ANM14_ARATH
ID ANM14_ARATH Reviewed; 528 AA.
AC A3KPF2; Q3E8E0; Q84WN5; Q9FI68;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable histone-arginine methyltransferase 1.4;
DE Short=AtPRMT14;
DE EC=2.1.1.319;
DE AltName: Full=Coactivator-associated methyltransferase 1B;
DE AltName: Full=Protein arginine N-methyltransferase 4A;
DE Short=AtPRMT4A;
GN Name=PRMT14; Synonyms=CARM1B, PRMT4A; OrderedLocusNames=At5g49020;
GN ORFNames=K19E20.17;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 94-528.
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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. Recruited to
CC promoters upon gene activation, methylates histone H3 and activates
CC transcription via chromatin remodeling. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A3KPF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A3KPF2-2; Sequence=VSP_026577;
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=BAB10326.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB017061; BAB10326.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95760.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95761.1; -; Genomic_DNA.
DR EMBL; BT030319; ABO09883.1; -; mRNA.
DR EMBL; BT030323; ABO09886.1; -; mRNA.
DR EMBL; BT002972; AAO22781.1; -; mRNA.
DR RefSeq; NP_199713.2; NM_124279.5. [A3KPF2-1]
DR RefSeq; NP_974913.1; NM_203184.2. [A3KPF2-2]
DR AlphaFoldDB; A3KPF2; -.
DR SMR; A3KPF2; -.
DR BioGRID; 20207; 2.
DR STRING; 3702.AT5G49020.1; -.
DR iPTMnet; A3KPF2; -.
DR PaxDb; A3KPF2; -.
DR PRIDE; A3KPF2; -.
DR ProteomicsDB; 244422; -. [A3KPF2-1]
DR EnsemblPlants; AT5G49020.1; AT5G49020.1; AT5G49020. [A3KPF2-1]
DR EnsemblPlants; AT5G49020.2; AT5G49020.2; AT5G49020. [A3KPF2-2]
DR GeneID; 834961; -.
DR Gramene; AT5G49020.1; AT5G49020.1; AT5G49020. [A3KPF2-1]
DR Gramene; AT5G49020.2; AT5G49020.2; AT5G49020. [A3KPF2-2]
DR KEGG; ath:AT5G49020; -.
DR Araport; AT5G49020; -.
DR TAIR; locus:2154339; AT5G49020.
DR eggNOG; KOG1500; Eukaryota.
DR InParanoid; A3KPF2; -.
DR OMA; PTQCYQF; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; A3KPF2; -.
DR PRO; PR:A3KPF2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; A3KPF2; baseline and differential.
DR Genevisible; A3KPF2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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; IGI:TAIR.
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:0009909; P:regulation of flower development; IGI:TAIR.
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; Alternative splicing; Chromatin regulator; Cytoplasm;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..528
FT /note="Probable histone-arginine methyltransferase 1.4"
FT /id="PRO_0000294005"
FT DOMAIN 144..459
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 260
FT /evidence="ECO:0000250"
FT ACT_SITE 269
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 274
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:0007744|PubMed:22223895"
FT VAR_SEQ 123..124
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026577"
SQ SEQUENCE 528 AA; 58857 MW; 31BC878D35445BD8 CRC64;
MEIPSLNKQQ EFTLASVTDL TSPSSSLSSS PVVATFSCVN EVKELRFQES KSSDGFSFDL
SSTQLFKLGP LQFTCVSDGS ISSAKEKSSF SRGVVIKFRD EKDSKEFCDS FEECKKDDAV
KQGSALPNGT VVSANKSKFD DKIEAASAKM YFHYYGQLLH QQNMLQDYVR TGTYHAAVME
NRSDFSGRVV VDVGAGSGIL SMFAALAGAK HVYAVEASEM AEYARKLIAG NPLLAERITV
IKGKIEDIEL PEKADVLISE PMGTLLVNER MLETYVIARD RFLSPNGKMF PTVGRIHMAP
FADEFLFVEM ANKALFWQQQ NYYGVDLTPL YVSAHQGYFS QPVVDAFDPR LLVAPSMFHV
IDFTMMTEEQ FYEIDIPLKF TASVCTRIHG LACWFDVLFD GSTVQRWFTT APGAPTTHWY
QIRCVLSQPI HVMAGQEITG RLHLIAHSAQ SYTINLTLSA KMWGPGANQG GILQTSSCKL
DLKEPYYRMS QPQVYPTQEP PAQSQDIHIH SDDLEELELL QQNANAQL
