PAPS4_ARATH
ID PAPS4_ARATH Reviewed; 741 AA.
AC Q8VYW1; B3H654; B9DFE4; F4JV63; F4JV67; F4JV69; F4JV71; F4JV72; Q0WLA9;
AC Q7XJ91; Q9M075;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nuclear poly(A) polymerase 4 {ECO:0000303|PubMed:18479511};
DE Short=AtPAP(IV) {ECO:0000303|PubMed:16282318};
DE Short=PAP(IV) {ECO:0000305};
DE Short=Poly(A) polymerase IV {ECO:0000305};
DE Short=nPAP {ECO:0000303|PubMed:16282318};
DE EC=2.7.7.19 {ECO:0000269|PubMed:15297145};
DE AltName: Full=Polynucleotide adenylyltransferase 4 {ECO:0000305};
GN Name=PAPS4 {ECO:0000303|PubMed:18479511};
GN Synonyms=NPAP {ECO:0000303|PubMed:16282318};
GN OrderedLocusNames=At4g32850 {ECO:0000312|Araport:AT4G32850};
GN ORFNames=T16I18.60 {ECO:0000312|EMBL:CAB80002.1};
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:AAL47435.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] (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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING, FUNCTION,
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15297145; DOI=10.1016/j.bbaexp.2004.06.001;
RA Addepalli B., Meeks L.R., Forbes K.P., Hunt A.G.;
RT "Novel alternative splicing of mRNAs encoding poly(A) polymerases in
RT Arabidopsis.";
RL Biochim. Biophys. Acta 1679:117-128(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP INTERACTION WITH CFIS2; PAPS1; PABN1; PABN2; PABN3; FIPS3 AND FIPS5, 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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19956626; DOI=10.1371/journal.pone.0008082;
RA Meeks L.R., Addepalli B., Hunt A.G.;
RT "Characterization of genes encoding poly(A) polymerases in plants: evidence
RT for duplication and functional specialization.";
RL PLoS ONE 4:E8082-E8082(2009).
CC -!- FUNCTION: Essential protein (PubMed:19956626). Polymerase that creates
CC the 3'-poly(A) tail of mRNA's (PubMed:15297145). Also required for the
CC endoribonucleolytic cleavage reaction at some polyadenylation sites.
CC May acquire specificity through interaction with a cleavage and
CC polyadenylation specificity factor (CPSF) at its C-terminus (By
CC similarity). {ECO:0000250|UniProtKB:P25500,
CC ECO:0000269|PubMed:15297145, ECO:0000269|PubMed:19956626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000269|PubMed:15297145};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P25500};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P25500};
CC Note=Binds 2 magnesium ions. Also active with manganese.
CC {ECO:0000250|UniProtKB:P25500};
CC -!- SUBUNIT: Monomer (By similarity). Forms a complex with cleavage and
CC polyadenylation specificity factor (CPSF) subunits CFIS2, FIPS3, PAPS1,
CC PABN1, PABN2, PABN3 and FIPS5 (PubMed:16282318, PubMed:18479511).
CC {ECO:0000250|UniProtKB:P25500, ECO:0000269|PubMed:16282318,
CC ECO:0000269|PubMed:18479511}.
CC -!- INTERACTION:
CC Q8VYW1; F4KDH9: FIPS5; NbExp=3; IntAct=EBI-962558, EBI-962489;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:19956626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q8VYW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VYW1-2; Sequence=VSP_057252;
CC Name=3;
CC IsoId=Q8VYW1-3; Sequence=VSP_057254;
CC Name=4;
CC IsoId=Q8VYW1-4; Sequence=VSP_057249;
CC Name=5;
CC IsoId=Q8VYW1-5; Sequence=VSP_057246, VSP_057251;
CC Name=6;
CC IsoId=Q8VYW1-6; Sequence=VSP_057250;
CC Name=7;
CC IsoId=Q8VYW1-7; Sequence=VSP_057247, VSP_057248;
CC Name=8;
CC IsoId=Q8VYW1-8; Sequence=VSP_057253;
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers (very active in pollen,
CC sepals, styles, and stigmas), cotyledons and hypocotyls, and, to a
CC lower extent, in roots (confined to the vascular tissue in the radicle)
CC and leaves (in the vascular tissue and leaf petioles). Barely detected
CC in stems (PubMed:15297145, PubMed:19956626). Active in the primary and
CC secondary root systems (PubMed:19956626). {ECO:0000269|PubMed:15297145,
CC ECO:0000269|PubMed:19956626}.
