PABP8_ARATH
ID PABP8_ARATH Reviewed; 671 AA.
AC Q9FXA2;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Polyadenylate-binding protein 8;
DE Short=PABP-8;
DE Short=Poly(A)-binding protein 8;
GN Name=PAB8; OrderedLocusNames=At1g49760; ORFNames=F14J22.3;
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 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 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 [5]
RP INDUCTION, INTERACTION WITH VIRAL VPG-PRO AND RDRP, AND DISRUPTION
RP 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 [6]
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).
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 (By similarity). During infection with
CC potyvirus TuMV, acts as a potential integral component of the viral
CC replicase complex that could play an important role in the regulation
CC of potyviral RNA-dependent RNA polymerase (RdRp) (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ERD15/CID1. Interacts with Turnip mosaic virus
CC (TuMV) VPg-Pro and RNA-dependent RNA polymerase (RdRp).
CC {ECO:0000269|PubMed:18753244, ECO:0000269|PubMed:22118612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in immature flowers.
CC -!- INDUCTION: By potyvirus TuMV infection. {ECO:0000269|PubMed:18753244}.
CC -!- DISRUPTION PHENOTYPE: Pab2 and pab8 double mutants show significant
CC growth and development defects and more resistance to Turnip mosaic
CC virus (TuMV). {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; AC011807; AAG13056.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32472.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32473.1; -; Genomic_DNA.
DR EMBL; AF370517; AAK43894.1; -; mRNA.
DR EMBL; AY064622; AAL47336.1; -; mRNA.
DR PIR; C96534; C96534.
DR RefSeq; NP_001185184.1; NM_001198255.1.
DR RefSeq; NP_564554.1; NM_103863.3.
DR AlphaFoldDB; Q9FXA2; -.
DR SMR; Q9FXA2; -.
DR BioGRID; 26624; 9.
DR IntAct; Q9FXA2; 7.
DR STRING; 3702.AT1G49760.1; -.
DR iPTMnet; Q9FXA2; -.
DR MetOSite; Q9FXA2; -.
DR PaxDb; Q9FXA2; -.
DR PRIDE; Q9FXA2; -.
DR ProMEX; Q9FXA2; -.
DR ProteomicsDB; 248651; -.
DR EnsemblPlants; AT1G49760.1; AT1G49760.1; AT1G49760.
DR EnsemblPlants; AT1G49760.2; AT1G49760.2; AT1G49760.
DR GeneID; 841399; -.
DR Gramene; AT1G49760.1; AT1G49760.1; AT1G49760.
DR Gramene; AT1G49760.2; AT1G49760.2; AT1G49760.
DR KEGG; ath:AT1G49760; -.
DR Araport; AT1G49760; -.
DR TAIR; locus:2012161; AT1G49760.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; Q9FXA2; -.
DR OMA; AHLTNEY; -.
DR OrthoDB; 1027234at2759; -.
DR PhylomeDB; Q9FXA2; -.
DR PRO; PR:Q9FXA2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXA2; baseline and differential.
DR Genevisible; Q9FXA2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
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 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; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Translation regulation.
FT CHAIN 1..671
FT /note="Polyadenylate-binding protein 8"
FT /id="PRO_0000422645"
FT DOMAIN 45..123
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 133..210
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 224..301
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 327..404
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 573..650
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 467..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 72779 MW; 49712E5333ED4E55 CRC64;
MAQIQHQGQN ANGGVAVPGA AAAEAAAAAA GAAAAAAGAA QQGTTSLYVG DLDATVTDSQ
LFEAFTQAGQ VVSVRVCRDM TTRRSLGYGY VNYATPQDAS RALNELNFMA LNGRAIRVMY
SVRDPSLRKS GVGNIFIKNL DKSIDHKALH ETFSAFGPIL SCKVAVDPSG QSKGYGFVQY
DTDEAAQGAI DKLNGMLLND KQVYVGPFVH KLQRDPSGEK VKFTNVYVKN LSESLSDEEL
NKVFGEFGVT TSCVIMRDGE GKSKGFGFVN FENSDDAARA VDALNGKTFD DKEWFVGKAQ
KKSERETELK QKFEQSLKEA ADKSQGSNLY VKNLDESVTD DKLREHFAPF GTITSCKVMR
DPSGVSRGSG FVAFSTPEEA TRAITEMNGK MIVTKPLYVA LAQRKEDRKA RLQAQFSQMR
PVNMPPAVGP RMQMYPPGGP PMGQQLFYGQ GPPAMIPQPG FGYQQQLVPG MRPGGSPMPN
FFMPMMQQGQ QQQQQQQQQQ RPGGGRRGAL PQPQQPSPMM QQQMHPRGRM YRYPQRDVNT
MPGPTQNMLS VPYDVSSGGG VHHRDSPTSQ PVPIVALATR LANAAPEQQR TMLGENLYPL
VEQLEPESAA KVTGMLLEMD QTEVLHLLES PEALKAKVTE AMDVLRSVAQ QQAGGAADQL
ASLSLGDNIV P
