| IED ID | IndEnz0002015773 |
| Enzyme Type ID | protease015773 |
| Protein Name |
Aminopeptidase NAALADL1 EC 3.4.11.- N-acetylated-alpha-linked acidic dipeptidase-like protein NAALADase L |
| Gene Name | Naaladl1 Gm964 Naaladasel |
| 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 | MHWVKILGVALGAAALLGLGIILGHFAIPKATSPLTSSTSDSQDLDLAILDSVMGQLDASRIRENLRELSKEPHVATSPRDEALVQLLLGRWKDTATGLDSAKTYEYRVLLSFPNAEQPNSVEVVGPNGTTFHSFQPFEKNLTGEQAGPNVLQPYAAYAPPGTPKGLLVYANQGSEEDFKELETQGINLEGTIALTRYGGVGRGAKAINAAKHGVVGVLVYTDPGDINDGKSLPNETFPNSWRLPPSGVERGSYYEYFGDPLTPYLPAHPSSFRLDPHNTSGFPPIPTQPIGFEDARDLLCNLTGTSAPAFWQGALGCEYKLGPGFEPNGSFPAGSEVKVSVHNRLELRTSSNVLGIIQGAVEPDRYVIYGNHRDSWVHGAVDPSSGTAVLLEISRVLGTLLKKGTWRPRRSIIFASWGAEEFGLIGSTEFTEEFLSKLQERTVAYINVDISVFSNATLRAQGTPPVQSVIFSATKEISAPGSSGLSIYDNWIRYTNRTSPVYGLVPSLGTLGAGSDYAAFVHFLGITSMDLAYTYDRSKTSARIYPTYHTAFDTFDYVEKFLDPGFSSHQAVARTAGSVLLRLSDSLFLPLNVSDYSETLQSFLQAAQEALGTQLEKQNISLGPLVTAVANFKAAAASLGEHILTLQKSSPDPLQVRMVNDQLMLLERAFLNPRAFPEERHYSHVLWAPNTASVDTFPGLANAYAKAQEINSGSEAWAEVQRQLSIVVTALEGAAATLVPVADL |
| Enzyme Length | 745 |
| Uniprot Accession Number | Q7M758 |
| Absorption | |
| Active Site | ACT_SITE 421; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q9UQQ1 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Aminopeptidase with broad substrate specificity. Has lower activity with substrates that have Asp or Glu in the P2' position, or Pro in the P3' position. Lacks activity with substrates that have both Pro in the P3' position and Asp or Glu in the P2' position. Lacks carboxypeptidase activity. Lacks dipeptidyl-peptidase IV type activity. {ECO:0000250|UniProtKB:Q9UQQ1}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Glycosylation (10); Metal binding (10); Topological domain (2); Transmembrane (1) |
| Keywords | Aminopeptidase;Calcium;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:O54697}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O54697}. Note=Ileal brush border membrane. {ECO:0000250|UniProtKB:O54697}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000250|UniProtKB:O54697}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 17205597; 21267068; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,513 |
| Kinetics | |
| Metal Binding | METAL 263; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 266; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 373; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 383; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 383; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 422; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 430; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 433; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 450; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 550; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q9UQQ1 |
| Rhea ID | |
| Cross Reference Brenda |