ANM15_ARATH
ID ANM15_ARATH Reviewed; 642 AA.
AC Q8GWT4; Q9M090;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein arginine N-methyltransferase 1.5;
DE Short=AtPMRT15;
DE Short=AtPMRT5;
DE EC=2.1.1.319;
DE AltName: Full=Shk1 kinase-binding protein 1 homolog;
GN Name=PMRT15; Synonyms=PMRT5, SKB1; OrderedLocusNames=At4g31120;
GN ORFNames=F6E21.40;
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] (ISOFORM 2).
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 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 [5]
RP FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17363895; DOI=10.1038/sj.emboj.7601647;
RA Wang X., Zhang Y., Ma Q., Zhang Z., Xue Y., Bao S., Chong K.;
RT "SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering
RT time in Arabidopsis.";
RL EMBO J. 26:1934-1941(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=20962777; DOI=10.1038/nature09470;
RA Sanchez S.E., Petrillo E., Beckwith E.J., Zhang X., Rugnone M.L.,
RA Hernando C.E., Cuevas J.C., Godoy Herz M.A., Depetris-Chauvin A.,
RA Simpson C.G., Brown J.W., Cerdan P.D., Borevitz J.O., Mas P., Ceriani M.F.,
RA Kornblihtt A.R., Yanovsky M.J.;
RT "A methyl transferase links the circadian clock to the regulation of
RT alternative splicing.";
RL Nature 468:112-116(2010).
CC -!- FUNCTION: Methylates arginine residues of myelin basic protein (MBP) in
CC vitro. Methylates symmetrically histone H4 of the FLC chromatin to form
CC H4R3me2s, which in turn suppresses FLC expression to induce flowering.
CC Regulates alternative splicing by methylating spliceosomal proteins.
CC Involved in the post-transcriptional regulation of the circadian clock.
CC {ECO:0000269|PubMed:17363895, ECO:0000269|PubMed:20962777}.
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: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8GWT4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GWT4-2; Sequence=VSP_027572, VSP_027573;
CC Name=3;
CC IsoId=Q8GWT4-3; Sequence=VSP_027574;
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers, roots and siliques,
CC lower expression in stems and mature leaves (at protein level).
CC Abundant in shoot apex, young leaves and leaf primordia, floral and
CC inflorescence meristems, gynoecium, stamens, sepals and young siliques,
CC but not in older leaves, petals and vascular tissues.
CC {ECO:0000269|PubMed:17363895}.
CC -!- DEVELOPMENTAL STAGE: High levels from 5 to 20 days after germination
CC (at protein level). {ECO:0000269|PubMed:17363895}.
CC -!- INDUCTION: Circadian-regulation. {ECO:0000269|PubMed:20962777}.
CC -!- DISRUPTION PHENOTYPE: Plants are late-flowering. Increased alternative
CC splicing of several genes, including APRR9.
CC {ECO:0000269|PubMed:17363895, ECO:0000269|PubMed:20962777}.
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=CAB79830.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL161578; CAB79830.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85860.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85861.1; -; Genomic_DNA.
DR EMBL; BT005907; AAO64842.1; -; mRNA.
DR EMBL; AK118648; BAC43244.1; -; mRNA.
DR PIR; T10666; T10666.
DR RefSeq; NP_194841.2; NM_119262.6. [Q8GWT4-1]
DR RefSeq; NP_974647.1; NM_202918.2. [Q8GWT4-3]
DR AlphaFoldDB; Q8GWT4; -.
DR SMR; Q8GWT4; -.
DR BioGRID; 14527; 6.
DR STRING; 3702.AT4G31120.1; -.
DR PaxDb; Q8GWT4; -.
DR PRIDE; Q8GWT4; -.
DR ProteomicsDB; 245055; -. [Q8GWT4-1]
DR EnsemblPlants; AT4G31120.1; AT4G31120.1; AT4G31120. [Q8GWT4-1]
DR EnsemblPlants; AT4G31120.2; AT4G31120.2; AT4G31120. [Q8GWT4-3]
DR GeneID; 829240; -.
