| IED ID | IndEnz0002003058 |
| Enzyme Type ID | protease003058 |
| Protein Name |
Glutamate carboxypeptidase 2 EC 3.4.17.21 Folate hydrolase 1 Folylpoly-gamma-glutamate carboxypeptidase FGCP Glutamate carboxypeptidase II GCPII Membrane glutamate carboxypeptidase mGCP N-acetylated-alpha-linked acidic dipeptidase I NAALADase I Prostate-specific membrane antigen homolog Pteroylpoly-gamma-glutamate carboxypeptidase |
| Gene Name | Folh1 Naalad1 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MWNAQQDSDSAEALGRRQRWFCAGTLVLAFTGTFIIGFLFGWFIKPSNDSTSSVSYPGMKKAFLQELKAENIKKFLYNFTRTPHLAGTQHNFELAKQIHAQWKEFGLDLVELSDYDVLLSYPNKTHPNYISIINEDGNEIFKTSLAELSPPGYENISDVVPPYSAFSPQGTPEGDLVYVNYARTEDFFKLERVMKINCSGKIVIARYGQVFRGNKVKNAQLAGAKGIILYSDPADYFVPGVKSYPDGWNLPGGGVQRGNVLNLNGAGDPLTPGYPANEYAYRHEFTEAVGLPSIPVHPIGYDDAQKLLEHMGGSAPPDSSWKGGLKVPYNVGPGFAGNFSKQKVKLHIHSYNKVTRIYNVIGTLKGAVEPDRYVILGGHRDAWVFGGIDPQSGAAVVHEIVRTFGTLKKKGWRPRRTILFASWDAEEFGLLGSTEWAEEHSRLLQERGVAYINADSSIEGNYTLRVDCTPLMHSLVYNLTKELPSPDEGFEGKSLYDSWKEKSPSTEFIGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWKNNKVSSYPLYHSVYETYELVEKFYDPTFKYHLTVAQVRGAMVFELANSIVLPFDCQSYAVALKKHAETIYNISMNHPQEMKAYMISFDSLFSAVNNFTDVASKFNQRLQDLDKSNPILLRILNDQLMYLERAFIDPLGLPGRPFYRHIIYAPSSHNKYAGESFPGIYDALFDINNKVDTSKAWREVKRQISIAAFTVQAAAETLREVD |
| Enzyme Length | 752 |
| Uniprot Accession Number | P70627 |
| Absorption | |
| Active Site | ACT_SITE 426; /note=Nucleophile; for NAALADase activity; /evidence=ECO:0000250; ACT_SITE 630; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 668; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 691; /note=Charge relay system; /evidence=ECO:0000255 |
| Activity Regulation | ACTIVITY REGULATION: The NAALADase activity is inhibited by beta-NAAG, quisqualic acid and 2-(phosphonomethyl)glutaric acid (PMG). |
| Binding Site | BINDING 212; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; BINDING 259; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; BINDING 426; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; BINDING 521; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q04609; BINDING 554; /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 both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides (By similarity). In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. {ECO:0000250}.; FUNCTION: Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (4); Binding site (5); Chain (1); Glycosylation (10); Metal binding (10); Modified residue (1); Region (5); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Calcium;Carboxypeptidase;Cell membrane;Dipeptidase;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Multifunctional enzyme;Phosphoprotein;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 | MOD_RES 10; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12876198; |
| Motif | |
| Gene Encoded By | |
| Mass | 84,540 |
| Kinetics | |
| Metal Binding | METAL 271; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 274; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 379; /note=Zinc 1; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 389; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 389; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 427; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 435; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 438; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 455; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 555; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q04609 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.21; |