ANM1_XENTR
ID ANM1_XENTR Reviewed; 351 AA.
AC Q28F07; Q6GL90;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Protein arginine N-methyltransferase 1 {ECO:0000312|EMBL:AAH74614.1};
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:Q99873};
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 2 {ECO:0000312|EMBL:CAJ83544.1};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT1;
GN Name=prmt1 {ECO:0000312|EMBL:AAH74614.1};
GN Synonyms=hrmt1l2 {ECO:0000312|EMBL:CAJ83544.1}; ORFNames=TGas059i20.1;
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].
RC TISSUE=Gastrula {ECO:0000312|EMBL:CAJ83544.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud {ECO:0000312|EMBL:AAH74614.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Arginine methyltransferase that methylates (mono and
CC asymmetric dimethylation) the guanidino nitrogens of arginyl residues
CC present in target proteins. Constitutes the main enzyme that mediates
CC monomethylation and asymmetric dimethylation of histone H4 'Arg-4'
CC (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic
CC transcriptional activation. Methylates ilf3 to regulate its DNA-binding
CC activity. Required for neural induction, playing a key role in the
CC control of epidermal versus neural cell fate choice (By similarity).
CC Methylates cirbp to regulate its subcellular location. Acts transiently
CC during metamorphosis as a transcription coactivator, enhancing thyroid
CC hormone (T3) receptor (TR)-mediated transcription by enhancing TR
CC binding to the T3 response element (TRE), and histone modification
CC through recruitment of other coactivators.
CC {ECO:0000250|UniProtKB:Q99873}.
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:Q99873};
CC -!- SUBUNIT: Homodimer. Homooctamer; individual homodimers associates to
CC form a homooctamer and homooligomerization is required for proper
CC localization to the cell membrane. Individual homodimers can associate
CC to form a homohexamer (By similarity). Component of a complex with
CC lsm14a/rap55a. Interacts with cirbp (By similarity).
CC {ECO:0000250|UniProtKB:Q8AV13, ECO:0000250|UniProtKB:Q99873}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9JIF0}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q9JIF0}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JIF0}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99873}.
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=AAH74614.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR762238; CAJ83544.1; -; mRNA.
DR EMBL; BC074614; AAH74614.1; ALT_INIT; mRNA.
DR RefSeq; NP_001005629.2; NM_001005629.2.
DR AlphaFoldDB; Q28F07; -.
DR SMR; Q28F07; -.
DR PaxDb; Q28F07; -.
DR DNASU; 448086; -.
DR Ensembl; ENSXETT00000094658; ENSXETP00000069119; ENSXETG00000002877.
DR GeneID; 448086; -.
DR KEGG; xtr:448086; -.
DR CTD; 3276; -.
DR Xenbase; XB-GENE-484022; prmt1.
DR eggNOG; KOG1499; Eukaryota.
DR InParanoid; Q28F07; -.
DR OrthoDB; 840669at2759; -.
DR Reactome; R-XTR-3214858; RMTs methylate histone arginines.
DR Reactome; R-XTR-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-XTR-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-XTR-9018519; Estrogen-dependent gene expression.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000002877; Expressed in egg cell and 21 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0008170; F:N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008276; F:protein methyltransferase activity; 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:0035241; F:protein-arginine omega-N monomethyltransferase activity; ISS:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0048738; P:cardiac muscle tissue development; ISS:UniProtKB.
DR GO; GO:0043985; P:histone H4-R3 methylation; ISS:UniProtKB.
DR GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
DR GO; GO:0007552; P:metamorphosis; ISS:UniProtKB.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006479; P:protein methylation; ISS:UniProtKB.
DR GO; GO:0031056; P:regulation of histone modification; ISS:UniProtKB.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; 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 PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; Developmental protein; Differentiation;
KW Methyltransferase; Neurogenesis; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..351
FT /note="Protein arginine N-methyltransferase 1"
FT /id="PRO_0000391367"
FT DOMAIN 30..331
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 142
FT /evidence="ECO:0000250"
FT ACT_SITE 151
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 351 AA; 40454 MW; 5C3CC440B3DB4B7C CRC64;
MAEASTCNME VSCTQPESSV KPNAEDMTSK DYYFDSYAHF GIHEEMLKDE VRTLTYRNSM
FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG AKKVIGIECS SISDYAIKIV KANKLDHVVT
IIKGKVEEVE LPVEKVDIII SEWMGYCLFY ESMLNTVIYA RDKWLTPDGL IFPDRATLYV
TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV DPKQLVTNAC LIKEVDIYTV
KVDDLTFTSP FCLQVKRNDY IHALVAYFNI EFTRCHKRTG FSTSPESPYT HWKQTVFYME
DYLTVKTGEE IFGTISMKPN AKNNRDLDFT VDIDFKGQLC ELSCSTDYRM R
