GENTAUR Molecular Products.

 ANM3_RAT                Reviewed;         528 AA.
 O70467;
 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
 01-AUG-1998, sequence version 1.
 28-FEB-2018, entry version 144.
 RecName: Full=Protein arginine N-methyltransferase 3;
          EC=2.1.1.-;
 AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3;
 Name=Prmt3; Synonyms=Hrmt1l3;
 Rattus norvegicus (Rat).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
 Muroidea; Muridae; Murinae; Rattus.
 NCBI_TaxID=10116;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 PubMed=9642256; DOI=10.1074/jbc.273.27.16935;
 Tang J., Gary J.D., Clarke S., Herschman H.R.;
 "PRMT 3, a type I protein arginine N-methyltransferase that differs
 from PRMT1 in its oligomerization, subcellular localization, substrate
 specificity, and regulation.";
 J. Biol. Chem. 273:16935-16945(1998).
 [2]
 ANALYSIS OF ZINC-FINGER, AND ENZYME REGULATION.
 PubMed=10931850; DOI=10.1074/jbc.M006445200;
 Frankel A., Clarke S.;
 "PRMT3 is a distinct member of the protein arginine N-
 methyltransferase family. Conferral of substrate specificity by a
 zinc-finger domain.";
 J. Biol. Chem. 275:32974-32982(2000).
 [3]
 FUNCTION, AND INTERACTION WITH EPB41L3.
 PubMed=15334060; DOI=10.1038/sj.onc.1208057;
 Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A.,
 Gutmann D.H., Herschman H.R., Clarke S., Newsham I.F.;
 "DAL-1/4.1B tumor suppressor interacts with protein arginine N-
 methyltransferase 3 (PRMT3) and inhibits its ability to methylate
 substrates in vitro and in vivo.";
 Oncogene 23:7761-7771(2004).
 [4]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 208-528 IN COMPLEX WITH
 S-ADENOSYL-L-HOMOCYSTEINE, ACTIVE SITE, AND SUBUNIT.
 PubMed=10899106; DOI=10.1093/emboj/19.14.3509;
 Zhang X., Zhou L., Cheng X.;
 "Crystal structure of the conserved core of protein arginine
 methyltransferase PRMT3.";
 EMBO J. 19:3509-3519(2000).
 -!- FUNCTION: Methylates (mono and asymmetric dimethylation) the
     guanidino nitrogens of arginyl residues in some proteins.
     {ECO:0000269|PubMed:15334060}.
 -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide and high
     concentrations of zinc chloride. {ECO:0000269|PubMed:10931850}.
 -!- SUBUNIT: Monomer or homodimer. Interacts with the 40S ribosomal
     protein RPS2 (By similarity). Interacts with EPB41L3; this
     inhibits methylation of target proteins. {ECO:0000250,
     ECO:0000269|PubMed:10899106, ECO:0000269|PubMed:15334060}.
 -!- SUBCELLULAR LOCATION: Cytoplasm.
 -!- DOMAIN: The zinc-finger is responsible for substrate specificity.
 -!- SIMILARITY: Belongs to the class I-like SAM-binding
     methyltransferase superfamily. Protein arginine N-
     methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01015}.
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 EMBL; AF059530; AAC40158.1; -; mRNA.
 RefSeq; NP_446009.1; NM_053557.1.
 UniGene; Rn.33389; -.
 PDB; 1F3L; X-ray; 2.03 A; A=208-528.
 PDBsum; 1F3L; -.
 ProteinModelPortal; O70467; -.
 SMR; O70467; -.
 IntAct; O70467; 1.
 STRING; 10116.ENSRNOP00000020853; -.
 iPTMnet; O70467; -.
 PhosphoSitePlus; O70467; -.
 PaxDb; O70467; -.
 PRIDE; O70467; -.
 Ensembl; ENSRNOT00000020853; ENSRNOP00000020853; ENSRNOG00000014829.
 GeneID; 89820; -.
 KEGG; rno:89820; -.
 UCSC; RGD:620413; rat.
 CTD; 10196; -.
 RGD; 620413; Prmt3.
 eggNOG; KOG1499; Eukaryota.
 eggNOG; ENOG410XQYH; LUCA.
 GeneTree; ENSGT00550000074406; -.
 HOGENOM; HOG000198521; -.
 HOVERGEN; HBG001793; -.
 InParanoid; O70467; -.
 KO; K11436; -.
 PhylomeDB; O70467; -.
 EvolutionaryTrace; O70467; -.
 PRO; PR:O70467; -.
 Proteomes; UP000002494; Chromosome 1.
 Bgee; ENSRNOG00000014829; -.
 ExpressionAtlas; O70467; baseline and differential.
 Genevisible; O70467; RN.
 GO; GO:0005737; C:cytoplasm; IDA:RGD.
 GO; GO:0005829; C:cytosol; ISO:RGD.
 GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0008168; F:methyltransferase activity; ISO:RGD.
 GO; GO:0072341; F:modified amino acid binding; IDA:RGD.
 GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:RGD.
 GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:RGD.
 GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; TAS:RGD.
 GO; GO:0060997; P:dendritic spine morphogenesis; IMP:RGD.
 GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
 GO; GO:0018216; P:peptidyl-arginine methylation; IDA:RGD.
 GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA:RGD.
 GO; GO:0006479; P:protein methylation; ISO:RGD.
 GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
 InterPro; IPR025799; Arg_MeTrfase.
 InterPro; IPR029063; SAM-dependent_MTases.
 InterPro; IPR036236; Znf_C2H2_sf.
 SUPFAM; SSF53335; SSF53335; 1.
 SUPFAM; SSF57667; SSF57667; 1.
