IED ID | IndEnz0002018485 |
Enzyme Type ID | protease018485 |
Protein Name |
Glutamate carboxypeptidase 2 homolog EC 3.4.17.21 Glutamate carboxypeptidase II homolog |
Gene Name | gcp-2.1 CBG08178 |
Organism | Caenorhabditis briggsae |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis briggsae |
Enzyme Sequence | MPYVGVGAQKASTNLTGGPMMKAYAFVLAFFLLGLGVLALGKHHSGRRFNQYSKVSIDDIHETDAKTIQDNIKSENIKKYLRIFTQEPHIAGTDANKKVAYAIASAWTEAGLEDVHTLPYEVLLSYPDFENPNSVVIQNSAGKEIFRSKGVSPVIIPDEQSGKYAGHQWLAYGGNGTVSADVVYINRGNANDFKNLKLMGVDVKGKIALMRYGHGFRGDKVYKAQQAGAIGAILFSDTSDVAQDGVDSEHVYPKTIWMPNEGVQRGSLMHGDGDPLSPFYPSKKELFKGRTIEEAKDDGTLPSIPVLPVSYTTALQLLKRMSGRAVPSDWQGFVGGNLTYKLGPGFVNGEKLTINVHSELKTKRIRNVIGYIRGAEEPDRYIMLGNHFDAWVYGSIDPNSGTAVLAEVARAMMQTINETSWRPARTIVFNAWDAEEFGLIGSTEFVEEFVDVLQKRAVVYINMDCIQGNASLHVDTVPTLEHIAIEAAKHVPNPSKRERSRGRNTVYDTWMKVFPEKKAGRPKIRVPGGGSDHAPFLNFAGVPVINFNYKNYTTFDTYPLYHSMYETPFTNIHLMDTEDLAVHRAIGQYWAELAKTFADEVVLPMNTTNLASVMIKSYLPQLKASISGINVSRIDFESIRTQYALLSKSSQDLLVMSKKFQETMQFTFHSFSQNPYDAKHVNAVNERLISTERCFINPRGVSKHNPSARHVLFSVSDSDSYSNSLMAGIQNAIHSYETSPSKKNLREIINQISTVQYSVICVVNTLRDVI |
Enzyme Length | 770 |
Uniprot Accession Number | Q5WN23 |
Absorption | |
Active Site | ACT_SITE 435; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q04609 |
Activity Regulation | |
Binding Site | |
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; Evidence={ECO:0000250|UniProtKB:Q04609}; |
DNA Binding | |
EC Number | 3.4.17.21 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Glycosylation (7); Metal binding (6); Region (1); Topological domain (2); Transmembrane (1) |
Keywords | Carboxypeptidase;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 85,603 |
Kinetics | |
Metal Binding | METAL 387; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 397; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 397; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 436; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 464; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 562; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609 |
Rhea ID | |
Cross Reference Brenda |