ANM1B_XENLA
ID ANM1B_XENLA Reviewed; 351 AA.
AC Q6VRB0; Q3KQC7; Q6IP49;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protein arginine N-methyltransferase 1-B {ECO:0000303|PubMed:16214893};
DE Short=xPRMT1b {ECO:0000303|PubMed:16214893};
DE EC=2.1.1.319 {ECO:0000269|PubMed:18636753};
DE AltName: Full=Arginine methyltransferase 1b {ECO:0000312|EMBL:AAQ65243.1};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT1-B;
GN Name=prmt1-b; Synonyms=prmt1, prmt1b {ECO:0000303|PubMed:16214893};
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:AAQ65243.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC TISSUE=Gastrula {ECO:0000269|PubMed:16214893};
RX PubMed=16214893; DOI=10.1073/pnas.0502483102;
RA Batut J., Vandel L., Leclerc C., Daguzan C., Moreau M., Neant I.;
RT "The Ca2+-induced methyltransferase xPRMT1b controls neural fate in
RT amphibian embryo.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15128-15133(2005).
RN [2] {ECO:0000312|EMBL:AAI06276.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula {ECO:0000312|EMBL:AAI06276.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18636753; DOI=10.1021/bi7008486;
RA Cazanove O., Batut J., Scarlett G., Mumford K., Elgar S., Thresh S.,
RA Neant I., Moreau M., Guille M.;
RT "Methylation of Xilf3 by Xprmt1b alters its DNA, but not RNA, binding
RT activity.";
RL Biochemistry 47:8350-8357(2008).
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 ilf3 to regulate
CC its DNA-binding activity (PubMed:18636753). Required for neural
CC induction, playing a key role in the control of epidermal versus neural
CC cell fate choice (PubMed:16214893). {ECO:0000250|UniProtKB:Q99873,
CC ECO:0000269|PubMed:16214893, ECO:0000269|PubMed:18636753}.
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: 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 -!- TISSUE SPECIFICITY: From the onset of gastrulation, expressed in dorsal
CC mesoderm, and in dorsal and ventral ectoderm. At the neurula and tail
CC bud stages, expression is restricted to the neuroectoderm, with highest
CC expression in the anterior neural plate. {ECO:0000269|PubMed:16214893}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed throughout all embryonic stages.
CC {ECO:0000269|PubMed:16214893}.
CC -!- INDUCTION: By Ca(2+). {ECO:0000269|PubMed:16214893}.
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=AAH72069.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI06276.1; Type=Erroneous initiation; 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; AY330768; AAQ65243.1; -; mRNA.
DR EMBL; BC072069; AAH72069.1; ALT_INIT; mRNA.
DR EMBL; BC106275; AAI06276.1; ALT_INIT; mRNA.
DR RefSeq; NP_001082771.1; NM_001089302.1.
DR AlphaFoldDB; Q6VRB0; -.
DR SMR; Q6VRB0; -.
DR DNASU; 398716; -.
DR GeneID; 398716; -.
DR KEGG; xla:398716; -.
DR CTD; 398716; -.
DR Xenbase; XB-GENE-865039; prmt1.L.
DR OMA; DADETMC; -.
DR OrthoDB; 840669at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 398716; 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: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:0016274; F:protein-arginine N-methyltransferase activity; IDA: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: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; IDA:UniProtKB.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; 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 1: Evidence at protein 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-B"
FT /id="PRO_0000391366"
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"
FT CONFLICT 14
FT /note="A -> P (in Ref. 2; AAI06276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 40437 MW; 885A08E03B04EC9A CRC64;
MAEAKTCNME VSCALPEGSV KPNAEDMTSK DYYFDSYAHF GIHEEMLKDE VRTLTYRNSM
FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG AKKVIGIECS SISDYAIKIV KANKLDHVVT
IIKGKVEEVE LPVEKVDIII SEWMGYCLFY ESMLNTVIYA RDKWLNPDGL IFPDRATLYV
TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV DPKQLVSNAC LIKEVDIYTV
KVDDLTFTSP FCLQVKRNDY IHAMVAYFNI EFTRCHKRTG FSTSPESPYT HWKQTVFYME
DYLTVKTGEE IFGTISMKPN AKNNRDLDFT VDIDFKGQLC ELSCSTDYRM R