 PROSITE; PS51678; SAM_MT_PRMT; 1.
 PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
 1: Evidence at protein level;
 3D-structure; Acetylation; Complete proteome; Cytoplasm;
 Metal-binding; Methyltransferase; Phosphoprotein; Reference proteome;
 S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
 INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:O60678}.
 CHAIN         2    528       Protein arginine N-methyltransferase 3.
                              /FTId=PRO_0000212328.
 DOMAIN      214    528       SAM-dependent MTase PRMT-type.
                              {ECO:0000255|PROSITE-ProRule:PRU01015}.
 ZN_FING      46     69       C2H2-type.
 ACT_SITE    326    326       {ECO:0000269|PubMed:10899106}.
 ACT_SITE    335    335       {ECO:0000269|PubMed:10899106}.
 BINDING     227    227       S-adenosyl-L-methionine. {ECO:0000250}.
 BINDING     236    236       S-adenosyl-L-methionine.
 BINDING     260    260       S-adenosyl-L-methionine; via carbonyl
                              oxygen.
 BINDING     282    282       S-adenosyl-L-methionine.
 BINDING     311    311       S-adenosyl-L-methionine.
 MOD_RES       2      2       N-acetylcysteine.
                              {ECO:0000250|UniProtKB:O60678}.
 MOD_RES      22     22       Phosphoserine.
                              {ECO:0000250|UniProtKB:O60678}.
 MOD_RES      24     24       Phosphoserine.
                              {ECO:0000250|UniProtKB:O60678}.
 MOD_RES     169    169       Phosphoserine.
                              {ECO:0000250|UniProtKB:O60678}.
 STRAND      210    212       {ECO:0000244|PDB:1F3L}.
 HELIX       215    220       {ECO:0000244|PDB:1F3L}.
 STRAND      222    224       {ECO:0000244|PDB:1F3L}.
 HELIX       225    231       {ECO:0000244|PDB:1F3L}.
 HELIX       234    246       {ECO:0000244|PDB:1F3L}.
 HELIX       248    250       {ECO:0000244|PDB:1F3L}.
 TURN        251    253       {ECO:0000244|PDB:1F3L}.
 STRAND      255    260       {ECO:0000244|PDB:1F3L}.
 HELIX       265    273       {ECO:0000244|PDB:1F3L}.
 STRAND      276    284       {ECO:0000244|PDB:1F3L}.
 HELIX       286    296       {ECO:0000244|PDB:1F3L}.
 TURN        300    302       {ECO:0000244|PDB:1F3L}.
 STRAND      303    308       {ECO:0000244|PDB:1F3L}.
 TURN        310    312       {ECO:0000244|PDB:1F3L}.
 STRAND      316    318       {ECO:0000244|PDB:1F3L}.
 STRAND      320    324       {ECO:0000244|PDB:1F3L}.
 TURN        333    335       {ECO:0000244|PDB:1F3L}.
 HELIX       337    348       {ECO:0000244|PDB:1F3L}.
 STRAND      349    357       {ECO:0000244|PDB:1F3L}.
 STRAND      359    367       {ECO:0000244|PDB:1F3L}.
 HELIX       370    376       {ECO:0000244|PDB:1F3L}.
 HELIX       378    381       {ECO:0000244|PDB:1F3L}.
 HELIX       389    394       {ECO:0000244|PDB:1F3L}.
 TURN        395    397       {ECO:0000244|PDB:1F3L}.
 STRAND      400    402       {ECO:0000244|PDB:1F3L}.
 HELIX       406    408       {ECO:0000244|PDB:1F3L}.
 STRAND      414    420       {ECO:0000244|PDB:1F3L}.
 TURN        421    423       {ECO:0000244|PDB:1F3L}.
 HELIX       426    429       {ECO:0000244|PDB:1F3L}.
 STRAND      430    439       {ECO:0000244|PDB:1F3L}.
 STRAND      443    456       {ECO:0000244|PDB:1F3L}.
 STRAND      464    467       {ECO:0000244|PDB:1F3L}.
 STRAND      479    490       {ECO:0000244|PDB:1F3L}.
 STRAND      495    504       {ECO:0000244|PDB:1F3L}.
 STRAND      511    518       {ECO:0000244|PDB:1F3L}.
 STRAND      521    527       {ECO:0000244|PDB:1F3L}.
 SEQUENCE   528 AA;  59420 MW;  B25D627902594B39 CRC64;
 MCSLAAGNGQ GAELGPEPLE LSDSGDDAGW EDEDADAEPA QGRQHTPCLF CDRLFRSAEE
 TFSHCKLEHQ FNIDGMVHKH GLEFYGYIKL INFIRLKNPT VEYMNSIYNP VPWDKDEYLK
 PVLEDDLLLQ FDVEDLYEPV SAPFTYPNGL SENTSAVEKL KLMEARALSA EAALARARED
 LQKMKQFAQD FVMNVDVRTC SSTTTIADLQ EDEDGVYFSS YGHYGIHEEM LKDKVRTESY
 RDFIYQNPHI FKDKVVLDVG CGTGILSMFA AKAGAKKVIA VDQSEILYQA MDIIRLNKLE
 DTIVLIKGKI EEVSLPVEKV DVIISEWMGY FLLFESMLDS VLYAKSKYLA KGGSVYPDIC
 TISLVAVSDV SKHADRIAFW DDVYGFNMSC MKKAVIPEAV VEVVDHKTLI SDPCDIKHID
 CHTTSISDLE FSSDFTLRTT KTAMCTAVAG YFDIYFEKNC HNRVVFSTGP QSTKTHWKQT
 IFLLEKPFPV KAGEALKGKI TVHKNKKDPR SLIVTLTLNS STQTYSLQ

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