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   02-SEP-2026, entry version 123.
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
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   [6]
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 =
CC         N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC         homocysteine + 2 H(+); Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532,
CC         Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61897;
CC         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; OZ408687; CAO7055779.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7055780.1; -; 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   FunCoup; A3KPF2; 3638.
DR   STRING; 3702.A3KPF2; -.
DR   iPTMnet; A3KPF2; -.
DR   PaxDb; 3702-A3KPF2; -.
DR   ProteomicsDB; 244422; -. [A3KPF2-1]
DR   GeneID; 834961; -.
DR   KEGG; ath:AT5G49020; -.
DR   Araport; AT5G49020; -.
DR   TAIR; AT5G49020; PRMT4A.
DR   eggNOG; KOG1500; Eukaryota.
DR   InParanoid; A3KPF2; -.
DR   OMA; MHLPNGA; -.
DR   PhylomeDB; A3KPF2; -.
DR   PRO; PR:A3KPF2; -.
DR   Proteomes; UP000006548; Chromosome 5.
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:0035642; F:histone H3R17 methyltransferase activity; IDA:TAIR.
DR   GO; GO:0070611; F:histone H3R2 methyltransferase activity; IDA:TAIR.
DR   GO; GO:0140903; F:histone H3R26 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:0016274; F:protein-arginine N-methyltransferase activity; IDA: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: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   CDD; cd02440; AdoMet_MTases; 1.
DR   FunFam; 2.70.160.11:FF:000002; Probable histone-arginine methyltransferase CARM1; 1.
DR   FunFam; 3.40.50.150:FF:000052; Probable histone-arginine methyltransferase CARM1; 1.
DR   Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR057622; CARM1-like_PH.
DR   InterPro; IPR055135; PRMT_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11006:SF101; HISTONE-ARGININE METHYLTRANSFERASE 1.4-RELATED; 1.
DR   PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR   Pfam; PF25350; PH_PRMT_N; 1.
DR   Pfam; PF06325; PrmA; 1.
DR   Pfam; PF22528; PRMT_C; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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
//