ANM2_XENLA
ID ANM2_XENLA Reviewed; 432 AA.
AC D9IVE5;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Protein arginine N-methyltransferase 2;
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:P55345};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT2;
GN Name=prmt2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CTNNB1.
RX PubMed=20708585; DOI=10.1016/j.devcel.2010.07.007;
RA Blythe S.A., Cha S.-W., Tadjuidje E., Heasman J., Klein P.S.;
RT "beta-Catenin primes organizer gene expression by recruiting a histone H3
RT arginine 8 methyltransferase, Prmt2.";
RL Dev. Cell 19:220-231(2010).
CC -!- FUNCTION: Arginine methyltransferase that methylates the guanidino
CC nitrogens of arginyl residues in proteins such as histones. Involved in
CC growth regulation (By similarity). Involved in embryonic dorsal
CC development. {ECO:0000250, ECO:0000269|PubMed:20708585}.
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 Evidence={ECO:0000250|UniProtKB:P55345};
CC -!- SUBUNIT: Interacts with ctnnb1. {ECO:0000269|PubMed:20708585}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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=ADK11289.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; HM205111; ADK11289.1; ALT_INIT; mRNA.
DR RefSeq; NP_001181877.1; NM_001194948.1.
DR AlphaFoldDB; D9IVE5; -.
DR SMR; D9IVE5; -.
DR GeneID; 100499207; -.
DR KEGG; xla:100499207; -.
DR CTD; 100499207; -.
DR Xenbase; XB-GENE-6486904; prmt2.L.
DR OrthoDB; 840669at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 100499207; Expressed in spleen and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISS:UniProtKB.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0048588; P:developmental cell growth; IMP:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISS:UniProtKB.
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 InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; SH3 domain; Transferase.
FT CHAIN 1..432
FT /note="Protein arginine N-methyltransferase 2"
FT /id="PRO_0000404155"
FT DOMAIN 29..88
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 101..405
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 432 AA; 49525 MW; 55CF6D6414BB7724 CRC64;
MESSSECSSI SDFQDSTEGD DANTLPENLC MREYVVICDY VATDNTQLSL CSGDKVLLLN
AVSQDWWWVN HNGTCGYVPA SHLHDALNEQ EDTEVNDPWQ DEEYYGSYKT LKLHLEMLSD
VPRTMTYQNV ILKNSSSLCG KHILDLGCGT GIISFFCAKF AQPEAVYAVE ASKIAEQTCR
LVEQNGISSL VHVIRQQAEE LDLPTKVDVL VSEWMGTCLL FEFMLESVLQ ARDRWLKEDG
VMWPSTACIH LVPCSAYKEY SNKVLFWDNP YQLDFSLLKP PATKEFFAKP QPDYILQPED
CLSEPCTLFH LNLKTLQVAE LERMNCDFTF LVHTNGLLHG FTAWFSVQFE NLEEQGHLEL
NTGPFSPLTH WKHTLFMLDE PLQVQKRDKI SGSVVFERNS VWRRHMSVTL SWVISRELKM
QKVGCKVFPI WR
