ANM1A_XENLA
ID ANM1A_XENLA Reviewed; 369 AA.
AC Q8AV13; Q7SY97; Q7ZY05;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein arginine N-methyltransferase 1-A {ECO:0000312|EMBL:BAC53990.1};
DE Short=xPRMT1 {ECO:0000312|EMBL:BAC53990.1};
DE EC=2.1.1.319 {ECO:0000269|PubMed:12466543};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT1-A;
GN Name=prmt1-a; Synonyms=prmt1 {ECO:0000303|PubMed:12466543};
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] {ECO:0000305, ECO:0000312|EMBL:BAC53990.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP CIRBP.
RC TISSUE=Oocyte {ECO:0000269|PubMed:12466543};
RX PubMed=12466543; DOI=10.1093/nar/gkf638;
RA Aoki K., Ishii Y., Matsumoto K., Tsujimoto M.;
RT "Methylation of Xenopus CIRP2 regulates its arginine- and glycine-rich
RT region-mediated nucleocytoplasmic distribution.";
RL Nucleic Acids Res. 30:5182-5192(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH44033.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tadpole {ECO:0000312|EMBL:AAH54955.1}, and
RC Tail bud {ECO:0000312|EMBL:AAH44033.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=16686947; DOI=10.1186/1471-2164-7-113;
RA Vallee M., Robert C., Methot S., Palin M.F., Sirard M.A.;
RT "Cross-species hybridizations on a multi-species cDNA microarray to
RT identify evolutionarily conserved genes expressed in oocytes.";
RL BMC Genomics 7:113-113(2006).
RN [4] {ECO:0000305}
RP IDENTIFICATION IN A COMPLEX WITH LSM14A.
RX PubMed=17074753; DOI=10.1074/jbc.m609059200;
RA Tanaka K.J., Ogawa K., Takagi M., Imamoto N., Matsumoto K., Tsujimoto M.;
RT "RAP55, a cytoplasmic mRNP component, represses translation in Xenopus
RT oocytes.";
RL J. Biol. Chem. 281:40096-40106(2006).
RN [5] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=19047371; DOI=10.1128/mcb.00827-08;
RA Matsuda H., Paul B.D., Choi C.Y., Hasebe T., Shi Y.B.;
RT "Novel functions of protein arginine methyltransferase 1 in thyroid hormone
RT receptor-mediated transcription and in the regulation of metamorphic rate
RT in Xenopus laevis.";
RL Mol. Cell. Biol. 29:745-757(2009).
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 (By similarity). Methylates cirbp to
CC regulate its subcellular location (PubMed:12466543). 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 (PubMed:19047371).
CC {ECO:0000250|UniProtKB:Q99873, ECO:0000269|PubMed:12466543,
CC ECO:0000269|PubMed:19047371}.
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:0000269|PubMed:12466543};
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. {ECO:0000250|UniProtKB:Q99873,
CC ECO:0000269|PubMed:12466543, ECO:0000269|PubMed:17074753}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:12466543};
CC IsoId=Q8AV13-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8AV13-2; Sequence=VSP_053193;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed in oocytes (at protein level). Up-regulated during
CC metamorphosis, peaking at stage 62 before dramatically reducing by the
CC end of metamorphosis (stage 66). {ECO:0000269|PubMed:16686947,
CC ECO:0000269|PubMed:19047371}.
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=AAH44033.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH54955.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB085173; BAC53990.1; -; mRNA.
DR EMBL; BC044033; AAH44033.1; ALT_INIT; mRNA.
DR EMBL; BC054955; AAH54955.1; ALT_INIT; mRNA.
DR RefSeq; NP_001083793.1; NM_001090324.1. [Q8AV13-1]
DR AlphaFoldDB; Q8AV13; -.
DR SMR; Q8AV13; -.
DR DNASU; 399121; -.
DR GeneID; 399121; -.
DR KEGG; xla:399121; -.
DR CTD; 399121; -.
DR Xenbase; XB-GENE-6254417; prmt1.S.
DR OMA; TTDRMEV; -.
DR OrthoDB; 840669at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 399121; Expressed in gastrula and 19 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:0032991; C:protein-containing complex; IPI: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; IDA:UniProtKB.
DR GO; GO:0008276; F:protein 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; IMP:UniProtKB.
DR GO; GO:0048738; P:cardiac muscle tissue development; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043985; P:histone H4-R3 methylation; ISS:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IMP:UniProtKB.
DR GO; GO:0007552; P:metamorphosis; IMP:UniProtKB.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006479; P:protein methylation; IDA:UniProtKB.
DR GO; GO:0031056; P:regulation of histone modification; IMP: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 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; Methyltransferase; Neurogenesis; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..369
FT /note="Protein arginine N-methyltransferase 1-A"
FT /id="PRO_0000391365"
FT DOMAIN 48..369
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 160
FT /evidence="ECO:0000250"
FT ACT_SITE 169
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT VAR_SEQ 11..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_053193"
SQ SEQUENCE 369 AA; 42325 MW; 820402CA2A28DF11 CRC64;
MAEATTCNME NFVAKLANGM SLRTPIEDVN SAPPEGGVKT NAEDMTSKDY YFDSYAHFGI
HEEMLKDEVR TLTYRNSMFH NRHLFKDKVV LDVGSGTGIL CMFAAKAGAK KVIGIECSSI
SDYAIKIVKA NKLDHVVTII KGKVEEVELP VEKVDIIISE WMGYCLFYES MLNTVIYARD
KWLTPDGLIF PDRATLYITA IEDRQYKDYK IHWWENVYGF DMSCIKDVAI KEPLVDVVDP
KQLVSNACLI KEVDIYTVKV DDLSFTSPFC LQVKRNDYIH ALVAYFNIEF TRCHKRTGFS
TSPESPYTHW KQTVFYMEDY LTVKTGEEIF GTIGMKPNAK NNRDLDFTFD IDFKGQLCEL
SCSTDYRMR
