ANM3_RAT
ID ANM3_RAT Reviewed; 528 AA.
AC O70467;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protein arginine N-methyltransferase 3 {ECO:0000305|PubMed:9642256};
DE EC=2.1.1.319 {ECO:0000269|PubMed:9642256};
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3;
GN Name=Prmt3 {ECO:0000312|RGD:620413}; Synonyms=Hrmt1l3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9642256; DOI=10.1074/jbc.273.27.16935;
RA Tang J., Gary J.D., Clarke S., Herschman H.R.;
RT "PRMT 3, a type I protein arginine N-methyltransferase that differs from
RT PRMT1 in its oligomerization, subcellular localization, substrate
RT specificity, and regulation.";
RL J. Biol. Chem. 273:16935-16945(1998).
RN [2]
RP DOMAIN, AND ACTIVITY REGULATION.
RX PubMed=10931850; DOI=10.1074/jbc.m006445200;
RA Frankel A., Clarke S.;
RT "PRMT3 is a distinct member of the protein arginine N-methyltransferase
RT family. Conferral of substrate specificity by a zinc-finger domain.";
RL J. Biol. Chem. 275:32974-32982(2000).
RN [3]
RP FUNCTION, AND INTERACTION WITH EPB41L3.
RX PubMed=15334060; DOI=10.1038/sj.onc.1208057;
RA Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A.,
RA Gutmann D.H., Herschman H.R., Clarke S., Newsham I.F.;
RT "DAL-1/4.1B tumor suppressor interacts with protein arginine N-
RT methyltransferase 3 (PRMT3) and inhibits its ability to methylate
RT substrates in vitro and in vivo.";
RL Oncogene 23:7761-7771(2004).
RN [4] {ECO:0007744|PDB:1F3L}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 208-528 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, ACTIVE SITE, AND SUBUNIT.
RX PubMed=10899106; DOI=10.1093/emboj/19.14.3509;
RA Zhang X., Zhou L., Cheng X.;
RT "Crystal structure of the conserved core of protein arginine
RT methyltransferase PRMT3.";
RL EMBO J. 19:3509-3519(2000).
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 (PubMed:9642256, PubMed:15334060,
CC PubMed:10899106). May regulate retinoic acid synthesis and signaling by
CC inhibiting ALDH1A1 retinal dehydrogenase activity (By similarity).
CC {ECO:0000250|UniProtKB:O60678, ECO:0000269|PubMed:10899106,
CC ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:9642256}.
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:0000269|PubMed:9642256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48101;
CC Evidence={ECO:0000305|PubMed:9642256};
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:9642256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097;
CC Evidence={ECO:0000305|PubMed:9642256};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide and high
CC concentrations of zinc chloride. {ECO:0000269|PubMed:10931850}.
CC -!- SUBUNIT: Monomer and homodimer (PubMed:9642256, PubMed:10899106).
CC Interacts with EPB41L3 (via FERM domain); the interaction is direct and
CC inhibits the protein-arginine N-methyltransferase activity of PRMT3
CC (PubMed:15334060). Interacts with the 40S ribosomal protein RPS2 (By
CC similarity). Interacts with ALDH1A1; the interaction is direct,
CC inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of
CC the methyltransferase activity of PRMT3 (PubMed:15334060).
CC {ECO:0000250|UniProtKB:O60678, ECO:0000269|PubMed:10899106,
CC ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:9642256}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9642256}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9642256}.
CC -!- DOMAIN: The C2H2-type zinc-finger is responsible for substrate
CC specificity. {ECO:0000269|PubMed:10931850}.
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; AF059530; AAC40158.1; -; mRNA.
DR RefSeq; NP_446009.1; NM_053557.1.
DR PDB; 1F3L; X-ray; 2.03 A; A=208-528.
DR PDBsum; 1F3L; -.
DR AlphaFoldDB; O70467; -.
DR SMR; O70467; -.
DR IntAct; O70467; 1.
DR STRING; 10116.ENSRNOP00000020853; -.
DR iPTMnet; O70467; -.
DR PhosphoSitePlus; O70467; -.
DR jPOST; O70467; -.
DR PaxDb; O70467; -.
DR PRIDE; O70467; -.
DR GeneID; 89820; -.
DR KEGG; rno:89820; -.
DR UCSC; RGD:620413; rat.
DR CTD; 10196; -.
DR RGD; 620413; Prmt3.
DR VEuPathDB; HostDB:ENSRNOG00000014829; -.
DR eggNOG; KOG1499; Eukaryota.
DR HOGENOM; CLU_017375_6_2_1; -.
DR InParanoid; O70467; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; O70467; -.
DR BRENDA; 2.1.1.319; 5301.
DR Reactome; R-RNO-3214858; RMTs methylate histone arginines.
DR Reactome; R-RNO-8876725; Protein methylation.
DR EvolutionaryTrace; O70467; -.
DR PRO; PR:O70467; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000014829; Expressed in quadriceps femoris and 19 other tissues.
DR ExpressionAtlas; O70467; baseline and differential.
DR Genevisible; O70467; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; ISO:RGD.
DR GO; GO:0072341; F:modified amino acid binding; IDA:RGD.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:RGD.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:RGD.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IEA:RHEA.
DR GO; GO:0043022; F:ribosome binding; ISO:RGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; TAS:RGD.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:1900053; P:negative regulation of retinoic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IDA:RGD.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA:RGD.
DR GO; GO:0006479; P:protein methylation; ISO:RGD.
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_0000212328"
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..42
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:0000269|PubMed:10899106,
FT ECO:0007744|PDB:1F3L"
FT REGION 310..311
FT /note="S-adenosyl-L-methionine"
FT /evidence="ECO:0000269|PubMed:10899106,
FT ECO:0007744|PDB:1F3L"
FT ACT_SITE 326
FT /evidence="ECO:0000269|PubMed:10899106"
FT ACT_SITE 335
FT /evidence="ECO:0000269|PubMed:10899106"
FT BINDING 236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:10899106,
FT ECO:0007744|PDB:1F3L"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:10899106,
FT ECO:0007744|PDB:1F3L"
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:0000250|UniProtKB:O60678"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60678"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60678"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1F3L"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:1F3L"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:1F3L"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:1F3L"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 349..357
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 359..367
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 370..376
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:1F3L"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 414..420
FT /evidence="ECO:0007829|PDB:1F3L"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:1F3L"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 430..439
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 443..456
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 479..490
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 495..504
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 511..518
FT /evidence="ECO:0007829|PDB:1F3L"
FT STRAND 521..527
FT /evidence="ECO:0007829|PDB:1F3L"
SQ 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
