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   16-DEC-2008, entry version 44.
DE   RecName: Full=Probable protein arginine N-methyltransferase 1.2;
DE            EC=2.1.1.-;
GN   Name=PRMT1.2; OrderedLocusNames=At2g19670; ORFNames=F6F22.30;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083487; 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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [3]
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.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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
RT   their pharmacological and therapeutic potential.";
RL   Pharmacol. Ther. 113:50-87(2007).
CC   -!- FUNCTION: Methylates (mono and asymmetric dimethylation) the
CC       guanidino nitrogens of arginyl residues present in a glycine and
CC       arginine-rich domain (can methylate histones) (By similarity).
CC   -!- INTERACTION:
CC       Q94AH9:FIB2; NbExp=1; IntAct=EBI-1382526, EBI-1382666;
CC       P62805:HIST1H4A (xeno); NbExp=1; IntAct=EBI-1382526, EBI-302023;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the protein arginine N-methyltransferase
CC       family.
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DR   EMBL; AC005169; AAC62148.1; -; Genomic_DNA.
DR   EMBL; BT006491; AAP21299.1; -; mRNA.
DR   EMBL; AK227449; BAE99452.1; -; mRNA.
DR   PIR; F84579; F84579.
DR   RefSeq; NP_179557.1; -.
DR   UniGene; At.39807; -.
DR   HSSP; Q63009; 1ORH.
DR   IntAct; O82210; 2.
DR   PRIDE; O82210; -.
DR   GeneID; 816486; -.
DR   GenomeReviews; CT485783_GR; AT2G19670.
DR   KEGG; ath:AT2G19670; -.
DR   NMPDR; fig|3702.1.peg.8961; -.
DR   TAIR; At2g19670; -.
DR   ArrayExpress; O82210; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR013217; Methyltransf_12.
DR   Pfam; PF08242; Methyltransf_12; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Methyltransferase; Nucleus; Transferase.
FT   CHAIN         1    366       Probable protein arginine N-
FT                                methyltransferase 1.2.
FT                                /FTId=PRO_0000293987.
FT   COMPBIAS      6      9       Poly-Asn.
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
//