PABP4_ARATH
ID PABP4_ARATH Reviewed; 662 AA.
AC O22173; Q9C5J0;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Polyadenylate-binding protein 4;
DE Short=PABP-4;
DE Short=Poly(A)-binding protein 4;
GN Name=PAB4; OrderedLocusNames=At2g23350; ORFNames=T20D16.2;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [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. {ECO:0000269|PubMed:18753244,
CC ECO:0000269|PubMed:22118612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- INDUCTION: By potyvirus TuMV infection. {ECO:0000269|PubMed:18753244}.
CC -!- DISRUPTION PHENOTYPE: Pab2 and pab4 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; AC002391; AAB87097.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07446.1; -; Genomic_DNA.
DR EMBL; AF360217; AAK25927.1; -; mRNA.
DR EMBL; AY050859; AAK92796.1; -; mRNA.
DR EMBL; AY079389; AAL85120.1; -; mRNA.
DR PIR; T00497; T00497.
DR RefSeq; NP_179916.1; NM_127899.4.
DR AlphaFoldDB; O22173; -.
DR SMR; O22173; -.
DR BioGRID; 2219; 5.
DR IntAct; O22173; 4.
DR STRING; 3702.AT2G23350.1; -.
DR iPTMnet; O22173; -.
DR MetOSite; O22173; -.
DR PaxDb; O22173; -.
DR PRIDE; O22173; -.
DR ProMEX; O22173; -.
DR ProteomicsDB; 248630; -.
DR EnsemblPlants; AT2G23350.1; AT2G23350.1; AT2G23350.
DR GeneID; 816867; -.
DR Gramene; AT2G23350.1; AT2G23350.1; AT2G23350.
DR KEGG; ath:AT2G23350; -.
DR Araport; AT2G23350; -.
DR TAIR; locus:2058573; AT2G23350.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; O22173; -.
DR OMA; MIRITYS; -.
DR OrthoDB; 1027234at2759; -.
DR PhylomeDB; O22173; -.
DR PRO; PR:O22173; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22173; baseline and differential.
DR Genevisible; O22173; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
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..662
FT /note="Polyadenylate-binding protein 4"
FT /id="PRO_0000422643"
FT DOMAIN 46..124
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 134..211
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 225..302
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 328..405
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 558..635
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 642
FT /note="E -> D (in Ref. 3; AAK25927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 71653 MW; 448481E183DF339E CRC64;
MAQVQAPSSH SPPPPAVVND GAATASATPG IGVGGGGDGV THGALCSLYV GDLDFNVTDS
QLYDYFTEVC QVVSVRVCRD AATNTSLGYG YVNYSNTDDA EKAMQKLNYS YLNGKMIRIT
YSSRDSSARR SGVGNLFVKN LDKSVDNKTL HEAFSGCGTI VSCKVATDHM GQSRGYGFVQ
FDTEDSAKNA IEKLNGKVLN DKQIFVGPFL RKEERESAAD KMKFTNVYVK NLSEATTDDE
LKTTFGQYGS ISSAVVMRDG DGKSRCFGFV NFENPEDAAR AVEALNGKKF DDKEWYVGKA
QKKSERELEL SRRYEQGSSD GGNKFDGLNL YVKNLDDTVT DEKLRELFAE FGTITSCKVM
RDPSGTSKGS GFVAFSAASE ASRVLNEMNG KMVGGKPLYV ALAQRKEERR AKLQAQFSQM
RPAFIPGVGP RMPIFTGGAP GLGQQIFYGQ GPPPIIPHQP GFGYQPQLVP GMRPAFFGGP
MMQPGQQGPR PGGRRSGDGP MRHQHQQPMP YMQPQMMPRG RGYRYPSGGR NMPDGPMPGG
MVPVAYDMNV MPYSQPMSAG QLATSLANAT PAQQRTLLGE SLYPLVDQIE SEHAAKVTGM
LLEMDQTEVL HLLESPEALN AKVSEALDVL RNVNQPSSQG SEGNKSGSPS DLLASLSIND
HL
