ANM3_MOUSE
ID ANM3_MOUSE Reviewed; 528 AA.
AC Q922H1; Q3U2K1; Q80VU9; Q8BFV5;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein arginine N-methyltransferase 3 {ECO:0000250|UniProtKB:O70467};
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:O70467};
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3;
GN Name=Prmt3 {ECO:0000312|MGI:MGI:1919224}; Synonyms=Hrmt1l3;
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 [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Hauser L.J., Webb L.S., Dhar M.S., Mural R.M., Larimer F.W., Johnson D.K.;
RT "Genomic organization, chromosomal mapping, and expression analysis of the
RT murine Prmt3 and Htatip2 genes.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-24, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP STRUCTURE BY NMR OF 38-145.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C2H2 zinc finger domain of the protein arginine
RT N-methyltransferase 3 from Mus musculus.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Protein-arginine N-methyltransferase that catalyzes both the
CC monomethylation and asymmetric dimethylation of the guanidino nitrogens
CC of arginine residues in target proteins, and therefore falls into the
CC group of type I methyltransferases (By similarity). May regulate
CC retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal
CC dehydrogenase activity (By similarity). {ECO:0000250|UniProtKB:O60678,
CC ECO:0000250|UniProtKB:O70467}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:65280;
CC Evidence={ECO:0000250|UniProtKB:O70467};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48101;
CC Evidence={ECO:0000250|UniProtKB:O70467};
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:O70467};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097;
CC Evidence={ECO:0000250|UniProtKB:O70467};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide and high
CC concentrations of zinc chloride. {ECO:0000250|UniProtKB:O70467}.
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with EPB41L3
CC (via FERM domain); the interaction is direct and inhibits the protein-
CC arginine N-methyltransferase activity of PRMT3. Interacts with the 40S
CC ribosomal protein RPS2. Interacts with ALDH1A1; the interaction is
CC direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is
CC independent of the methyltransferase activity of PRMT3 (By similarity).
CC {ECO:0000250|UniProtKB:O60678, ECO:0000250|UniProtKB:O70467}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O70467}.
CC -!- DOMAIN: The C2H2-type zinc-finger is responsible for substrate
CC specificity. {ECO:0000250|UniProtKB:O70467}.
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; AY151050; AAN84530.1; -; Genomic_DNA.
DR EMBL; AK031738; BAC27531.1; -; mRNA.
DR EMBL; AK086646; BAC39708.1; -; mRNA.
DR EMBL; AK155236; BAE33139.1; -; mRNA.
DR EMBL; JH584275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008128; AAH08128.1; -; mRNA.
DR EMBL; BC050775; AAH50775.1; -; mRNA.
DR CCDS; CCDS21307.1; -.
DR PDB; 1WIR; NMR; -; A=38-145.
DR PDBsum; 1WIR; -.
DR AlphaFoldDB; Q922H1; -.
DR BMRB; Q922H1; -.
DR SMR; Q922H1; -.
DR BioGRID; 215067; 2.
DR IntAct; Q922H1; 2.
DR MINT; Q922H1; -.
DR STRING; 10090.ENSMUSP00000032715; -.
DR iPTMnet; Q922H1; -.
DR PhosphoSitePlus; Q922H1; -.
DR EPD; Q922H1; -.
DR jPOST; Q922H1; -.
DR MaxQB; Q922H1; -.
DR PaxDb; Q922H1; -.
DR PRIDE; Q922H1; -.
DR Antibodypedia; 1605; 345 antibodies from 33 providers.
DR DNASU; 71974; -.
DR Ensembl; ENSMUST00000032715; ENSMUSP00000032715; ENSMUSG00000030505.
DR GeneID; 71974; -.
DR CTD; 10196; -.
DR MGI; MGI:1919224; Prmt3.
DR VEuPathDB; HostDB:ENSMUSG00000030505; -.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000156825; -.
DR HOGENOM; CLU_017375_6_2_1; -.