CC -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000269|PubMed:19956626}.
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence. {ECO:0000305|Ref.6}.
CC -!- MISCELLANEOUS: [Isoform 4]: Incomplete sequence.
CC {ECO:0000305|PubMed:15297145}.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB80002.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL161582; CAB80002.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE86126.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86127.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86128.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86129.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86130.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86131.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86132.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86133.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86134.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86135.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67865.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67866.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67867.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67868.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67869.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67870.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67871.1; -; Genomic_DNA.
DR EMBL; AY069880; AAL47435.1; -; mRNA.
DR EMBL; BT000485; AAN18054.1; -; mRNA.
DR EMBL; AK316738; BAH19461.1; -; mRNA.
DR EMBL; AK318704; BAH56819.1; -; mRNA.
DR EMBL; AY323908; AAP86216.1; -; mRNA.
DR EMBL; AK230297; BAF02098.1; -; mRNA.
DR PIR; T10692; T10692.
DR RefSeq; NP_001031778.1; NM_001036701.1. [Q8VYW1-7]
DR RefSeq; NP_001031779.1; NM_001036702.1. [Q8VYW1-8]
DR RefSeq; NP_001119102.1; NM_001125630.1. [Q8VYW1-3]
DR RefSeq; NP_001119103.1; NM_001125631.2. [Q8VYW1-2]
DR RefSeq; NP_001329663.1; NM_001342181.1. [Q8VYW1-5]
DR RefSeq; NP_001329664.1; NM_001342180.1. [Q8VYW1-5]
DR RefSeq; NP_001329665.1; NM_001342179.1. [Q8VYW1-5]
DR RefSeq; NP_001329666.1; NM_001342185.1. [Q8VYW1-5]
DR RefSeq; NP_001329667.1; NM_001342184.1. [Q8VYW1-5]
DR RefSeq; NP_001329668.1; NM_001342183.1. [Q8VYW1-5]
DR RefSeq; NP_001329669.1; NM_001342182.1. [Q8VYW1-5]
DR RefSeq; NP_195011.4; NM_119438.4. [Q8VYW1-6]
DR RefSeq; NP_849561.1; NM_179230.2. [Q8VYW1-1]
DR RefSeq; NP_849562.2; NM_179231.2. [Q8VYW1-4]
DR RefSeq; NP_974668.1; NM_202939.3. [Q8VYW1-5]
DR RefSeq; NP_974669.1; NM_202940.3. [Q8VYW1-3]
DR RefSeq; NP_974670.2; NM_202941.3. [Q8VYW1-4]
DR AlphaFoldDB; Q8VYW1; -.
DR SMR; Q8VYW1; -.
DR BioGRID; 14706; 9.
DR IntAct; Q8VYW1; 7.
DR STRING; 3702.AT4G32850.8; -.
DR iPTMnet; Q8VYW1; -.
DR PaxDb; Q8VYW1; -.
DR PRIDE; Q8VYW1; -.
