ID   ANM2_XENTR              Reviewed;         433 AA.
AC   B3DLB3; Q08CW9;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=N6; TISSUE=Intestine, and Oviduct;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Arginine methyltransferase that methylates the guanidino
CC       nitrogens of arginyl residues in proteins such as histones. Involved in
CC       growth regulation. Involved in embryonic dorsal development.
CC       {ECO:0000250}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B3DLB3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B3DLB3-2; Sequence=VSP_040525;
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; BC124052; AAI24053.1; -; mRNA.
DR   EMBL; BC167381; AAI67381.1; -; mRNA.
DR   RefSeq; NP_001072706.2; NM_001079238.2.
DR   AlphaFoldDB; B3DLB3; -.
DR   SMR; B3DLB3; -.
DR   STRING; 8364.ENSXETP00000062304; -.
DR   PaxDb; B3DLB3; -.
DR   DNASU; 780163; -.
DR   GeneID; 780163; -.
DR   KEGG; xtr:780163; -.
DR   CTD; 3275; -.
DR   Xenbase; XB-GENE-980934; prmt2.
DR   eggNOG; KOG1499; Eukaryota.
DR   InParanoid; B3DLB3; -.
DR   OrthoDB; 840669at2759; -.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0030331; F:nuclear estrogen receptor binding; ISS:UniProtKB.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR   GO; GO:0048588; P:developmental cell growth; ISS:UniProtKB.
DR   GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS: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; PF00018; SH3_1; 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   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; SH3 domain; Transferase.
FT   CHAIN           1..433
FT                   /note="Protein arginine N-methyltransferase 2"
FT                   /id="PRO_0000404156"
FT   DOMAIN          30..89
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          102..416
FT                   /note="SAM-dependent MTase PRMT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        214
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         324..433
FT                   /note="RMNSDFTFFVHTDGLLHGFTAWFSVQFQNLEEQGQLELNTGPFSPLTHWKHT
FT                   LFMLDEPLQVQKGDKISGSVVFQRNSVWRRHMSVTLSWVINGKLTMQNVSQQWQAILA
FT                   -> VRAILSNLH (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_040525"
SQ   SEQUENCE   433 AA;  49519 MW;  54B827FE81323C89 CRC64;
     MSTSGCSSEK SDFQDSTEGE EEEDTQSENL CMREYVVIRD YMAADATQLS LCFGDKVLLL
     SAVTQDWWWV KHNGICGYVP ASYLHDALND QEDTEVDDPW QDEEYYGSYK TLKLHLEMLS
     DVPRTTAYKE VILRNSSSLC GKHILDLGCG TGIISFFCAK LAQPEAVYAV EASEIAEQTR
     RLVKQNGISN LVHVIRQRAE ELQLPTKVDI LVSEWMGTCL LFEFMLESVL QARDRWLKED
     GVMWPSTACI HLVPCSASKE YANKVLFWDN PYQLDFSLLK PLAAKEFFAR PKPDYVLQPE
     DCLSEPCILL HLNLKTLQLA ELERMNSDFT FFVHTDGLLH GFTAWFSVQF QNLEEQGQLE
     LNTGPFSPLT HWKHTLFMLD EPLQVQKGDK ISGSVVFQRN SVWRRHMSVT LSWVINGKLT
     MQNVSQQWQA ILA