ID   ANM12_ARATH             Reviewed;         366 AA.
AC   O82210;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Probable protein arginine N-methyltransferase 1.2;
DE            Short=AtPRMT12;
DE            EC=2.1.1.-;
GN   Name=PRMT12; Synonyms=PRMT1.2, PRMT1A; OrderedLocusNames=At2g19670;
GN   ORFNames=F6F22.30;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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;
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].
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   [5]
RP   FUNCTION, INTERACTION WITH PRMT11 AND FIB2, AND SUBCELLULAR LOCATION.
RX   PubMed=17666011; DOI=10.1042/bj20070786;
RA   Yan D., Zhang Y., Niu L., Yuan Y., Cao X.;
RT   "Identification and characterization of two closely related histone H4
RT   arginine 3 methyltransferases in Arabidopsis thaliana.";
RL   Biochem. J. 408:113-121(2007).
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).
CC   -!- FUNCTION: Methylates (mono and asymmetric dimethylation) the guanidino
CC       nitrogens of arginyl residues present in a glycine and arginine-rich
CC       domain. Type I arginine methyltransferase active on both histones and
CC       non-histone proteins. Mediates the methylation of MED36A.
CC       {ECO:0000269|PubMed:17666011}.
CC   -!- SUBUNIT: Interacts with FIB2 and PRMT11. {ECO:0000269|PubMed:17666011}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17666011}. Cytoplasm
CC       {ECO:0000269|PubMed:17666011}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Protein arginine N-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR   EMBL; AC005169; AAC62148.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06910.1; -; Genomic_DNA.
DR   EMBL; BT006491; AAP21299.1; -; mRNA.
DR   EMBL; AK227449; BAE99452.1; -; mRNA.
DR   PIR; F84579; F84579.
DR   RefSeq; NP_179557.1; NM_127525.5.
DR   AlphaFoldDB; O82210; -.
DR   SMR; O82210; -.
DR   BioGRID; 1841; 2.
DR   IntAct; O82210; 2.
DR   STRING; 3702.AT2G19670.1; -.
DR   PaxDb; O82210; -.
DR   PRIDE; O82210; -.
DR   ProteomicsDB; 245054; -.
DR   EnsemblPlants; AT2G19670.1; AT2G19670.1; AT2G19670.
DR   GeneID; 816486; -.
DR   Gramene; AT2G19670.1; AT2G19670.1; AT2G19670.
DR   KEGG; ath:AT2G19670; -.
DR   Araport; AT2G19670; -.
DR   TAIR; locus:2051995; AT2G19670.
DR   eggNOG; KOG1499; Eukaryota.
DR   HOGENOM; CLU_017375_1_2_1; -.
DR   InParanoid; O82210; -.
DR   OMA; CHNSIAS; -.
DR   OrthoDB; 840669at2759; -.
DR   PhylomeDB; O82210; -.
DR   PRO; PR:O82210; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O82210; baseline and differential.
DR   Genevisible; O82210; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11006; PTHR11006; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Cytoplasm; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..366
FT                   /note="Probable protein arginine N-methyltransferase 1.2"
FT                   /id="PRO_0000293987"
FT   DOMAIN          45..347
FT                   /note="SAM-dependent MTase PRMT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   366 AA;  41172 MW;  9C31A654BDCC4C70 CRC64;
     MTSTENNNNG SDETQTTKLH FEDADESMHD GDDNNADVAD DITSADYYFD SYSHFGIHEE
     MLKDVVRTKS YQDVIYKNKF LIKDKIVLDV GAGTGILSLF CAKAGAAHVY AVECSQMADT
     AKEIVKSNGF SDVITVLKGK IEEIELPVPK VDVIISEWMG YFLLYENMLD TVLYARNKWL
     VDGGIVLPDK ASLYVTAIED AHYKDDKVEF WDDVYGFDMS CIKRRAITEP LVDTVDGNQI
     VTDSKLLKTM DISKMAAGDA SFTAPFKLVA QRNDHIHALV AYFDVSFTMC HKKMGFSTGP
     KSRATHWKQT VLYLEDVLTI CEGETITGSM TIAQNKKNPR DVDIKLSYSL NGQHCNISRT
     HFYKMR