ANM11_ARATH
ID ANM11_ARATH Reviewed; 390 AA.
AC Q9SU94; O81813; Q8VZP0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein arginine N-methyltransferase 1.1;
DE Short=AtPRMT11;
DE EC=2.1.1.319;
DE AltName: Full=Arginine methyltransferase pam1;
DE AltName: Full=Histone-arginine N-methyltransferase PRMT11;
GN Name=PRMT11; Synonyms=PAM1, PRMT1.1, PRMT1B; OrderedLocusNames=At4g29510;
GN ORFNames=T16L4.20;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-376.
RC STRAIN=cv. Columbia;
RA Salchert K., Breuer F., Koncz C.;
RT "Identification and isolation of the first protein arginine
RT methyltransferase from Arabidopsis thaliana.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, INTERACTION WITH PRMT12 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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MBD7, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=17711414; DOI=10.1111/j.1365-313x.2007.03238.x;
RA Scebba F., De Bastiani M., Bernacchia G., Andreucci A., Galli A., Pitto L.;
RT "PRMT11: a new Arabidopsis MBD7 protein partner with arginine
RT methyltransferase activity.";
RL Plant J. 52:210-222(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. Required for leaves and flowers development.
CC Mediates the methylation of MBD7 and MED36A.
CC {ECO:0000269|PubMed:17666011, ECO:0000269|PubMed:17711414}.
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 -!- SUBUNIT: Interacts with PRMT12, MBD7 and FIB2.
CC {ECO:0000269|PubMed:17666011, ECO:0000269|PubMed:17711414}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Excluded from nucleolus.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of proteins with asymmetrically
CC dimethylated arginines. Altered leaf morphology and development (curled
CC leaves), multiple rosettes with an increased number of leaves, delayed
CC flowering, disturbed inflorescence morphology, increased sterility.
CC {ECO:0000269|PubMed:17711414}.
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; AL079344; CAB45311.1; -; Genomic_DNA.
DR EMBL; AL161575; CAB79709.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85638.1; -; Genomic_DNA.
DR EMBL; AY150407; AAN12952.1; -; mRNA.
DR EMBL; AY063970; AAL36326.1; -; mRNA.
DR EMBL; AY087817; AAM65371.1; -; mRNA.
DR EMBL; AJ007582; CAA07570.1; -; mRNA.
DR PIR; T09914; T09914.
DR PIR; T52248; T52248.
DR RefSeq; NP_194680.1; NM_119096.3.
DR AlphaFoldDB; Q9SU94; -.
DR SMR; Q9SU94; -.
DR BioGRID; 14359; 9.
DR IntAct; Q9SU94; 4.
DR STRING; 3702.AT4G29510.1; -.
DR iPTMnet; Q9SU94; -.
DR PaxDb; Q9SU94; -.
DR PRIDE; Q9SU94; -.
DR ProteomicsDB; 244431; -.
DR EnsemblPlants; AT4G29510.1; AT4G29510.1; AT4G29510.
DR GeneID; 829072; -.
DR Gramene; AT4G29510.1; AT4G29510.1; AT4G29510.
DR KEGG; ath:AT4G29510; -.
DR Araport; AT4G29510; -.
DR TAIR; locus:2134328; AT4G29510.
DR eggNOG; KOG1499; Eukaryota.
DR HOGENOM; CLU_017375_1_2_1; -.
DR InParanoid; Q9SU94; -.
DR OMA; MEFTKCH; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q9SU94; -.
DR PRO; PR:Q9SU94; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU94; baseline and differential.
DR Genevisible; Q9SU94; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:TAIR.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:UniProtKB-EC.
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; 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 Chromatin regulator; Cytoplasm; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..390
FT /note="Protein arginine N-methyltransferase 1.1"
FT /id="PRO_0000293986"
FT DOMAIN 69..390
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /evidence="ECO:0000250"
FT ACT_SITE 190
FT /evidence="ECO:0000250"
FT CONFLICT 260
FT /note="D -> G (in Ref. 3; AAL36326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43894 MW; 9BE43387CD7AE0B2 CRC64;
MTKNSNHDEN EFISFEPNQN TKIRFEDADE DEVAEGSGVA GEETPQDESM FDAGESADTA
EVTDDTTSAD YYFDSYSHFG IHEEMLKDVV RTKTYQNVIY QNKFLIKDKI VLDVGAGTGI
LSLFCAKAGA AHVYAVECSQ MADMAKEIVK ANGFSDVITV LKGKIEEIEL PTPKVDVIIS
EWMGYFLLFE NMLDSVLYAR DKWLVEGGVV LPDKASLHLT AIEDSEYKED KIEFWNSVYG
FDMSCIKKKA MMEPLVDTVD QNQIVTDSRL LKTMDISKMS SGDASFTAPF KLVAQRNDYI
HALVAYFDVS FTMCHKLLGF STGPKSRATH WKQTVLYLED VLTICEGETI TGTMSVSPNK
KNPRDIDIKL SYSLNGQHCK ISRTQHYKMR
