PABN1_ARATH
ID PABN1_ARATH Reviewed; 227 AA.
AC Q93VI4; Q8LG48; Q9LU62;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Polyadenylate-binding protein 1 {ECO:0000303|PubMed:18479511};
DE Short=AtPabN1 {ECO:0000303|PubMed:18479511};
DE Short=Poly(A)-binding protein 1 {ECO:0000303|PubMed:18479511};
DE AltName: Full=Nuclear poly(A)-binding protein 1 {ECO:0000305};
DE AltName: Full=Poly(A)-binding protein I {ECO:0000305};
DE Short=PABI {ECO:0000305};
GN Name=PABN1 {ECO:0000303|PubMed:16282318, ECO:0000303|PubMed:18479511};
GN OrderedLocusNames=At5g51120 {ECO:0000312|Araport:AT5G51120};
GN ORFNames=MWD22.6 {ECO:0000312|EMBL:BAA97374.1};
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|EMBL:AAL09819.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND INTERACTION WITH FIPS5.
RX PubMed=16282318; DOI=10.1074/jbc.m510964200;
RA Forbes K.P., Addepalli B., Hunt A.G.;
RT "An Arabidopsis Fip1 homolog interacts with RNA and provides conceptual
RT links with a number of other polyadenylation factor subunits.";
RL J. Biol. Chem. 281:176-186(2006).
RN [6]
RP SUBUNIT, HOMODIMER, INTERACTION WITH FIPS5; PABN2; PABN3 AND PAPS4, GENE
RP 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 [7]
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 FIPS5, PABN3 and PAPS4 (PubMed:16282318, PubMed:18479511).
CC Interacts with CSP3 (PubMed:23334891). {ECO:0000250|UniProtKB:Q86U42,
CC ECO:0000269|PubMed:16282318, ECO:0000269|PubMed:18479511,
CC ECO:0000269|PubMed:23334891}.
CC -!- INTERACTION:
CC Q93VI4; F4KDH9: FIPS5; NbExp=3; IntAct=EBI-962543, EBI-962489;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q93VI4-1; Sequence=Displayed;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97374.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB023044; BAA97374.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96038.1; -; Genomic_DNA.
DR EMBL; AY054186; AAL06847.1; -; mRNA.
DR EMBL; AY057580; AAL09819.1; -; mRNA.
DR EMBL; AY079392; AAL85123.1; -; mRNA.
DR EMBL; AY116673; AAM47151.1; -; mRNA.
DR EMBL; AY084464; AAM61036.1; -; mRNA.
DR RefSeq; NP_568751.1; NM_124491.3. [Q93VI4-1]
DR AlphaFoldDB; Q93VI4; -.
DR SMR; Q93VI4; -.
DR BioGRID; 20431; 12.
DR IntAct; Q93VI4; 10.
DR PRIDE; Q93VI4; -.
DR ProteomicsDB; 234944; -. [Q93VI4-1]
DR EnsemblPlants; AT5G51120.1; AT5G51120.1; AT5G51120. [Q93VI4-1]
DR GeneID; 835186; -.
DR Gramene; AT5G51120.1; AT5G51120.1; AT5G51120. [Q93VI4-1]
DR KEGG; ath:AT5G51120; -.
DR Araport; AT5G51120; -.
DR PhylomeDB; Q93VI4; -.
DR PRO; PR:Q93VI4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93VI4; baseline and differential.
DR Genevisible; Q93VI4; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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 Alternative splicing; Coiled coil; Cytoplasm; mRNA processing; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..227
FT /note="Polyadenylate-binding protein 1"
FT /id="PRO_0000431328"
FT DOMAIN 103..179
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..227
FT /note="Necessary for homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q86U42"
FT COILED 48..83
FT /evidence="ECO:0000255"
FT MOTIF 176..183
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 12..32
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 15
FT /note="E -> D (in Ref. 4; AAM61036)"
SQ SEQUENCE 227 AA; 25671 MW; B5243EA7809A55DA CRC64;
MPVHDEQEHE VYGGEIPEEE EGEMDTEEYE EHGGEEGAAA GDEELEPGSS SRDLEDMKKR
IKEIEEEAGA LREMQAKAEK DMGASQDPSG GVSAAEKEEV DSRSIYVGNV DYACTPEEVQ
QHFQSCGTVN RVTILTDKFG QPKGFAYVEF VEVEAVQNSL ILNESELHGR QIKVSAKRTN
VPGMRQFRGR GRPFRPMRGF MPGVPFYPPY AYGRVPRFRR PMRYRPY
