ANM10_ARATH
ID ANM10_ARATH Reviewed; 383 AA.
AC Q9MAT5; Q8W552; Q93Z15;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein arginine N-methyltransferase PRMT10;
DE EC=2.1.1.319;
GN Name=PRMT10; Synonyms=PRMT4.2; OrderedLocusNames=At1g04870;
GN ORFNames=F13M7.14, F13M7_12;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORMS 1 AND 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 X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 11-383 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, SUBUNIT, AND MUTAGENESIS OF
RP 203-TRP--GLY-225.
RX PubMed=21986201; DOI=10.1016/j.jmb.2011.09.040;
RA Cheng Y., Frazier M., Lu F., Cao X., Redinbo M.R.;
RT "Crystal structure of the plant epigenetic protein arginine
RT methyltransferase 10.";
RL J. Mol. Biol. 414:106-122(2011).
CC -!- FUNCTION: Methylates (mono and asymmetric dimethylation) the guanidino
CC nitrogens of arginyl residues in some proteins. Essential for
CC regulating flowering time. {ECO:0000269|PubMed:21986201}.
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: Ring-like homodimer. {ECO:0000269|PubMed:21986201}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9MAT5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9MAT5-2; Sequence=VSP_027462;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
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; AC004809; AAF40450.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27753.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27754.1; -; Genomic_DNA.
DR EMBL; AF436837; AAL32019.1; -; mRNA.
DR EMBL; AY058846; AAL24234.1; -; mRNA.
DR EMBL; AY132011; AAM91044.1; -; mRNA.
DR PIR; A86182; A86182.
DR RefSeq; NP_563720.1; NM_100365.4. [Q9MAT5-1]
DR RefSeq; NP_849591.1; NM_179260.1. [Q9MAT5-2]
DR PDB; 3R0Q; X-ray; 2.61 A; A/C/E/G=11-383.
DR PDBsum; 3R0Q; -.
DR AlphaFoldDB; Q9MAT5; -.
DR SMR; Q9MAT5; -.
DR BioGRID; 24628; 4.
DR IntAct; Q9MAT5; 4.
DR MINT; Q9MAT5; -.
DR STRING; 3702.AT1G04870.2; -.
DR MetOSite; Q9MAT5; -.
DR PaxDb; Q9MAT5; -.
DR PRIDE; Q9MAT5; -.
DR ProteomicsDB; 244430; -. [Q9MAT5-1]
DR EnsemblPlants; AT1G04870.1; AT1G04870.1; AT1G04870. [Q9MAT5-2]
DR EnsemblPlants; AT1G04870.2; AT1G04870.2; AT1G04870. [Q9MAT5-1]
DR GeneID; 839393; -.
DR Gramene; AT1G04870.1; AT1G04870.1; AT1G04870. [Q9MAT5-2]
DR Gramene; AT1G04870.2; AT1G04870.2; AT1G04870. [Q9MAT5-1]
DR KEGG; ath:AT1G04870; -.
DR Araport; AT1G04870; -.
DR TAIR; locus:2010607; AT1G04870.
DR eggNOG; KOG1499; Eukaryota.
DR HOGENOM; CLU_017375_1_2_1; -.
DR InParanoid; Q9MAT5; -.
DR OMA; MWVAPIR; -.
DR PhylomeDB; Q9MAT5; -.
DR BRENDA; 2.1.1.319; 399.
DR PRO; PR:Q9MAT5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAT5; baseline and differential.
DR Genevisible; Q9MAT5; AT.
DR GO; GO:0016277; F:[myelin basic protein]-arginine N-methyltransferase activity; IDA:TAIR.
DR GO; GO:0008469; F:histone-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:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
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 3D-structure; Alternative splicing; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..383
FT /note="Protein arginine N-methyltransferase PRMT10"
FT /id="PRO_0000294008"
FT DOMAIN 29..360
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..230
FT /note="Dimerization arm"
FT ACT_SITE 143
FT /evidence="ECO:0000250"
FT ACT_SITE 152
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 54
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_027462"
FT MUTAGEN 203..225
FT /note="Missing: No dimerization and no observable activity
FT toward histones H2A and H4."
FT /evidence="ECO:0000269|PubMed:21986201"
FT CONFLICT 362
FT /note="N -> Y (in Ref. 3; AAL32019)"
FT /evidence="ECO:0000305"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:3R0Q"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:3R0Q"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:3R0Q"
FT TURN 64..71
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3R0Q"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:3R0Q"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:3R0Q"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:3R0Q"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3R0Q"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3R0Q"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:3R0Q"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 166..184
FT /evidence="ECO:0007829|PDB:3R0Q"
FT HELIX 188..212
FT /evidence="ECO:0007829|PDB:3R0Q"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3R0Q"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3R0Q"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:3R0Q"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:3R0Q"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 268..277
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 283..299
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 302..311
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 324..335
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 340..349
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 356..366
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3R0Q"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:3R0Q"
SQ SEQUENCE 383 AA; 43130 MW; 9EF68DF7EE30B3F5 CRC64;
MRSSQNGGAM GGRAAGTGGG GPSAPVDKEV DYAQYFCTYS FLYHQKDMLS DRVRMDAYFN
AVFQNKHHFE GKTVLDVGTG SGILAIWSAQ AGARKVYAVE ATKMADHARA LVKANNLDHI
VEVIEGSVED ISLPEKVDVI ISEWMGYFLL RESMFDSVIS ARDRWLKPTG VMYPSHARMW
LAPIKSNIAD RKRNDFDGAM ADWHNFSDEI KSYYGVDMGV LTKPFAEEQE KYYIQTAMWN
DLNPQQIIGT PTIVKEMDCL TASVSEIEEV RSNVTSVINM EHTRLCGFGG WFDVQFSGRK
EDPAQQEIEL TTAPSEQHCT HWGQQVFIMS NPINVEEGDN LNLGLLMSRS KENHRLMEIE
LNCEIKEASG NPKESFKKTY FIE
