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Polyadenylate-binding protein 2 (PABP-2) (Poly(A)-binding protein 2)

 PABP2_ARATH             Reviewed;         629 AA.
P42731; Q8RXR5;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-OCT-2017, entry version 130.
RecName: Full=Polyadenylate-binding protein 2;
Short=PABP-2;
Short=Poly(A)-binding protein 2;
Name=PAB2; OrderedLocusNames=At4g34110; ORFNames=F28A23.130;
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 [MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia; TISSUE=Shoot;
PubMed=8029336; DOI=10.1104/pp.103.2.525;
Hilson P., Carroll K.L., Masson P.H.;
"Molecular characterization of PAB2, a member of the multigene family
coding for poly(A)-binding proteins in Arabidopsis thaliana.";
Plant Physiol. 103:525-533(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
FUNCTION, AND INTERACTION WITH EIF-ISO4G.
PubMed=10849337; DOI=10.1046/j.1365-313x.2000.00721.x;
Palanivelu R., Belostotsky D.A., Meagher R.B.;
"Arabidopsis thaliana poly (A) binding protein 2 (PAB2) functions in
yeast translational and mRNA decay processes.";
Plant J. 22:187-198(2000).
[6]
TISSUE SPECIFICITY.
PubMed=10849338; DOI=10.1046/j.1365-313x.2000.00720.x;
Palanivelu R., Belostotsky D.A., Meagher R.B.;
"Conserved expression of Arabidopsis thaliana poly (A) binding protein
2 (PAB2) in distinct vegetative and reproductive tissues.";
Plant J. 22:199-210(2000).
[7]
GENE FAMILY.
PubMed=12586718;
Belostotsky D.A.;
"Unexpected complexity of poly(A)-binding protein gene families in
flowering plants: three conserved lineages that are at least 200
million years old and possible auto- and cross-regulation.";
Genetics 163:311-319(2003).
[8]
INTERACTION WITH VIRAL VPG-PRO.
PubMed=15039548; DOI=10.1099/vir.0.19706-0;
Leonard S., Viel C., Beauchemin C., Daigneault N., Fortin M.G.,
Laliberte J.F.;
"Interaction of VPg-Pro of turnip mosaic virus with the translation
initiation factor 4E and the poly(A)-binding protein in planta.";
J. Gen. Virol. 85:1055-1063(2004).
[9]
INTERACTION WITH CID1/ERD15 AND CID7, AND TISSUE SPECIFICITY.
PubMed=15650869; DOI=10.1007/s00438-004-1090-9;
Bravo J., Aguilar-Henonin L., Olmedo G., Guzman P.;
"Four distinct classes of proteins as interaction partners of the PABC
domain of Arabidopsis thaliana Poly(A)-binding proteins.";
Mol. Genet. Genomics 272:651-665(2005).
[10]
SUBCELLULAR LOCATION.
PubMed=17670821; DOI=10.1128/JVI.01243-07;
Beauchemin C., Laliberte J.F.;
"The poly(A) binding protein is internalized in virus-induced vesicles
or redistributed to the nucleolus during turnip mosaic virus
infection.";
J. Virol. 81:10905-10913(2007).
[11]
FUNCTION, INDUCTION, INTERACTION WITH VIRAL VPG-PRO AND RDRP, AND
DISRUPTION PHENOTYPE.
PubMed=18753244; DOI=10.1099/vir.0.2008/002139-0;
Dufresne P.J., Ubalijoro E., Fortin M.G., Laliberte J.F.;
"Arabidopsis thaliana class II poly(A)-binding proteins are required
for efficient multiplication of turnip mosaic virus.";
J. Gen. Virol. 89:2339-2348(2008).
[12]
INTERACTION WITH VIRAL RDRP, AND FUNCTION.
PubMed=18222516; DOI=10.1016/j.virol.2007.12.014;
Dufresne P.J., Thivierge K., Cotton S., Beauchemin C., Ide C.,
Ubalijoro E., Laliberte J.F., Fortin M.G.;
"Heat shock 70 protein interaction with Turnip mosaic virus RNA-
dependent RNA polymerase within virus-induced membrane vesicles.";
Virology 374:217-227(2008).
[13]
INTERACTION WITH ERD15/CID1.
PubMed=22118612; DOI=10.1016/j.plantsci.2011.08.009;
Aalto M.K., Helenius E., Kariola T., Pennanen V., Heino P., Horak H.,
Puzorjova I., Kollist H., Palva E.T.;
"ERD15--an attenuator of plant ABA responses and stomatal aperture.";
Plant Sci. 182:19-28(2012).
-!- FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an
important mediator of the multiple roles of the poly(A) tail in
mRNA biogenesis, stability and translation. In the cytoplasm,
affects both translation and mRNA decay. Stimulates translation by
interaction with translation initiation factor eIF4G, a subunit of
the cap-binding complex eIF4F, bringing the 5'- and 3'-ends of the
mRNA in proximity. The formation of this circular mRNP structure
appears to be critical for the synergistic effects of the cap and
the poly(A) tail in facilitating translation initiation, recycling
of ribosomes, and mRNA stability. During infection with potyvirus
TuMV, acts as a potential integral component of the viral
replicase complex that could play an important role in the
regulation of potyviral RNA-dependent RNA polymerase (RdRp).
