| IED ID | IndEnz0002015772 |
| Enzyme Type ID | protease015772 |
| Protein Name |
Aminopeptidase NAALADL1 EC 3.4.11.- 100 kDa ileum brush border membrane protein I100 Ileal dipeptidylpeptidase N-acetylated-alpha-linked acidic dipeptidase-like protein NAALADase L |
| Gene Name | NAALADL1 NAALADASEL NAALADL |
| 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 | MQWTKVLGLGLGAAALLGLGIILGHFAIPKKANSLAPQDLDLEILETVMGQLDAHRIRENLRELSREPHLASSPRDEDLVQLLLQRWKDPESGLDSAEASTYEVLLSFPSQEQPNVVDIVGPTGGIIHSCHRTEENVTGEQGGPDVVQPYAAYAPSGTPQGLLVYANRGAEEDFKELQTQGIKLEGTIALTRYGGVGRGAKAVNAAKHGVAGVLVYTDPADINDGLSSPDETFPNSWYLPPSGVERGSYYEYFGDPLTPYLPAVPSSFRVDLANVSGFPPIPTQPIGFQDARDLLCNLNGTLAPATWQGALGCHYRLGPGFRPDGDFPADSQVNVSVYNRLELRNSSNVLGIIRGAVEPDRYVLYGNHRDSWVHGAVDPSSGTAVLLELSRVLGTLLKKGTWRPRRSIVFASWGAEEFGLIGSTEFTEEFFNKLQERTVAYINVDISVFANATLRVQGTPPVQSVVFSATKEIRSPGPGDLSIYDNWIRYFNRSSPVYGLVPSLGSLGAGSDYAPFVHFLGISSMDIAYTYDRSKTSARIYPTYHTAFDTFDYVDKFLDPGFSSHQAVARTAGSVILRLSDSFFLPLKVSDYSETLRSFLQAAQQDLGALLEQHSISLGPLVTAVEKFEAEAAALGQRISTLQKGSPDPLQVRMLNDQLMLLERTFLNPRAFPEERYYSHVLWAPRTGSVVTFPGLSNACSRARDTASGSEAWAEVQRQLSIVVTALEGAAATLRPVADL |
| Enzyme Length | 740 |
| Uniprot Accession Number | Q9UQQ1 |
| Absorption | |
| Active Site | ACT_SITE 416; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:25752612 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by bestatin. {ECO:0000269|PubMed:25752612}. |
| 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 (PubMed:25752612). Lacks carboxypeptidase activity. Lacks dipeptidyl-peptidase IV type activity (PubMed:25752612). {ECO:0000269|PubMed:25752612}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (11); Beta strand (30); Chain (1); Disulfide bond (1); Frameshift (1); Glycosylation (7); Helix (26); Metal binding (10); Mutagenesis (1); Natural variant (3); Sequence conflict (1); Topological domain (2); Transmembrane (1); Turn (9) |
| Keywords | 3D-structure;Alternative splicing;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 | X-ray crystallography (1) |
| Cross Reference PDB | 4TWE; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 80,558 |
| Kinetics | |
| Metal Binding | METAL 258; /note="Calcium"; /evidence="ECO:0000269|PubMed:25752612, ECO:0007744|PDB:4TWE"; METAL 261; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:25752612, ECO:0007744|PDB:4TWE"; METAL 368; /note="Zinc 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:25752612, ECO:0007744|PDB:4TWE"; METAL 378; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:25752612, ECO:0007744|PDB:4TWE"; METAL 378; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:25752612, ECO:0007744|PDB:4TWE"; METAL 417; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:25752612, ECO:0007744|PDB:4TWE"; METAL 425; /note="Calcium"; /evidence="ECO:0000269|PubMed:25752612, ECO:0007744|PDB:4TWE"; METAL 428; /note="Calcium"; /evidence="ECO:0000269|PubMed:25752612, ECO:0007744|PDB:4TWE"; METAL 445; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:25752612, ECO:0007744|PDB:4TWE"; METAL 545; /note="Zinc 2; via tele nitrogen"; /evidence="ECO:0000269|PubMed:25752612, ECO:0007744|PDB:4TWE" |
| Rhea ID | |
| Cross Reference Brenda |