DR InParanoid; Q922H1; -.
DR OMA; ETHWQQG; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q922H1; -.
DR TreeFam; TF323587; -.
DR Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR Reactome; R-MMU-8876725; Protein methylation.
DR BioGRID-ORCS; 71974; 6 hits in 77 CRISPR screens.
DR ChiTaRS; Prmt8; mouse.
DR EvolutionaryTrace; Q922H1; -.
DR PRO; PR:Q922H1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q922H1; protein.
DR Bgee; ENSMUSG00000030505; Expressed in undifferentiated genital tubercle and 256 other tissues.
DR ExpressionAtlas; Q922H1; baseline and differential.
DR Genevisible; Q922H1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; ISO:MGI.
DR GO; GO:0072341; F:modified amino acid binding; ISO:MGI.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:MGI.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; ISO:MGI.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IEA:RHEA.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:1900053; P:negative regulation of retinoic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; ISO:MGI.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; ISO:MGI.
DR GO; GO:0006479; P:protein methylation; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Metal-binding; Methyltransferase;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60678"
FT CHAIN 2..528
FT /note="Protein arginine N-methyltransferase 3"
FT /id="PRO_0000212327"
FT DOMAIN 214..528
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ZN_FING 46..69
FT /note="C2H2-type"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..528
FT /note="Mediates interaction with ALDH1A1"
FT /evidence="ECO:0000250|UniProtKB:O60678"
FT REGION 282..284
FT /note="S-adenosyl-L-methionine"
FT /evidence="ECO:0000250|UniProtKB:O70467"
FT REGION 310..311
FT /note="S-adenosyl-L-methionine"
FT /evidence="ECO:0000250|UniProtKB:O70467"
FT ACT_SITE 326
FT /evidence="ECO:0000250|UniProtKB:O70467"
FT ACT_SITE 335
FT /evidence="ECO:0000250|UniProtKB:O70467"
FT BINDING 236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O70467"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O70467"
FT BINDING 340
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O60678"
FT MOD_RES 2
FT /note="N-acetylcysteine"
FT /evidence="ECO:0000250|UniProtKB:O60678"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60678"
FT CONFLICT 131
FT /note="F -> Y (in Ref. 2; BAE33139)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="K -> KMDGK (in Ref. 4; AAH50775)"
FT /evidence="ECO:0000305"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1WIR"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1WIR"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:1WIR"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:1WIR"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:1WIR"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:1WIR"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1WIR"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1WIR"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1WIR"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1WIR"
SQ SEQUENCE 528 AA; 59471 MW; E8DF5B88AB6B92FF CRC64;
MCSLAAGNGR GAELGPEPLE LSDSGDDAGW EDEDADTEPA HGRQHTPCLF CDRLFASAEE
TFSHCKLEHQ FNIDSMVHKH GLEFYGYIKL INFIRLKNPT VEYMNSIYNP VPWEKDEYLK
PVLEDDLLLQ FDVEDLYEPV STPFSYPNGL SESASVVEKL KHMEARALSA EAALARARED
LQKMKQFAQD FVMNVDVRTC SSTTTIADLQ EDEDGVYFSS YGHYGIHEEM LKDKVRTESY
RDFIYQNPHI FKDKVVLDVG CGTGILSMFA AKVGAKKVIA VDQSEILYQA MDIIRLNKLE
DTIVLIKGKI EEVSLPVEKV DVIISEWMGY FLLFESMLDS VLYAKSKYLA KGGSVYPDIC
TISLVAVSDV SKHADRIAFW DDVYGFNMSC MKKAVIPEAV VEVVDHKTLI SDPCDIKHID
CHTTSISDLE FSSDFTLRTT KTAMCTAVAG YFDIYFEKNC HNRVVFSTGP QSTKTHWKQT
VFLLEKPFPV KAGEALKGKI TVHKNKKDPR SLIVTLTLNS STQTYSLQ
