O70467 · ANM3_RAT
- ProteinProtein arginine N-methyltransferase 3
- GenePrmt3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids528 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases (PubMed:10899106, PubMed:15334060, PubMed:9642256).
May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity (By similarity).
May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity (By similarity).
Catalytic activity
- L-arginyl-[protein] + S-adenosyl-L-methionine = H+ + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Activity regulation
Inhibited by N-ethylmaleimide and high concentrations of zinc chloride.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 236 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 260 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 282 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 284 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 310 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 311 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 326 | |||||
Sequence: E | ||||||
Active site | 335 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | histone methyltransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | methyltransferase activity | |
Molecular Function | modified amino acid binding | |
Molecular Function | protein-arginine N-methyltransferase activity | |
Molecular Function | protein-arginine omega-N asymmetric methyltransferase activity | |
Molecular Function | protein-arginine omega-N monomethyltransferase activity | |
Molecular Function | ribosome binding | |
Molecular Function | S-adenosylmethionine-dependent methyltransferase activity | |
Biological Process | chromatin remodeling | |
Biological Process | dendritic spine morphogenesis | |
Biological Process | methylation | |
Biological Process | negative regulation of protein ubiquitination | |
Biological Process | negative regulation of retinoic acid biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein arginine N-methyltransferase 3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionO70467
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylcysteine | ||||
Sequence: C | ||||||
Chain | PRO_0000212328 | 2-528 | Protein arginine N-methyltransferase 3 | |||
Sequence: CSLAAGNGQGAELGPEPLELSDSGDDAGWEDEDADAEPAQGRQHTPCLFCDRLFRSAEETFSHCKLEHQFNIDGMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWDKDEYLKPVLEDDLLLQFDVEDLYEPVSAPFTYPNGLSENTSAVEKLKLMEARALSAEAALARAREDLQKMKQFAQDFVMNVDVRTCSSTTTIADLQEDEDGVYFSSYGHYGIHEEMLKDKVRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKVDVIISEWMGYFLLFESMLDSVLYAKSKYLAKGGSVYPDICTISLVAVSDVSKHADRIAFWDDVYGFNMSCMKKAVIPEAVVEVVDHKTLISDPCDIKHIDCHTTSISDLEFSSDFTLRTTKTAMCTAVAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTIFLLEKPFPVKAGEALKGKITVHKNKKDPRSLIVTLTLNSSTQTYSLQ | ||||||
Modified residue | 22 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 24 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 169 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Monomer and homodimer (PubMed:10899106, PubMed:9642256).
Interacts with EPB41L3 (via FERM domain); the interaction is direct and inhibits the protein-arginine N-methyltransferase activity of PRMT3 (PubMed:15334060).
Interacts with the 40S ribosomal protein RPS2 (By similarity).
Interacts with ALDH1A1; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3 (PubMed:15334060).
Interacts with EPB41L3 (via FERM domain); the interaction is direct and inhibits the protein-arginine N-methyltransferase activity of PRMT3 (PubMed:15334060).
Interacts with the 40S ribosomal protein RPS2 (By similarity).
Interacts with ALDH1A1; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3 (PubMed:15334060).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-42 | Disordered | ||||
Sequence: MCSLAAGNGQGAELGPEPLELSDSGDDAGWEDEDADAEPAQG | ||||||
Zinc finger | 46-69 | C2H2-type | ||||
Sequence: TPCLFCDRLFRSAEETFSHCKLEH | ||||||
Region | 184-528 | Mediates interaction with ALDH1A1 | ||||
Sequence: MKQFAQDFVMNVDVRTCSSTTTIADLQEDEDGVYFSSYGHYGIHEEMLKDKVRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKVDVIISEWMGYFLLFESMLDSVLYAKSKYLAKGGSVYPDICTISLVAVSDVSKHADRIAFWDDVYGFNMSCMKKAVIPEAVVEVVDHKTLISDPCDIKHIDCHTTSISDLEFSSDFTLRTTKTAMCTAVAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTIFLLEKPFPVKAGEALKGKITVHKNKKDPRSLIVTLTLNSSTQTYSLQ | ||||||
Domain | 214-528 | SAM-dependent MTase PRMT-type | ||||
Sequence: DGVYFSSYGHYGIHEEMLKDKVRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKVDVIISEWMGYFLLFESMLDSVLYAKSKYLAKGGSVYPDICTISLVAVSDVSKHADRIAFWDDVYGFNMSCMKKAVIPEAVVEVVDHKTLISDPCDIKHIDCHTTSISDLEFSSDFTLRTTKTAMCTAVAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTIFLLEKPFPVKAGEALKGKITVHKNKKDPRSLIVTLTLNSSTQTYSLQ |
Domain
The C2H2-type zinc-finger is responsible for substrate specificity.
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length528
- Mass (Da)59,420
- Last updated1998-08-01 v1
- ChecksumB25D627902594B39
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JW52 | A0A0G2JW52_RAT | Prmt3 | 499 | ||
A0A8L2QAU2 | A0A8L2QAU2_RAT | Prmt3 | 524 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF059530 EMBL· GenBank· DDBJ | AAC40158.1 EMBL· GenBank· DDBJ | mRNA |