ANM13_ARATH
ID ANM13_ARATH Reviewed; 535 AA.
AC Q84W92; Q0WRU3; Q66GI8; Q9M906;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable histone-arginine methyltransferase 1.3;
DE Short=AtPRMT13;
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:Q99873};
DE AltName: Full=Coactivator-associated methyltransferase 1A;
DE AltName: Full=Protein arginine N-methyltransferase 4B;
DE Short=AtPRMT4B;
GN Name=PRMT13; Synonyms=CARM1A, PRMT4B;
GN OrderedLocusNames=At3g06930 {ECO:0000312|Araport:AT3G06930};
GN ORFNames=F17A9.8 {ECO:0000312|EMBL:AAF26997.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17005254; DOI=10.1016/j.pharmthera.2006.06.007;
RA Krause C.D., Yang Z.-H., Kim Y.-S., Lee J.-H., Cook J.R., Pestka S.;
RT "Protein arginine methyltransferases: evolution and assessment of their
RT pharmacological and therapeutic potential.";
RL Pharmacol. Ther. 113:50-87(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PQT3, REPRESSION BY PQT3,
RP INDUCTION BY MG132, SUBCELLULAR LOCATION, AND UBIQUITINATION BY PQT3.
RC STRAIN=cv. Columbia;
RX PubMed=27676073; DOI=10.1371/journal.pgen.1006332;
RA Luo C., Cai X.-T., Du J., Zhao T.-L., Wang P.-F., Zhao P.-X., Liu R.,
RA Xie Q., Cao X.-F., Xiang C.-B.;
RT "PARAQUAT TOLERANCE3 is an E3 ligase that switches off activated oxidative
RT response by targeting histone-modifying PROTEIN METHYLTRANSFERASE4b.";
RL PLoS Genet. 12:E1006332-E1006332(2016).
CC -!- FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino
CC nitrogens of arginyl residues in several proteins involved in DNA
CC packaging, transcription regulation, and mRNA stability (By
CC similarity). Recruited to promoters upon gene activation, methylates
CC histone H3 and activates transcription via chromatin remodeling
CC (PubMed:27676073). Positive regulator in the oxidative stress tolerance
CC that promotes the expression of enzymes preventing oxidative stress
CC such as APX1 and GPX1 by histone methylation (H3R17me2a). Confers
CC tolerance to cadmium CdCl(2) and salt NaCl stresses (PubMed:27676073).
CC {ECO:0000250|UniProtKB:Q9WVG6, ECO:0000269|PubMed:27676073}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC Evidence={ECO:0000250|UniProtKB:Q99873};
CC -!- SUBUNIT: Interacts with PQT3 in the nucleus.
CC {ECO:0000269|PubMed:27676073}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27676073}. Cytoplasm
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84W92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84W92-3; Sequence=VSP_027461;
CC -!- INDUCTION: Targeted by PQT3 to degradation via 26S proteasome. Induced
CC by proteasome inhibitor MG132 treatment (at protein level).
CC {ECO:0000269|PubMed:27676073}.
CC -!- PTM: Ubiquitinated by PQT3. {ECO:0000269|PubMed:27676073}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to paraquat-triggered
CC oxidative stress. Slower root elongation after cadmium ion CdCl(2)
CC treatment. Decreased histone H3 methylation (H3R17me2a) leading to
CC reduced levels of APX1 and GPX1. {ECO:0000269|PubMed:27676073}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26997.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF00156.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. Its C-terminal part is derived from gene At1g80500, which oded for an intracellular transporter.; Evidence={ECO:0000305};
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DR EMBL; AC016827; AAF26997.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74477.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74478.1; -; Genomic_DNA.
DR EMBL; BT004102; AAO42127.1; -; mRNA.
DR EMBL; BT015414; AAU05537.1; -; mRNA.
DR EMBL; AK228202; BAF00156.1; ALT_SEQ; mRNA.
