| IED ID | IndEnz0002015771 |
| Enzyme Type ID | protease015771 |
| Protein Name |
N-acetylated-alpha-linked acidic dipeptidase 2 EC 3.4.17.21 Glutamate carboxypeptidase III GCPIII N-acetylaspartylglutamate peptidase II NAAG-peptidase II N-acetylated-alpha-linked acidic dipeptidase II NAALADase II |
| Gene Name | Naalad2 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MARPRHLRGLGMCITAVLASFIAGFTVGWFIKPLKETTTSAGYHQSIQQKLLSEMKAENIRSFLRSFTKLPHLAGTEQNLLLAKKIQTQWKKFGLDSANLVHYDVLLSYPNETNANYVSIVDEHGVEIFKTSYLEPPPDGYENVTNIIPPYNAFSASGMPEGELVYVNYARTEDFFKLEREMNINCTGKIVIARYGKIFRGNKVKNAMLAGAMGIILYSDPADYFAPDVQPYPKGWNLPGAAAQRGNVLNLNGAGDPLTPGYPAKEYTFRLPVEEAVGIPNIPVHPIGYNDAERLLRNLGGAAPPDKSWKGSLNVSYNIGPGFTGSEYSRNIRMHVNNINKITRIYNVIGTIRGSTEPDRYVILGGHRDSWVFGGIDPTTGTAVLQEIARSFGKLVNGGWRPRRTIIFASWDAEEFGLLGSTEWAEENAKLLQERSIAYINSDSAIEGNYTLRVDCTPLLNQLVYKVAREISSPDDGFESKSLYESWLEKDPSPENKECPRINKLGSGSDFEAYFQRLGIASGRARYTKNKKTDKYSSYPVYHTIYETFELVQNFYDPTFKKQLSVAQLRGALVYELADSVVIPFNIQDYAKALKNYAASIFNISKKHDQQLRNHAVSFDPLFSAVKNFSEAASDFHRRLTQVDLNNPIAVRIMNDQQMLLERAFIDPLGLPGRKFYRHIIFAPSSHNKYAGESFPGIYDAMFDIENKADPSLAWAEVKKHISIAAFTIQAAAGTLTNVL |
| Enzyme Length | 740 |
| Uniprot Accession Number | Q9CZR2 |
| Absorption | |
| Active Site | ACT_SITE 414; /note=Nucleophile; for NAALADase activity; /evidence=ECO:0000250; ACT_SITE 618; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 656; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 679; /note=Charge relay system; /evidence=ECO:0000255 |
| Activity Regulation | |
| Binding Site | BINDING 200; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; BINDING 247; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; BINDING 414; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; BINDING 542; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q04609 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.; EC=3.4.17.21; |
| DNA Binding | |
| EC Number | 3.4.17.21 |
| Enzyme Function | FUNCTION: Has N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Also exhibits a dipeptidyl-peptidase IV type activity. Inactivates the peptide neurotransmitter N-acetylaspartylglutamate. {ECO:0000269|PubMed:15086519}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (4); Binding site (4); Chain (1); Glycosylation (7); Metal binding (10); Region (5); Sequence conflict (2); Topological domain (2); Transmembrane (1) |
| Keywords | Carboxypeptidase;Cell membrane;Dipeptidase;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Multifunctional enzyme;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q04609}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q04609}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10725249; 11217851; 12466851; 21267068; 21908619; |
| Motif | |
| Gene Encoded By | |
| Mass | 82,801 |
| Kinetics | |
| Metal Binding | METAL 259; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 262; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 367; /note=Zinc 1; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 377; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 377; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 415; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 423; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 426; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 443; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 543; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q04609 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.21; |