PABN2_ARATH
ID PABN2_ARATH Reviewed; 220 AA.
AC Q9FJN9;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Polyadenylate-binding protein 2 {ECO:0000303|PubMed:18479511};
DE Short=AtPabN2 {ECO:0000303|PubMed:18479511};
DE Short=AtPabN3 {ECO:0000303|PubMed:23334891};
DE Short=Poly(A)-binding protein 2 {ECO:0000303|PubMed:18479511};
DE AltName: Full=Nuclear poly(A)-binding protein 2 {ECO:0000305};
DE AltName: Full=Poly(A)-binding protein II {ECO:0000305};
DE Short=PABII {ECO:0000305};
GN Name=PABN2 {ECO:0000303|PubMed:18479511};
GN OrderedLocusNames=At5g65260 {ECO:0000312|Araport:AT5G65260};
GN ORFNames=MQN23.20 {ECO:0000312|EMBL:AAK62429.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 SUBUNIT, HOMODIMER, INTERACTION WITH PAPS2; PAPS4; FIPS5; PABN3 AND PABN1,
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18479511; DOI=10.1186/1471-2164-9-220;
RA Hunt A.G., Xu R., Addepalli B., Rao S., Forbes K.P., Meeks L.R., Xing D.,
RA Mo M., Zhao H., Bandyopadhyay A., Dampanaboina L., Marion A.,
RA Von Lanken C., Li Q.Q.;
RT "Arabidopsis mRNA polyadenylation machinery: comprehensive analysis of
RT protein-protein interactions and gene expression profiling.";
RL BMC Genomics 9:220-220(2008).
RN [5]
RP INTERACTION WITH CSP3, AND SUBCELLULAR LOCATION.
RX PubMed=23334891; DOI=10.1007/s12192-012-0398-3;
RA Kim M.H., Sonoda Y., Sasaki K., Kaminaka H., Imai R.;
RT "Interactome analysis reveals versatile functions of Arabidopsis COLD SHOCK
RT DOMAIN PROTEIN 3 in RNA processing within the nucleus and cytoplasm.";
RL Cell Stress Chaperones 18:517-525(2013).
CC -!- FUNCTION: Involved in the 3'-end formation of mRNA precursors (pre-
CC mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream
CC cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring
CC processivity on the poly(A) tail elongation reaction and controls also
CC the poly(A) tail length. Increases the affinity of poly(A) polymerase
CC for RNA. Binds to poly(A) and to poly(G) with high affinity. May
CC protect the poly(A) tail from degradation.
CC {ECO:0000250|UniProtKB:Q7KNF2}.
CC -!- SUBUNIT: Monomer and homooligomer (PubMed:18479511). Binds RNA as a
CC monomer and oligomerizes when bound to poly(A) (By similarity). Forms a
CC complex with cleavage and polyadenylation specificity factor (CPSF)
CC subunits PAPS2, FIPS5, PABN3 and PABN1 (PubMed:18479511). Interacts
CC with CSP3 (PubMed:23334891). {ECO:0000250|UniProtKB:Q86U42,
CC ECO:0000269|PubMed:18479511, ECO:0000269|PubMed:23334891}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000255|PROSITE-
CC ProRule:PRU00768, ECO:0000269|PubMed:23334891}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q7KNF2}. Note=Shuttles between the nucleus and
CC the cytoplasm but predominantly found in the nucleus.
CC {ECO:0000250|UniProtKB:Q7KNF2}.
CC -!- DOMAIN: The RRM domain is essential for the recognition of specific
CC adenine bases in the poly(A) tail, but not sufficient for poly(A)
CC binding. {ECO:0000250|UniProtKB:Q28165}.
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DR EMBL; AB013395; BAB11662.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98030.1; -; Genomic_DNA.
DR EMBL; AF386984; AAK62429.1; -; mRNA.
DR EMBL; BT000018; AAN15337.1; -; mRNA.
DR RefSeq; NP_201329.1; NM_125924.3.
DR AlphaFoldDB; Q9FJN9; -.
DR SMR; Q9FJN9; -.
DR BioGRID; 21893; 6.
DR IntAct; Q9FJN9; 5.
DR STRING; 3702.AT5G65260.1; -.
DR PaxDb; Q9FJN9; -.
DR PRIDE; Q9FJN9; -.
DR ProteomicsDB; 234945; -.
DR EnsemblPlants; AT5G65260.1; AT5G65260.1; AT5G65260.
DR GeneID; 836651; -.
DR Gramene; AT5G65260.1; AT5G65260.1; AT5G65260.
DR KEGG; ath:AT5G65260; -.
DR Araport; AT5G65260; -.
DR TAIR; locus:2171780; AT5G65260.
DR eggNOG; KOG4209; Eukaryota.
DR HOGENOM; CLU_012062_23_4_1; -.
DR InParanoid; Q9FJN9; -.
DR OMA; GFRRPYV; -.
DR OrthoDB; 1412946at2759; -.
DR PhylomeDB; Q9FJN9; -.
DR PRO; PR:Q9FJN9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJN9; baseline and differential.
DR Genevisible; Q9FJN9; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR Gene3D; 3.30.70.330; -; 1.
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; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..220
FT /note="Polyadenylate-binding protein 2"
FT /id="PRO_0000431329"
FT DOMAIN 92..168
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..219
FT /note="Necessary for homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q86U42"
FT COILED 34..74
FT /evidence="ECO:0000255"
FT MOTIF 165..172
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
SQ SEQUENCE 220 AA; 25250 MW; DEF2869F4049B73C CRC64;
MEEEEHEVYG GEIPDVGEMD GDMEALNPDL DMAAADDDAV KELDEMKKRL KEMEDEAAAL
REMQAKVEKE MGAQDPASIA ANQAGKEEVD ARSVFVGNVD YACTPEEVQQ HFQTCGTVHR
VTILTDKFGQ PKGFAYVEFV EVEAVQEALQ LNESELHGRQ LKVLQKRTNV PGLKQFRGRR
FNPYMGYRFR RPFMSPYMYS PYGYGKAPRF RRPMRYMPYQ
