ANM1_CAEEL
ID ANM1_CAEEL Reviewed; 348 AA.
AC Q9U2X0;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein arginine N-methyltransferase 1 {ECO:0000312|WormBase:Y113G7B.17};
DE EC=2.1.1.319 {ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:24140420, ECO:0000305|PubMed:27994012, ECO:0000305|PubMed:28158808};
GN Name=prmt-1 {ECO:0000303|PubMed:21531333, ECO:0000312|WormBase:Y113G7B.17};
GN Synonyms=epg-11 {ECO:0000303|PubMed:24140420,
GN ECO:0000312|WormBase:Y113G7B.17};
GN ORFNames=Y113G7B.17 {ECO:0000312|WormBase:Y113G7B.17};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH DAF-16, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-70.
RX PubMed=21531333; DOI=10.1016/j.cmet.2011.03.017;
RA Takahashi Y., Daitoku H., Hirota K., Tamiya H., Yokoyama A., Kako K.,
RA Nagashima Y., Nakamura A., Shimada T., Watanabe S., Yamagata K., Yasuda K.,
RA Ishii N., Fukamizu A.;
RT "Asymmetric arginine dimethylation determines life span in C. elegans by
RT regulating forkhead transcription factor DAF-16.";
RL Cell Metab. 13:505-516(2011).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PGL-1 AND PGL-3, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP HIS-288.
RX PubMed=24140420; DOI=10.1016/j.molcel.2013.09.014;
RA Li S., Yang P., Tian E., Zhang H.;
RT "Arginine methylation modulates autophagic degradation of PGL granules in
RT C. elegans.";
RL Mol. Cell 52:421-433(2013).
RN [4] {ECO:0000305}
RP INTERACTION WITH ALG-1.
RX PubMed=23516374; DOI=10.1371/journal.pgen.1003353;
RA Hunter S.E., Finnegan E.F., Zisoulis D.G., Lovci M.T.,
RA Melnik-Martinez K.V., Yeo G.W., Pasquinelli A.E.;
RT "Functional genomic analysis of the let-7 regulatory network in
RT Caenorhabditis elegans.";
RL PLoS Genet. 9:E1003353-E1003353(2013).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27994012; DOI=10.1128/mcb.00504-16;
RA Sha L., Daitoku H., Araoi S., Kaneko Y., Takahashi Y., Kako K.,
RA Fukamizu A.;
RT "Asymmetric arginine dimethylation modulates mitochondrial energy
RT metabolism and homeostasis in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 0:0-0(2016).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28158808; DOI=10.1093/jb/mvw101;
RA Hirota K., Shigekawa C., Araoi S., Sha L., Inagawa T., Kanou A., Kako K.,
RA Daitoku H., Fukamizu A.;
RT "Simultaneous ablation of prmt-1 and prmt-5 abolishes asymmetric and
RT symmetric arginine dimethylations in Caenorhabditis elegans.";
RL J. Biochem. 161:521-527(2017).
CC -!- FUNCTION: Arginine methyltransferase that methylates (mono and
CC asymmetric dimethylation) the guanidino nitrogens of arginyl residues
CC present in target proteins (PubMed:21531333, PubMed:24140420,
CC PubMed:27994012, PubMed:28158808). Catalyzes the formation of
CC monomethylarginine and asymmetric dimethylarginine on histones H2A and
CC H4, a specific tag for epigenetic transcriptional activation
CC (PubMed:21531333). Catalyzes asymmetric arginine dimethylation of
CC mitochondrial proteins necessary for mitochondrial oxidative
CC phosphorylation activity and thus aerobic respiration and ATP
CC synthesis, and the mitochondrial stress response (PubMed:27994012).
CC Methylates arginine residues in P-granule components pgl-1 and pgl-3 to
CC promote P-granule degradation by autophagy in somatic cells to ensure
CC exclusive localization of the P-granules in germ cells
CC (PubMed:24140420). Modulates the interaction of P-granule proteins epg-
CC 2 and sepa-1 (PubMed:24140420). Methylates arginine residues in daf-16,
CC which blocks ftt-2 binding to daf-16, prevents akt-mediated
CC phosphorylation and allows for daf-16 to translocate to the nucleus
CC (PubMed:21531333). In turn, association with daf-16 therefore allows
CC for the transcriptional activation of daf-16 and regulation of
CC longevity-related genes (PubMed:21531333). Maintains lifespan by
CC modulating daf-16 activity downstream of the daf-2 signaling pathway
CC (PubMed:21531333, PubMed:28158808). Plays a role in heat and oxidative
CC stress resistance (PubMed:21531333, PubMed:28158808). Role in stress
CC resistance and also fat storage may be in association with the daf-2
CC signaling pathway (PubMed:21531333). Required for normal feeding
CC behavior (PubMed:27994012). {ECO:0000269|PubMed:21531333,
CC ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:27994012,
CC ECO:0000269|PubMed:28158808}.
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:21531333, ECO:0000269|PubMed:24140420,
CC ECO:0000305|PubMed:27994012, ECO:0000305|PubMed:28158808};
CC -!- SUBUNIT: Interacts with daf-16 (PubMed:21531333). Interacts with pgl-1
CC and pgl-3 (PubMed:24140420). Interacts with alg-1 (PubMed:23516374).
CC {ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:23516374,
CC ECO:0000269|PubMed:24140420}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24140420}. Nucleus
CC {ECO:0000250|UniProtKB:Q99873}. Note=Diffuse cytoplasmic localization
CC during embryogenesis. {ECO:0000269|PubMed:24140420}.