DR Gramene; AT4G31120.1; AT4G31120.1; AT4G31120. [Q8GWT4-1]
DR Gramene; AT4G31120.2; AT4G31120.2; AT4G31120. [Q8GWT4-3]
DR KEGG; ath:AT4G31120; -.
DR Araport; AT4G31120; -.
DR TAIR; locus:2126276; AT4G31120.
DR eggNOG; KOG0822; Eukaryota.
DR HOGENOM; CLU_010247_3_0_1; -.
DR InParanoid; Q8GWT4; -.
DR OMA; IKYAWYE; -.
DR OrthoDB; 475852at2759; -.
DR PhylomeDB; Q8GWT4; -.
DR BRENDA; 2.1.1.320; 399.
DR PRO; PR:Q8GWT4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GWT4; baseline and differential.
DR Genevisible; Q8GWT4; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008276; F:protein 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:0034969; P:histone arginine methylation; IBA:GO_Central.
DR GO; GO:0043985; P:histone H4-R3 methylation; IMP:TAIR.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; IEA:InterPro.
DR GO; GO:0010220; P:positive regulation of vernalization response; IMP:TAIR.
DR GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR007857; Arg_MeTrfase_PRMT5.
DR InterPro; IPR035075; PRMT5.
DR InterPro; IPR035248; PRMT5_C.
DR InterPro; IPR035247; PRMT5_TIM.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10738; PTHR10738; 1.
DR Pfam; PF05185; PRMT5; 1.
DR Pfam; PF17286; PRMT5_C; 1.
DR Pfam; PF17285; PRMT5_TIM; 1.
DR PIRSF; PIRSF015894; Skb1_MeTrfase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Cytoplasm; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..642
FT /note="Protein arginine N-methyltransferase 1.5"
FT /id="PRO_0000293993"
FT DOMAIN 314..620
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 442
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 451
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 339..340
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 426..427
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 451
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT VAR_SEQ 492..510
FT /note="KAHKDLAHFETAYVVKLHS -> RLIKILRTLKLLMLSSCIV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_027572"
FT VAR_SEQ 511..642
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_027573"
FT VAR_SEQ 585..642
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_027574"
FT CONFLICT 10
FT /note="E -> G (in Ref. 3; AAO64842/BAC43244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 71870 MW; F9F85054688D1B01 CRC64;
MPLGERGGWE RTESRYCGVE TDFSNDVTHL LNFNISTGGF DYVLAPLVDP SYRPSLVEGN
GVDTQVLPVC GSDLVLSPSQ WSSHVVGKIS SWIDLDSEDE VLRMDSETTL KQEIAWATHL
SLQACLLPTP KGKSCANYAR CVNQILQGLT TLQLWLRVPL VKSEGDSMDD TSEGLNDSWE
LWNSFRLLCE HDSKLSVALD VLSTLPSETS LGRWMGESVR AAILSTDAFL TNARGYPCLS
KRHQKLIAGF FDHAAQVVIC GKPVHNLQKP LDSSSEGTEK NPLRIYLDYV AYLFQKMESL
SEQERIELGY RDFLQAPLQP LMDNLEAQTY ETFERDSVKY IQYQRAVEKA LVDRVPDEKA
SELTTVLMVV GAGRGPLVRA SLQAAEETDR KLKVYAVEKN PNAVVTLHNL VKMEGWEDVV
TIISCDMRFW NAPEQADILV SELLGSFGDN ELSPECLDGA QRFLKPDGIS IPSSYTSFIQ
PITASKLYND VKAHKDLAHF ETAYVVKLHS VAKLAPSQSV FTFTHPNFST KVNNQRYKKL
QFSLPSDAGS ALVHGFAGYF DSVLYKDVHL GIEPTTATPN MFSWFPIFFP LRKPVEVHPD
TPLEVHFWRC CGSSKVWYEW SVSSPTPSPM HNTNGRSYWV GL
