PABN3_ARATH
ID PABN3_ARATH Reviewed; 217 AA.
AC Q9LX90; F4KGU0; F4KGU1;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Polyadenylate-binding protein 3 {ECO:0000303|PubMed:18479511};
DE Short=AtPabN2 {ECO:0000303|PubMed:23334891};
DE Short=AtPabN3 {ECO:0000303|PubMed:18479511};
DE Short=Poly(A)-binding protein 3 {ECO:0000303|PubMed:18479511};
DE AltName: Full=Nuclear poly(A)-binding protein 3 {ECO:0000305};
DE AltName: Full=Poly(A)-binding protein III {ECO:0000305};
DE Short=PABIII {ECO:0000305};
GN Name=PABN3 {ECO:0000303|PubMed:18479511};
GN OrderedLocusNames=At5g10350 {ECO:0000312|Araport:AT5G10350};
GN ORFNames=F12B17.300 {ECO:0000312|EMBL:CAB89408.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] (ISOFORM 1).
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 CSTF50; PAPS4; PABN1; PABN2 AND FIPS5,
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 PAPS4, PABN1, PABN2, CSTF50 and FIPS5 (PubMed:18479511).
CC Interacts 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LX90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LX90-2; Sequence=VSP_057235;
CC Name=3;
CC IsoId=Q9LX90-3; Sequence=VSP_057236;
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; AL353995; CAB89408.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91528.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91529.1; -; Genomic_DNA.
DR EMBL; BT003893; AAO41941.1; -; mRNA.
DR EMBL; BT005003; AAO50536.1; -; mRNA.
DR PIR; T50004; T50004.
DR RefSeq; NP_196597.1; NM_121073.4. [Q9LX90-1]
DR RefSeq; NP_850803.1; NM_180472.1. [Q9LX90-3]
DR AlphaFoldDB; Q9LX90; -.
DR SMR; Q9LX90; -.
DR BioGRID; 16177; 16.
DR IntAct; Q9LX90; 8.
DR STRING; 3702.AT5G10350.1; -.
DR PaxDb; Q9LX90; -.
DR PRIDE; Q9LX90; -.
DR ProteomicsDB; 248648; -. [Q9LX90-1]
DR EnsemblPlants; AT5G10350.1; AT5G10350.1; AT5G10350. [Q9LX90-1]
DR EnsemblPlants; AT5G10350.2; AT5G10350.2; AT5G10350. [Q9LX90-3]
DR GeneID; 830899; -.
DR Gramene; AT5G10350.1; AT5G10350.1; AT5G10350. [Q9LX90-1]
DR Gramene; AT5G10350.2; AT5G10350.2; AT5G10350. [Q9LX90-3]
DR KEGG; ath:AT5G10350; -.
DR Araport; AT5G10350; -.
DR TAIR; locus:2142519; AT5G10350.
DR eggNOG; KOG4209; Eukaryota.
DR InParanoid; Q9LX90; -.
DR OMA; EMADTHA; -.
DR PhylomeDB; Q9LX90; -.
DR PRO; PR:Q9LX90; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LX90; baseline and differential.
DR Genevisible; Q9LX90; AT.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0008143; F:poly(A) binding; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IPI: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 Alternative splicing; Coiled coil; Cytoplasm; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..217
FT /note="Polyadenylate-binding protein 3"
FT /id="PRO_0000431330"
FT DOMAIN 89..165
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..216
FT /note="Necessary for homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q86U42"
FT COILED 30..71
FT /evidence="ECO:0000255"
FT MOTIF 162..169
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT VAR_SEQ 1..95
FT /note="MEEEEHEVYGGEIPEVGDTDVPDPDIDMSAADEDAVTELAEMKRRLKEMEEE
FT AAALREMQAKVEKEMGATQDPASMAANQEGKEEVDARSVYVGN -> MLAFYH (in
FT isoform 2)"
FT /id="VSP_057235"
FT VAR_SEQ 203..217
FT /note="Missing (in isoform 3)"
FT /id="VSP_057236"
SQ SEQUENCE 217 AA; 24804 MW; 78DDB8A0947DAE35 CRC64;
MEEEEHEVYG GEIPEVGDTD VPDPDIDMSA ADEDAVTELA EMKRRLKEME EEAAALREMQ
AKVEKEMGAT QDPASMAANQ EGKEEVDARS VYVGNVDYAC TPEEVQLHFQ TCGTVNRVTI
LMDKFGQPKG FAYVEFVEVE AVQEALQLNE SELHGRQLKV SPKRTNVPGM KQYHPGRFNP
SMGYRFRRPF VPPYFYSPYG YGKAPRFRRP MRYMPYQ