{ECO:0000269|PubMed:10849337, ECO:0000269|PubMed:18222516,
ECO:0000269|PubMed:18753244}.
-!- SUBUNIT: Interacts with eIF-iso4G. Interacts with ERD15/CID1 and
CID7. Interacts with Turnip mosaic virus (TuMV) VPg-Pro and RNA-
dependent RNA polymerase (RdRp). {ECO:0000269|PubMed:10849337,
ECO:0000269|PubMed:15039548, ECO:0000269|PubMed:15650869,
ECO:0000269|PubMed:18222516, ECO:0000269|PubMed:18753244,
ECO:0000269|PubMed:22118612}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17670821}.
Nucleus {ECO:0000269|PubMed:17670821}. Note=In TuMV-infected
plants, partially retargeted in cytoplasmic virus-induced vesicles
and in the nucleolus.
-!- TISSUE SPECIFICITY: Expressed in all organs (at the protein level)
but under distinct spatial and temporal regulation within each
organ. {ECO:0000269|PubMed:10849338, ECO:0000269|PubMed:15650869,
ECO:0000269|PubMed:8029336}.
-!- INDUCTION: By potyvirus TuMV infection.
{ECO:0000269|PubMed:18753244}.
-!- DISRUPTION PHENOTYPE: Pab2 and pab4 double mutants, as well as
pab2 and pab8 double mutants show significant growth and
development defects and more resistance to Turnip mosaic virus
(TuMV). {ECO:0000269|PubMed:18753244}.
-!- MISCELLANEOUS: A.thaliana contains 8 PABP genes.
-!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L19418; AAA61780.1; -; mRNA.
EMBL; AL021961; CAA17561.1; -; Genomic_DNA.
EMBL; AL161584; CAB80128.1; -; Genomic_DNA.
EMBL; CP002687; AEE86325.1; -; Genomic_DNA.
EMBL; AY080718; AAL86321.1; -; mRNA.
EMBL; BT002354; AAN86187.1; -; mRNA.
PIR; T05425; T05425.
RefSeq; NP_195137.5; NM_119572.7.
UniGene; At.25252; -.
ProteinModelPortal; P42731; -.
SMR; P42731; -.
BioGrid; 14839; 10.
ELM; P42731; -.
IntAct; P42731; 8.
STRING; 3702.AT4G34110.1; -.
PaxDb; P42731; -.
PRIDE; P42731; -.
EnsemblPlants; AT4G34110.1; AT4G34110.1; AT4G34110.
GeneID; 829557; -.
Gramene; AT4G34110.1; AT4G34110.1; AT4G34110.
KEGG; ath:AT4G34110; -.
Araport; AT4G34110; -.
TAIR; locus:2124261; AT4G34110.
eggNOG; KOG0123; Eukaryota.
eggNOG; ENOG410XR5X; LUCA.
HOGENOM; HOG000217922; -.
InParanoid; P42731; -.
KO; K13126; -.
OMA; PIMSIRV; -.
OrthoDB; EOG093606N5; -.
PhylomeDB; P42731; -.
Reactome; R-ATH-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-ATH-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-ATH-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
PRO; PR:P42731; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; P42731; baseline and differential.
Genevisible; P42731; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003729; F:mRNA binding; IDA:TAIR.
GO; GO:0003743; F:translation initiation factor activity; ISS:TAIR.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
GO; GO:1900151; P:regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:UniProtKB.
GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:UniProtKB.
GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0006413; P:translational initiation; ISS:TAIR.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR002343; Hud_Sxl_RNA.
InterPro; IPR036053; PABP-dom.
InterPro; IPR006515; PABP_1234.
InterPro; IPR002004; PABP_HYD.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR003954; RRM_dom_euk.
Pfam; PF00658; PABP; 1.
Pfam; PF00076; RRM_1; 4.
PRINTS; PR00961; HUDSXLRNA.
SMART; SM00517; PolyA; 1.
SMART; SM00360; RRM; 4.
SMART; SM00361; RRM_1; 4.
SUPFAM; SSF54928; SSF54928; 3.
SUPFAM; SSF63570; SSF63570; 1.
TIGRFAMs; TIGR01628; PABP-1234; 1.
PROSITE; PS51309; PABC; 1.
PROSITE; PS50102; RRM; 4.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Host-virus interaction;
Nonsense-mediated mRNA decay; Nucleus; Reference proteome; Repeat;
RNA-binding; Translation regulation.
CHAIN 1 629 Polyadenylate-binding protein 2.
/FTId=PRO_0000081714.
DOMAIN 36 114 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 124 201 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 215 292 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 318 395 RRM 4. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 539 616 PABC. {ECO:0000255|PROSITE-
ProRule:PRU00641}.
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


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