CC -!- TISSUE SPECIFICITY: Widely expressed in pharyngeal, body wall muscle,
CC intestinal and vulval cells. {ECO:0000269|PubMed:21531333,
CC ECO:0000269|PubMed:24140420}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryogenesis (PubMed:24140420).
CC Expressed during larval development and adulthood (PubMed:21531333).
CC {ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:24140420}.
CC -!- DISRUPTION PHENOTYPE: Viable with a slight decrease in egg-laying
CC (PubMed:28158808). Defective arginine methyltransferase activity with
CC reduced asymmetric dimethylation of targets (PubMed:21531333,
CC PubMed:28158808). Reduced asymmetric arginine dimethylation of
CC mitochondrial proteins which results in defective mitochondrial
CC oxidative phosphorylation activity characterized by a reduced oxygen
CC consumption rate during aerobic respiration as compared to wild-type
CC animals, defective electron chain function and increased reactive
CC oxygen species production (PubMed:27994012). This overall leads to
CC reduced ATP synthesis and increased mitochondrial stress with an up-
CC regulation of stress response genes conferring a food avoidance
CC phenotype (PubMed:27994012). Defective symmetric arginine dimethylation
CC of targets in mitochondria (PubMed:27994012). Increased phosphorylation
CC of daf-16, increased binding of daf-16 to ftt-2 and subsequently
CC increased cytoplasmic retention of daf-16 (PubMed:21531333). Reduced
CC lifespan as a result of reduced expression of longevity-related
CC proteins such as sod-3, mtl-7, sip-1 and lys-7 (PubMed:21531333,
CC PubMed:28158808). Increased sensitivity to heat and oxidative stress
CC (PubMed:28158808). Double knockout with prmt-5 results in prolonged
CC larval development, shorter body size, reduced brood size, decreased
CC egg-laying and 30% of eggs fail to hatch (PubMed:28158808). Double
CC knockout also results in reduced asymmetric and symmetric arginine
CC dimethylation of proteins (PubMed:28158808).
CC {ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:27994012,
CC ECO:0000269|PubMed:28158808}.
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; BX284605; CAB54335.1; -; Genomic_DNA.
DR PIR; T26447; T26447.
DR RefSeq; NP_507909.1; NM_075508.4.
DR AlphaFoldDB; Q9U2X0; -.
DR SMR; Q9U2X0; -.
DR IntAct; Q9U2X0; 4.
DR STRING; 6239.Y113G7B.17.1; -.
DR EPD; Q9U2X0; -.
DR PaxDb; Q9U2X0; -.
DR PeptideAtlas; Q9U2X0; -.
DR EnsemblMetazoa; Y113G7B.17.1; Y113G7B.17.1; WBGene00013766.
DR EnsemblMetazoa; Y113G7B.17.2; Y113G7B.17.2; WBGene00013766.
DR GeneID; 180326; -.
DR KEGG; cel:CELE_Y113G7B.17; -.
DR UCSC; Y113G7B.17.1; c. elegans.
DR CTD; 180326; -.
DR WormBase; Y113G7B.17; CE23297; WBGene00013766; prmt-1.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000155867; -.
DR HOGENOM; CLU_017375_1_2_1; -.
DR InParanoid; Q9U2X0; -.
DR OMA; MEFTKCH; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q9U2X0; -.
DR BRENDA; 2.1.1.319; 1045.
DR Reactome; R-CEL-3214858; RMTs methylate histone arginines.
DR Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-CEL-9018519; Estrogen-dependent gene expression.
DR SignaLink; Q9U2X0; -.
DR PRO; PR:Q9U2X0; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00013766; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:WormBase.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:WormBase.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0010286; P:heat acclimation; IGI:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA:WormBase.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; IDA:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:1905909; P:regulation of dauer entry; IGI:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IGI:UniProtKB.
DR GO; GO:0010883; P:regulation of lipid storage; IGI:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IGI:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
DR GO; GO:0009411; P:response to UV; IGI:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..348
FT /note="Protein arginine N-methyltransferase 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000439508"
FT DOMAIN 24..342
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 139
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT ACT_SITE 148
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT MUTAGEN 70
FT /note="G->A: Defective S-adenosyl-L-methionine binding and
FT reduces methylation of daf-16."
FT /evidence="ECO:0000269|PubMed:21531333"
FT MUTAGEN 288
FT /note="H->Y: In bp292; reduces methylation and impairs
FT degradation of P-granule components pgl-1 and pgl-3 in
FT somatic cells during embryogenesis. Reduces lifespan."
FT /evidence="ECO:0000269|PubMed:24140420"
SQ SEQUENCE 348 AA; 39771 MW; 4658749A0EE39725 CRC64;
MSTENGKSAD APVAAPAAKE LTSKDYYFDS YAHFGIHEEM LKDEVRTTTY RNSIYHNSHL
FKDKVVMDVG SGTGILSMFA AKAGAKKVFA MEFSNMALTS RKIIADNNLD HIVEVIQAKV
EDVHELPGGI EKVDIIISEW MGYCLFYESM LNTVLVARDR WLAPNGMLFP DKARLYVCAI
EDRQYKEDKI HWWDSVYGFN MSAIKNVAIK EPLVDIVDNA QVNTNNCLLK DVDLYTVKIE
DLTFKSDFKL RCTRSDYIQA FVTFFTVEFS KCHKKTGFST GPDVQYTHWK QTVFYLKDAL
TVKKGEEITG SFEMAPNKNN ERDLDINISF DFKGEVCDLN EQNTYTMH
