| IED ID | IndEnz0002014220 |
| Enzyme Type ID | protease014220 |
| Protein Name |
Aminopeptidase N AP-N mAPN EC 3.4.11.2 Alanyl aminopeptidase Aminopeptidase M AP-M Membrane protein p161 Microsomal aminopeptidase CD antigen CD13 |
| Gene Name | Anpep Lap-1 Lap1 |
| 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 | MAKGFYISKTLGILGILLGVAAVCTIIALSVVYAQEKNRNAENSATAPTLPGSTSATTATTTPAVDESKPWNQYRLPKTLIPDSYRVILRPYLTPNNQGLYIFQGNSTVRFTCNQTTDVIIIHSKKLNYTLKGNHRVVLRTLDGTPAPNIDKTELVERTEYLVVHLQGSLVEGRQYEMDSQFQGELADDLAGFYRSEYMEGDVKKVVATTQMQAADARKSFPCFDEPAMKAMFNITLIYPNNLIALSNMLPKESKPYPEDPSCTMTEFHSTPKMSTYLLAYIVSEFKNISSVSANGVQIGIWARPSAIDEGQGDYALNVTGPILNFFAQHYNTSYPLPKSDQIALPDFNAGAMENWGLVTYRESSLVFDSQSSSISNKERVVTVIAHELAHQWFGNLVTVAWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSSPADEIKTPDQIMELFDSITYSKGASVIRMLSSFLTEDLFKKGLSSYLHTYQYSNTVYLDLWEHLQKAVNQQTAVQPPATVRTIMDRWILQMGFPVITVNTNTGEISQKHFLLDSKSNVTRPSEFNYIWIAPIPFLKSGQEDHYWLDVEKNQSAKFQTSSNEWILLNINVTGYYLVNYDENNWKKLQNQLQTDLSVIPVINRAQIIHDSFNLASAKMIPITLALDNTLFLVKEAEYMPWQAALSSLNYFTLMFDRSEVYGPMKRYLKKQVTPLFFYFQNRTNNWVNRPPTLMEQYNEINAISTACSSGLKECRDLVVELYSQWMKNPNNNTIHPNLRSTVYCNAIAFGGEEEWNFAWEQFRNATLVNEADKLRSALACSKDVWILNRYLSYTLNPDYIRKQDTTSTIISIASNVAGHPLVWDFVRSNWKKLFENYGGGSFSFANLIQGVTRRFSSEFELQQLEQFKADNSATGFGTGTRALEQALEKTRANIDWVKENKDAVFKWFTENSS |
| Enzyme Length | 966 |
| Uniprot Accession Number | P97449 |
| Absorption | |
| Active Site | ACT_SITE 388; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; EC=3.4.11.2; Evidence={ECO:0000269|PubMed:8691132}; |
| DNA Binding | |
| EC Number | 3.4.11.2 |
| Enzyme Function | FUNCTION: Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines (By similarity). May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells (PubMed:8691132). May have a role in angiogenesis and promote cholesterol crystallization (By similarity). May have a role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 and regulating its activity (PubMed:22677001). {ECO:0000250|UniProtKB:P15144, ECO:0000269|PubMed:22677001, ECO:0000269|PubMed:8691132}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Glycosylation (13); Metal binding (3); Modified residue (4); Mutagenesis (4); Region (4); Sequence conflict (20); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Aminopeptidase;Angiogenesis;Cell membrane;Developmental protein;Differentiation;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Signal-anchor;Sulfation;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8805662}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15144}. Note=Also found as a soluble form. {ECO:0000250|UniProtKB:P15144}. |
| Modified Residue | MOD_RES 176; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 418; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 423; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 852; /note=Phosphotyrosine; /evidence=ECO:0007744|PubMed:17947660 |
| Post Translational Modification | PTM: N- and O-glycosylated. {ECO:0000269|PubMed:8805662}.; PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.; PTM: May undergo proteolysis and give rise to a soluble form. {ECO:0000250|UniProtKB:P15144}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11724556; 1203051; 12217325; 14610273; 14681479; 16081791; 16141072; 16615898; 16700521; 16990557; 17205597; 17360568; 17888402; 18346943; 18495788; 18554416; 20430777; 20489139; 21267068; 21339174; 2138915; 21708977; 21854845; 22307623; 22544935; 22723298; 22983824; 2304901; 23761403; 2393381; 23997214; 24297924; 24307555; 24627994; 24828040; 2512252; 2564851; 25801433; 26208633; 26514774; 26936360; 26952749; 27516371; 2792009; 28859152; 30104731; 31040262; 31056265; 314952; 31646784; 32369453; 32496646; 33505018; 33778075; 34031489; 3865183; 4040754; 6403543; 6735174; 6785912; 6929943; 6980942; 751643; |
| Motif | |
| Gene Encoded By | |
| Mass | 109,651 |
| Kinetics | |
| Metal Binding | METAL 387; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 391; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 410; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |