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Protein arginine N-methyltransferase 3 (EC 2.1.1.-) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3)

 ANM3_RAT                Reviewed;         528 AA.
O70467;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
25-OCT-2017, entry version 142.
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; IBA:GO_Central.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0018216; P:peptidyl-arginine methylation; IDA:RGD.
GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA: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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