| IED ID | IndEnz0002014214 |
| Enzyme Type ID | protease014214 |
| Protein Name |
Aminopeptidase N AP-N cAPN EC 3.4.11.2 Alanyl aminopeptidase Aminopeptidase M AP-M Microsomal aminopeptidase CD antigen CD13 |
| Gene Name | ANPEP |
| Organism | Canis lupus familiaris (Dog) (Canis familiaris) |
| 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 Laurasiatheria Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris) |
| Enzyme Sequence | MAKGFYISKALGILAIVLGIAAVSTIIALSVVYAQEKNKNAESSPVSSPVSSPVSSPVSPTNPSTTAATTLAQSKPWNHYRLPKTLIPSSYNVTLRPYLTPNSNGLYTFKGSSTVRFTCKESTSMIIIHSKKLNYTNIQGQRVALRGVGGSQAPAIDRTELVEVTEYLVVHLREPLQVNSQYEMDSKFEGELADDLAGFYRSEYTENGVKKVLATTQMQAADARKSFPCFDEPAMKATFNITLIHPSNLVALSNMLPRGPSVPFTEEPNWNVTEFETTPIMSTYLLAYIVSEFKNVQENTPSNVLIRIWARPSAMDQGHGNYALRVTGPILDFFSRHYDTPYPLNKSDQIALPDFNAGAMENWGLVTYRESALLYDPQSSSIGNKERVVTVIAHELAHQWFGNLVTLEWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLIVLNEVYRVMAVDALASSHPLSSPASEVNTPAQISEVFDSISYSKGASVLRMLSSFLTEDLFKKGVASYLHTFAYQNTIYLDLWNHLQWALGNQTAINLPYTVNAIMDRWILQMGFPVVTVDTTTGTLSQKHFLLDPQSNVTRPSKFNYLWIIPISSVKSGTQQAHYWMPDNAKVQNDLFKTTGDEWVLLNLNVTGYYLVNYDQNNWKKIHTQLQTDLSVIPVINRAQVIHDTFDLASAQIVPVTLALNSTLFLNQETEYMPWEAALSSLSYFKLMFDRSEVYGPMKNYLRKQVTPLFNHFEKITQNWTDHPQTLTEQYNEINAVSTACTYGVPKCKDLVSTLFAEWRKNPQNNPIYPNLRSTVYCNAIAQGGEEEWNFVWEQFRNTSLVNEADKLRSALACSTQVWILNRYLSYTLNPEFIRKQDVISTLSSIASNVIGQSLAWDFIQSNWKKLFEDYGTGSFSFSNLIQAVTRRFSTEFELQQLEQFKANNMDTGFGSGTRALEQALEKTKANIKWVKENKEAVLQWFRENSQ |
| Enzyme Length | 975 |
| Uniprot Accession Number | P79143 |
| Absorption | |
| Active Site | ACT_SITE 395; /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:0000250|UniProtKB:P15144}; |
| 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. May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization. May have a role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 and regulating its activity (By similarity). {ECO:0000250|UniProtKB:P15144, ECO:0000250|UniProtKB:P97449}.; FUNCTION: (Microbial infection) Probable receptor for canine coronavirus (CCoV). {ECO:0000269|PubMed:8985407}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Glycosylation (9); Metal binding (3); Modified residue (3); Region (4); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Aminopeptidase;Angiogenesis;Cell membrane;Developmental protein;Differentiation;Disulfide bond;Glycoprotein;Host cell receptor for virus entry;Host-virus interaction;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Receptor;Reference proteome;Signal-anchor;Sulfation;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15144}; 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 182; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 425; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 430; /note=Sulfotyrosine; /evidence=ECO:0000255 |
| Post Translational Modification | PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.; PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P15144}.; 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 | - |
| Motif | |
| Gene Encoded By | |
| Mass | 110,257 |
| Kinetics | |
| Metal Binding | METAL 394; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 398; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 417; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15144 |
| Rhea ID | |
| Cross Reference Brenda |