DR ProteomicsDB; 236323; -. [Q8VYW1-1]
DR EnsemblPlants; AT4G32850.1; AT4G32850.1; AT4G32850. [Q8VYW1-1]
DR EnsemblPlants; AT4G32850.10; AT4G32850.10; AT4G32850. [Q8VYW1-2]
DR EnsemblPlants; AT4G32850.11; AT4G32850.11; AT4G32850. [Q8VYW1-5]
DR EnsemblPlants; AT4G32850.12; AT4G32850.12; AT4G32850. [Q8VYW1-5]
DR EnsemblPlants; AT4G32850.13; AT4G32850.13; AT4G32850. [Q8VYW1-5]
DR EnsemblPlants; AT4G32850.14; AT4G32850.14; AT4G32850. [Q8VYW1-5]
DR EnsemblPlants; AT4G32850.15; AT4G32850.15; AT4G32850. [Q8VYW1-5]
DR EnsemblPlants; AT4G32850.16; AT4G32850.16; AT4G32850. [Q8VYW1-5]
DR EnsemblPlants; AT4G32850.17; AT4G32850.17; AT4G32850. [Q8VYW1-5]
DR EnsemblPlants; AT4G32850.2; AT4G32850.2; AT4G32850. [Q8VYW1-4]
DR EnsemblPlants; AT4G32850.3; AT4G32850.3; AT4G32850. [Q8VYW1-6]
DR EnsemblPlants; AT4G32850.4; AT4G32850.4; AT4G32850. [Q8VYW1-5]
DR EnsemblPlants; AT4G32850.5; AT4G32850.5; AT4G32850. [Q8VYW1-3]
DR EnsemblPlants; AT4G32850.6; AT4G32850.6; AT4G32850. [Q8VYW1-4]
DR EnsemblPlants; AT4G32850.7; AT4G32850.7; AT4G32850. [Q8VYW1-7]
DR EnsemblPlants; AT4G32850.8; AT4G32850.8; AT4G32850. [Q8VYW1-8]
DR EnsemblPlants; AT4G32850.9; AT4G32850.9; AT4G32850. [Q8VYW1-3]
DR GeneID; 829421; -.
DR Gramene; AT4G32850.1; AT4G32850.1; AT4G32850. [Q8VYW1-1]
DR Gramene; AT4G32850.10; AT4G32850.10; AT4G32850. [Q8VYW1-2]
DR Gramene; AT4G32850.11; AT4G32850.11; AT4G32850. [Q8VYW1-5]
DR Gramene; AT4G32850.12; AT4G32850.12; AT4G32850. [Q8VYW1-5]
DR Gramene; AT4G32850.13; AT4G32850.13; AT4G32850. [Q8VYW1-5]
DR Gramene; AT4G32850.14; AT4G32850.14; AT4G32850. [Q8VYW1-5]
DR Gramene; AT4G32850.15; AT4G32850.15; AT4G32850. [Q8VYW1-5]
DR Gramene; AT4G32850.16; AT4G32850.16; AT4G32850. [Q8VYW1-5]
DR Gramene; AT4G32850.17; AT4G32850.17; AT4G32850. [Q8VYW1-5]
DR Gramene; AT4G32850.2; AT4G32850.2; AT4G32850. [Q8VYW1-4]
DR Gramene; AT4G32850.3; AT4G32850.3; AT4G32850. [Q8VYW1-6]
DR Gramene; AT4G32850.4; AT4G32850.4; AT4G32850. [Q8VYW1-5]
DR Gramene; AT4G32850.5; AT4G32850.5; AT4G32850. [Q8VYW1-3]
DR Gramene; AT4G32850.6; AT4G32850.6; AT4G32850. [Q8VYW1-4]
DR Gramene; AT4G32850.7; AT4G32850.7; AT4G32850. [Q8VYW1-7]
DR Gramene; AT4G32850.8; AT4G32850.8; AT4G32850. [Q8VYW1-8]
DR Gramene; AT4G32850.9; AT4G32850.9; AT4G32850. [Q8VYW1-3]
DR KEGG; ath:AT4G32850; -.
DR Araport; AT4G32850; -.
DR TAIR; locus:2134113; AT4G32850.
DR eggNOG; KOG2245; Eukaryota.
DR OMA; ITAMHLR; -.
DR OrthoDB; 326577at2759; -.
DR PhylomeDB; Q8VYW1; -.
DR BRENDA; 2.7.7.19; 399.
DR PRO; PR:Q8VYW1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VYW1; baseline and differential.
DR Genevisible; Q8VYW1; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0043631; P:RNA polyadenylation; IDA:TAIR.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR007012; PolA_pol_cen_dom.
