| IED ID | IndEnz0002003307 |
| Enzyme Type ID | protease003307 |
| 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 | Sus scrofa (Pig) |
| 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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MWNPLHETDSTSVAWRRPRWLCAGALVLAAGLFVLGFLFGWFIKSPNEAANISPQHNVKKAFLDELKAENIKTFLYNFTRIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTRPNYISIIDEDGNEIFNTSLFEPPPPGYENVSDVVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKILIARYGKIFRGNKVKNAQLAGAKGIILYSDPADYFAPGVQSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRLQIAEAVGLPRIPVHPIGYSDAQKLLEKMGGSAPPDDSWKGSLHVPYNVGPGFTGNFSTQKVKMHIHSDNKVKRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGKLKKEGWRPRRTVLFASWDAEEYGLFGSTEWAEENSRILQERGVAYINADSSIEGNYTLRVDCTPLMYSLVYNLTKELQSPDEGFEGKSLFESWNEKSPSPEFSGLPRISKLGSGNDFEVFFQRLGIASGRARYTKDWVTNKFSSYPLYHSVYETYELVEKFYDPTFKYHLAVAQVRGGIVFELANSVVRPFDCRDYAVVLRNYADKLYNISMNHPQEMKAYSVSFDSLFSAVKNFTEIASNFSERVQDLDKNNPILLRIMNDQLMFLERAFIVPLGLPDRAFYRHVIYAPSSHNKYMGESFPGIYDALFDIENKVDPSKAWGEVKRQISIAAFTVQAAAGTLREVA |
| Enzyme Length | 751 |
| Uniprot Accession Number | O77564 |
| Absorption | |
| Active Site | ACT_SITE 425; /note=Nucleophile; for NAALADase activity; /evidence=ECO:0000250; ACT_SITE 629; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 667; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 690; /note=Charge relay system; /evidence=ECO:0000255 |
| Activity Regulation | ACTIVITY REGULATION: The NAALADase activity is inhibited by quisqualic acid, beta-NAAG and 2-(phosphonomethyl) pentanedioic acid (PMPA). Ethanol ingestion decreases the folate hydrolase activity by 50%. |
| Binding Site | BINDING 211; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; BINDING 258; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; BINDING 425; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; BINDING 520; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q04609; BINDING 553; /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 | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (4); Binding site (5); Chain (1); Glycosylation (12); Metal binding (10); Modified residue (1); Region (5); Topological domain (2); Transmembrane (1) |
| Keywords | Calcium;Carboxypeptidase;Cell membrane;Dipeptidase;Direct protein sequencing;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:0000250|UniProtKB:P70627 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 84,524 |
| Kinetics | |
| Metal Binding | METAL 270; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 273; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 378; /note=Zinc 1; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 388; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 388; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 426; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 434; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 437; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 454; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 554; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q04609 |
| Rhea ID | |
| Cross Reference Brenda |