IED Industry Enzyme Database

Detail Information for IndEnz0002015770
IED ID IndEnz0002015770
Enzyme Type ID protease015770
Protein Name N-acetylated-alpha-linked acidic dipeptidase 2
EC 3.4.17.21
Glutamate carboxypeptidase III
GCPIII
N-acetylated-alpha-linked acidic dipeptidase II
NAALADase II
Gene Name NAALAD2
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MAESRGRLYLWMCLAAALASFLMGFMVGWFIKPLKETTTSVRYHQSIRWKLVSEMKAENIKSFLRSFTKLPHLAGTEQNFLLAKKIQTQWKKFGLDSAKLVHYDVLLSYPNETNANYISIVDEHETEIFKTSYLEPPPDGYENVTNIVPPYNAFSAQGMPEGDLVYVNYARTEDFFKLEREMGINCTGKIVIARYGKIFRGNKVKNAMLAGAIGIILYSDPADYFAPEVQPYPKGWNLPGTAAQRGNVLNLNGAGDPLTPGYPAKEYTFRLDVEEGVGIPRIPVHPIGYNDAEILLRYLGGIAPPDKSWKGALNVSYSIGPGFTGSDSFRKVRMHVYNINKITRIYNVVGTIRGSVEPDRYVILGGHRDSWVFGAIDPTSGVAVLQEIARSFGKLMSKGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKILQERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEIPSPDDGFESKSLYESWLEKDPSPENKNLPRINKLGSGSDFEAYFQRLGIASGRARYTKNKKTDKYSSYPVYHTIYETFELVEKFYDPTFKKQLSVAQLRGALVYELVDSKIIPFNIQDYAEALKNYAASIYNLSKKHDQQLTDHGVSFDSLFSAVKNFSEAASDFHKRLIQVDLNNPIAVRMMNDQLMLLERAFIDPLGLPGKLFYRHIIFAPSSHNKYAGESFPGIYDAIFDIENKANSRLAWKEVKKHISIAAFTIQAAAGTLKEVL
Enzyme Length 740
Uniprot Accession Number Q9Y3Q0
Absorption
Active Site ACT_SITE 414; /note=Nucleophile; for NAALADase activity; /evidence=ECO:0000250|UniProtKB:Q04609; 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 ACTIVITY REGULATION: Inhibited by quisqualate.
Binding Site BINDING 200; /note="Substrate"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; BINDING 247; /note="Substrate"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; BINDING 414; /note="Substrate"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; 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:10085079}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (4); Alternative sequence (2); Beta strand (26); Binding site (4); Chain (1); Glycosylation (7); Helix (26); Metal binding (10); Natural variant (2); Region (5); Topological domain (2); Transmembrane (1); Turn (4)
Keywords 3D-structure;Alternative splicing;Calcium;Carboxypeptidase;Cell membrane;Dipeptidase;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Multifunctional enzyme;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc
Interact With Q9UHD4; Q6NTF9-3; B2RUZ4; O76024
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 X-ray crystallography (4)
Cross Reference PDB 3FEC; 3FED; 3FEE; 3FF3;
Mapped Pubmed ID 11905994; 12204797; 14716746; 16467855; 20379614; 20711500; 22304711; 30844704; 34198725;
Motif
Gene Encoded By
Mass 83,592
Kinetics
Metal Binding METAL 259; /note="Calcium"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; METAL 262; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; METAL 367; /note="Zinc 1; via tele nitrogen; catalytic"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; METAL 377; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; METAL 377; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; METAL 415; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; METAL 423; /note="Calcium"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; METAL 426; /note="Calcium"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; METAL 443; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"; METAL 543; /note="Zinc 2; via tele nitrogen"; /evidence="ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
Rhea ID
Cross Reference Brenda