ANM2_MOUSE
ID ANM2_MOUSE Reviewed; 448 AA.
AC Q9R144;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
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; Synonyms=Hrmt1l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tsyba L.O., Kvasha S.M., Skripkina I.Y., Anoprienko O.V., Slavov D.,
RA Tassone F., Rynditch A.V., Gardiner K.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, INTERACTION WITH RB1 AND E2F1, AND TISSUE SPECIFICITY.
RX PubMed=16616919; DOI=10.1016/j.yexcr.2006.03.001;
RA Yoshimoto T., Boehm M., Olive M., Crook M.F., San H., Langenickel T.,
RA Nabel E.G.;
RT "The arginine methyltransferase PRMT2 binds RB and regulates E2F
RT function.";
RL Exp. Cell Res. 312:2040-2053(2006).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16648481; DOI=10.1128/mcb.26.10.3864-3874.2006;
RA Ganesh L., Yoshimoto T., Moorthy N.C., Akahata W., Boehm M., Nabel E.G.,
RA Nabel G.J.;
RT "Protein methyltransferase 2 inhibits NF-kappaB function and promotes
RT apoptosis.";
RL Mol. Cell. Biol. 26:3864-3874(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20798359; DOI=10.1161/circresaha.110.225326;
RA Iwasaki H., Kovacic J.C., Olive M., Beers J.K., Yoshimoto T., Crook M.F.,
RA Tonelli L.H., Nabel E.G.;
RT "Disruption of protein arginine N-methyltransferase 2 regulates leptin
RT signaling and produces leanness in vivo through loss of STAT3
RT methylation.";
RL Circ. Res. 107:992-1001(2010).
RN [5]
RP FUNCTION.
RX PubMed=20708585; DOI=10.1016/j.devcel.2010.07.007;
RA Blythe S.A., Cha S.-W., Tadjuidje E., Heasman J., Klein P.S.;
RT "beta-Catenin primes organizer gene expression by recruiting a histone H3
RT arginine 8 methyltransferase, Prmt2.";
RL Dev. Cell 19:220-231(2010).
CC -!- FUNCTION: Arginine methyltransferase that methylates the guanidino
CC nitrogens of arginyl residues in proteins such as STAT3, FBL, histone
CC H4. May inhibit NF-kappa-B transcription, and promote apoptosis.
CC Represses E2F1 transcriptional activity (in a RB1-dependent manner).
CC Has a negative regulation effect on G1 to S transition of mitotic cell
CC cycle. Involved in growth regulation. Acts as a coactivator (with
CC NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as
CC a coactivator (with estrogen) of estrogen receptor (ER)-mediated
CC transactivation. Enhances PGR, PPARG, RARA-mediated transactivation.
CC {ECO:0000269|PubMed:16616919, ECO:0000269|PubMed:16648481,
CC ECO:0000269|PubMed:20708585, ECO:0000269|PubMed:20798359}.
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: Self-associates (By similarity). Interacts with HNRNPUL1.
CC Interacts with NFKBIA (By similarity). Interacts with NCOA6
CC coactivator. Interacts (via SH3 domain) with PRMT8. Interacts with AR.
CC Interacts with ESR1, ESR2, PGR, PPARG, RARA, RXRA and THRB (By
CC similarity). Interacts with RB1 and E2F1. {ECO:0000250,
CC ECO:0000269|PubMed:16616919}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Translocates from the cytoplasm to the nucleus, after hormone
CC exposure. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, pancreas, lung, brain, skeletal
CC muscle, heart, muscle and fat. {ECO:0000269|PubMed:16616919}.
CC -!- DISRUPTION PHENOTYPE: From 6 to 30 weeks of age, males gain less weight
CC than age-matched control wild-type mice when weaned onto a chow diet.
CC By 30 weeks of age, females are also lean compared with wild-type
CC females. At 12 weeks of age, male and female are 3% to 4% shorter than
CC wild-type controls. Shows less hepatic cytoplasmic vacuoles, more
CC distinct hepatic cords and sinusoids and increased leptin sensitivity.
CC {ECO:0000269|PubMed:16648481, ECO:0000269|PubMed:20798359}.
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; AF169620; AAD48847.1; -; mRNA.
DR AlphaFoldDB; Q9R144; -.
DR SMR; Q9R144; -.
DR IntAct; Q9R144; 1.
DR STRING; 10090.ENSMUSP00000097167; -.
DR iPTMnet; Q9R144; -.
DR PhosphoSitePlus; Q9R144; -.
DR PaxDb; Q9R144; -.
DR PRIDE; Q9R144; -.
DR ProteomicsDB; 296251; -.
DR MGI; MGI:1316652; Prmt2.
DR InParanoid; Q9R144; -.
DR PhylomeDB; Q9R144; -.
DR BRENDA; 2.1.1.319; 3474.
DR ChiTaRS; Prmt2; mouse.
DR PRO; PR:Q9R144; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9R144; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:BHF-UCL.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:BHF-UCL.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISS:UniProtKB.
DR GO; GO:0033142; F:nuclear progesterone receptor binding; ISS:BHF-UCL.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; ISS:BHF-UCL.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISS:BHF-UCL.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISS:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IMP: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; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0048588; P:developmental cell growth; IMP:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; NAS:BHF-UCL.
DR GO; GO:0032259; P:methylation; NAS:BHF-UCL.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA: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 GO; GO:0042509; P:regulation of tyrosine phosphorylation of STAT protein; NAS:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
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 1: Evidence at protein level;
KW Cytoplasm; Methylation; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; SH3 domain; Transferase.
FT CHAIN 1..448
FT /note="Protein arginine N-methyltransferase 2"
FT /id="PRO_0000212325"
FT DOMAIN 42..101
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 111..414
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..289
FT /note="Interaction with ESR1"
FT /evidence="ECO:0000250"
FT REGION 95..219
FT /note="Interaction with RB1"
FT /evidence="ECO:0000269|PubMed:16616919"
FT REGION 145..287
FT /note="Interaction with ESR1"
FT /evidence="ECO:0000250"
FT ACT_SITE 223
FT /evidence="ECO:0000250"
FT ACT_SITE 232
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 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P55345"
FT MOD_RES 84
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P55345"
SQ SEQUENCE 448 AA; 50476 MW; 63E1F8C3FC66C25E CRC64;
MEAPGEGPCS ESQVIPVLEE DPVDYGCEMQ LLQDGAQLQL QLQPEEFVAI ADYTATDETQ
LSFLRGEKIL ILRQTTADWW WGERAGCCGY IPANHLGKQL EEYDPEDTWQ DEEYFDSYGT
LKLHLEMLAD QPRTTKYHSV ILQNKESLKD KVILDVGCGT GIISLFCAHH ARPKAVYAVE
ASDMAQHTSQ LVLQNGFADT ITVFQQKVED VVLPEKVDVL VSEWMGTCLL FEFMIESILY
ARDTWLKGDG IIWPTTAALH LVPCSAEKDY HSKVLFWDNA YEFNLSALKS LAIKEFFSRP
KSNHILKPED CLSEPCTILQ LDMRTVQVPD LETMRGELRF DIQKAGTLHG FTAWFSVYFQ
SLEEGQPQQV VSTGPLHPTT HWKQTLFMMD DPVPVHTGDV VHGFCCVTKK SGMEKAHVCL
SELGCHVRTR SHVSTELETG SFRSGGDS
