.
RX PubMed=26972004; DOI=10.1016/j.celrep.2016.02.060;
RA Zuber H., Scheer H., Ferrier E., Sement F.M., Mercier P., Stupfler B.,
RA Gagliardi D.;
RT "Uridylation and PABP cooperate to repair mRNA deadenylated ends in
RT Arabidopsis.";
RL Cell Rep. 14:2707-2717(2016).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an important
CC mediator of the multiple roles of the poly(A) tail in mRNA biogenesis,
CC stability and translation. In the cytoplasm, affects both translation
CC and mRNA decay. Stimulates translation by interaction with translation
CC initiation factor eIF4G, a subunit of the cap-binding complex eIF4F,
CC bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of
CC this circular mRNP structure appears to be critical for the synergistic
CC effects of the cap and the poly(A) tail in facilitating translation
CC initiation, recycling of ribosomes, and mRNA stability. During
CC infection with potyvirus TuMV, acts as a potential integral component
CC of the viral replicase complex that could play an important role in the
CC regulation of potyviral RNA-dependent RNA polymerase (RdRp). Binds to
CC uridylated mRNAs and determines the size of uridine extensions
CC (PubMed:26972004). Limits uridine extension by URT1, likely by binding
CC to the oligo(A) tail and preventing URT1 access (PubMed:26972004).
CC {ECO:0000269|PubMed:10849337, ECO:0000269|PubMed:18222516,
CC ECO:0000269|PubMed:18753244, ECO:0000269|PubMed:26972004}.
CC -!- SUBUNIT: Interacts with eIF-iso4G. Interacts with ERD15/CID1 and CID7.
CC Interacts with Turnip mosaic virus (TuMV) VPg-Pro and RNA-dependent RNA
CC polymerase (RdRp). {ECO:0000269|PubMed:10849337,
CC ECO:0000269|PubMed:15039548, ECO:0000269|PubMed:15650869,
CC ECO:0000269|PubMed:18222516, ECO:0000269|PubMed:18753244,
CC ECO:0000269|PubMed:22118612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17670821}. Nucleus
CC {ECO:0000269|PubMed:17670821}. Note=In TuMV-infected plants, partially
CC retargeted in cytoplasmic virus-induced vesicles and in the nucleolus.
CC -!- TISSUE SPECIFICITY: Expressed in all organs (at the protein level) but
CC under distinct spatial and temporal regulation within each organ.
CC {ECO:0000269|PubMed:10849338, ECO:0000269|PubMed:15650869,
CC ECO:0000269|PubMed:8029336}.
CC -!- INDUCTION: By potyvirus TuMV infection. {ECO:0000269|PubMed:18753244}.
CC -!- DISRUPTION PHENOTYPE: Pab2 and pab4 double mutants, as well as pab2 and
CC pab8 double mutants show significant growth and development defects and
CC more resistance to Turnip mosaic virus (TuMV).
CC {ECO:0000269|PubMed:18753244}.
CC -!- MISCELLANEOUS: A.thaliana contains 8 PABP genes.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; L19418; AAA61780.1; -; mRNA.
DR EMBL; AL021961; CAA17561.1; -; Genomic_DNA.
DR EMBL; AL161584; CAB80128.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86325.1; -; Genomic_DNA.
DR EMBL; AY080718; AAL86321.1; -; mRNA.
DR EMBL; BT002354; AAN86187.1; -; mRNA.
DR PIR; T05425; T05425.
DR RefSeq; NP_195137.5; NM_119572.7.
DR AlphaFoldDB; P42731; -.
DR SMR; P42731; -.
DR BioGRID; 14839; 13.
DR ELM; P42731; -.
DR IntAct; P42731; 8.
DR STRING; 3702.AT4G34110.1; -.
DR MetOSite; P42731; -.
DR PaxDb; P42731; -.
DR PRIDE; P42731; -.
DR ProteomicsDB; 248740; -.
DR EnsemblPlants; AT4G34110.1; AT4G34110.1; AT4G34110.
DR GeneID; 829557; -.
DR Gramene; AT4G34110.1; AT4G34110.1; AT4G34110.
DR KEGG; ath:AT4G34110; -.
DR Araport; AT4G34110; -.
DR TAIR; locus:2124261; AT4G34110.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; P42731; -.
DR OMA; GYVNFAN; -.
DR OrthoDB; 1027234at2759; -.
DR PhylomeDB; P42731; -.
DR PRO; PR:P42731; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P42731; baseline and differential.
DR Genevisible; P42731; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:TAIR.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:1900151; P:regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:UniProtKB.
DR GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS:TAIR.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR002343; Hud_Sxl_RNA.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR PRINTS; PR00961; HUDSXLRNA.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 4.
DR SUPFAM; SSF54928; SSF54928; 3.
DR SUPFAM; SSF63570; SSF63570; 1.
DR TIGRFAMs; TIGR01628; PABP-1234; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Cytoplasm; Host-virus interaction; Nonsense-mediated mRNA decay; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Translation regulation.
FT CHAIN 1..629
FT /note="Polyadenylate-binding protein 2"
FT /id="PRO_0000081714"
FT DOMAIN 36..114
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 124..201
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 215..292
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 318..395
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 539..616
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 68672 MW; 0F809818D08BDC7E CRC64;
MAQVQLQGQT PNGSTAAVTS APATSGGATA TQFGNTSLYV GDLDFNVTDS QLFDAFGQMG
TVVTVRVCRD LVTRRSLGYG YVNFTNPQDA ARAIQELNYI PLYGKPIRVM YSHRDPSVRR
SGAGNIFIKN LDESIDHKAL HDTFSSFGNI VSCKVAVDSS GQSKGYGFVQ YANEESAQKA
IEKLNGMLLN DKQVYVGPFL RRQERDSTAN KTKFTNVYVK NLAESTTDDD LKNAFGEYGK
ITSAVVMKDG EGKSKGFGFV NFENADDAAR AVESLNGHKF DDKEWYVGRA QKKSERETEL
RVRYEQNLKE AADKFQSSNL YVKNLDPSIS DEKLKEIFSP FGTVTSSKVM RDPNGTSKGS
GFVAFATPEE ATEAMSQLSG KMIESKPLYV AIAQRKEDRR VRLQAQFSQV RPVAMQPSVG
PRMPVYPPGG PGIGQQMFYG QAPPAMIPPQ PGYGYQQQLV PGMRPGGGPV PSFFMPMVQP
QQQRPGGGRR PGGIQHSQQQ NPMMQQQMHP RGRMFRYPQG RGGSGDVPPY DMGNNMPLTI
GALASNLSNA TPEQQRTMLG EVLYPLVEQV EAESAAKVTG MLLEMDQTEV LHLLESPEAL
KAKVAEAMDV LRSVAAGGAT EQLASLNLS