DR InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR InterPro; IPR014492; PolyA_polymerase.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF04928; PAP_central; 1.
DR Pfam; PF04926; PAP_RNA-bind; 1.
DR PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR SUPFAM; SSF55003; SSF55003; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Magnesium; Metal-binding;
KW mRNA processing; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..741
FT /note="Nuclear poly(A) polymerase 4"
FT /id="PRO_0000431348"
FT REGION 494..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 485..492
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 526..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P25500"
FT BINDING 113..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P29468"
FT BINDING 114..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P25500"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25500"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25500"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25500"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25500"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P25500"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25500"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P25500"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P25500"
FT BINDING 248..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P25500"
FT SITE 160
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P29468"
FT SITE 330
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P29468"
FT SITE 401
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P29468"
FT SITE 406
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P29468"
FT SITE 598
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P29468"
FT VAR_SEQ 713..730
FT /note="SNSLVSGMEKSEDRARSE -> VIKLPHSSYHKISSVENI (in isoform
FT 5)"
FT /id="VSP_057246"
FT VAR_SEQ 713..716
FT /note="SNSL -> CQET (in isoform 7)"
FT /id="VSP_057247"
FT VAR_SEQ 717..741
FT /note="Missing (in isoform 7)"
FT /id="VSP_057248"
FT VAR_SEQ 728..741
FT /note="RSESFQKSQIRLLT -> STSRLSLKSTV (in isoform 4)"
FT /id="VSP_057249"
FT VAR_SEQ 729..741
FT /note="SESFQKSQIRLLT -> LSLKSTV (in isoform 6)"
FT /id="VSP_057250"
FT VAR_SEQ 731..741
FT /note="Missing (in isoform 5)"
FT /id="VSP_057251"
FT VAR_SEQ 739..741
FT /note="LLT -> HVCYAKS (in isoform 2)"
FT /id="VSP_057252"
FT VAR_SEQ 739..741
FT /note="LLT -> HAIDVKKTGDFNSNCCVGQTTESRSFW (in isoform 8)"
FT /id="VSP_057253"
FT VAR_SEQ 740..741
FT /note="LT -> SLKSTV (in isoform 3)"
FT /id="VSP_057254"
SQ SEQUENCE 741 AA; 83943 MW; BCA233700431BB6D CRC64;
MMVGTQNLGG SLPPLNSPKS YGITKPLSLA GPSSADIKRN VELEKYLVDE GLYESKDDTM
RREEVLGRID QIVKHWVKQL TQQRGYTDQM VEDANAVIFT FGSYRLGVHG PGADIDTLCV
GPSYVNREED FFIILHDILA EMEEVTELHP VPDAHVPVMK FKFQGIPIDL LYASISLLVV
PQDLDISSSS VLCEVDEPTV RSLNGCRVAD QILKLVPNFE HFRTTLRCLK YWAKKRGVYS
NVTGFLGGVN WALLVARVCQ LYPNAIPSML VSRFFRVYTQ WRWPNPVMLC AIEEDELGFP
VWDRRKNHRD RYHLMPIITP AYPCMNSSYN VSQSTLRVMT EQFQFGNNIL QEIELNKQHW
SSLFEQYMFF EAYKNYLQVD IVAADAEDLL AWKGWVESRF RQLTLKIERD TNGMLMCHPQ
PNEYVDTARQ FLHCAFFMGL QRAEGVGGQE CQQFDIRGTV DEFRQEVNMY MFWKPGMDVF
VSHVRRRQLP PFVFPNGYRR PRQSRHQNLP GGKSGEDGSV SHSGSVVERH AKRKNDSEMM
DVRPEKPEKR ASLSPQSLDI VSPENSAITT GWTPPVCNLR RPPSEEIEAD NLNTECTELT
DLARNECNSG SEQVLEVDSM AVVQECSDPA EPLGKCVTPD SVDVVACVSG QEENLDRNLR
SVSISGTDSP LLPSRSCGQN RDYEGFGFPA ANSDPMGKKN LYSQSGMSED LQSNSLVSGM
EKSEDRARSE SFQKSQIRLL T