DR RefSeq; NP_187349.2; NM_111573.5. [Q84W92-3]
DR RefSeq; NP_850528.1; NM_180197.2. [Q84W92-1]
DR AlphaFoldDB; Q84W92; -.
DR SMR; Q84W92; -.
DR BioGRID; 5213; 4.
DR IntAct; Q84W92; 1.
DR STRING; 3702.AT3G06930.2; -.
DR iPTMnet; Q84W92; -.
DR PaxDb; Q84W92; -.
DR PRIDE; Q84W92; -.
DR ProteomicsDB; 245004; -. [Q84W92-1]
DR EnsemblPlants; AT3G06930.1; AT3G06930.1; AT3G06930. [Q84W92-3]
DR EnsemblPlants; AT3G06930.2; AT3G06930.2; AT3G06930. [Q84W92-1]
DR GeneID; 819878; -.
DR Gramene; AT3G06930.1; AT3G06930.1; AT3G06930. [Q84W92-3]
DR Gramene; AT3G06930.2; AT3G06930.2; AT3G06930. [Q84W92-1]
DR KEGG; ath:AT3G06930; -.
DR Araport; AT3G06930; -.
DR TAIR; locus:2077567; AT3G06930.
DR eggNOG; KOG1500; Eukaryota.
DR HOGENOM; CLU_017375_0_2_1; -.
DR InParanoid; Q84W92; -.
DR OMA; FSRANFW; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q84W92; -.
DR PRO; PR:Q84W92; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84W92; baseline and differential.
DR Genevisible; Q84W92; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016277; F:[myelin basic protein]-arginine N-methyltransferase activity; IDA:TAIR.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:TAIR.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:TAIR.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:TAIR.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034971; P:histone H3-R17 methylation; IMP:UniProtKB.
DR GO; GO:0034970; P:histone H3-R2 methylation; IDA:TAIR.
DR GO; GO:0034972; P:histone H3-R26 methylation; IDA:TAIR.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA:TAIR.
DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IGI:TAIR.
DR GO; GO:0046686; P:response to cadmium ion; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IGI:TAIR.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Chromatin regulator;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Stress response; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation.
FT CHAIN 1..535
FT /note="Probable histone-arginine methyltransferase 1.3"
FT /id="PRO_0000294004"
FT DOMAIN 141..456
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 494..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 257
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT ACT_SITE 266
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 271
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:A3KPF2"
FT VAR_SEQ 510
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_027461"
FT CONFLICT 127
FT /note="G -> V (in Ref. 5; BAF00156)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="P -> Q (in Ref. 3; AAO42127)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="F -> L (in Ref. 3; AAO42127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 59915 MW; E70BF4F1F6606888 CRC64;
MEVSSVKKLE QLEYSLESVT DLSSSSVSSS SPAVATFSYV DGVTELRFLQ SDSTHCFNFD
LASAQLFKLG PVHFICVSDG SSSSEEKSFS KGVNIKFKNE KDSKDFCESF EEWRNDSVVQ
GSSLQNGTVS ANKSKFDNKI EASSAKMYFH YYGQLLHQQN MLQDYVRTGT YYAAVMENHS
DFAGRVVVDV GAGSGILSMF AAQAGAKHVY AVEASEMAEY ARKLIAGNPL FADRITVIKG
KVEDIELPEK ADILISEPMG TLLVNERMLE SYVIARDRFM TPKGKMFPTV GRIHMAPFSD
EFLFIEMANK AMFWQQQNYY GVDLTPLYGS AHQGYFSQPV VDAFDPRLLV ASPMFHMIDF
TQMKEEDFYE IDIPLKFTAS MCTRMHGLAC WFDVLFDGST VQRWLTTAPG APTTHWYQIR
CVLSQPIYVM AGQEITGRLH LIAHSAQSYT IDLTLSAKMW GPGASQGGIL QSSTCKFDLK
EPYYRMSQPQ AYPVAQEPPL QPQPELSTQQ DIQTPNDELE EELLQQLPQN PSAQL
