| IED ID | IndEnz0002016762 |
| Enzyme Type ID | protease016762 |
| Protein Name |
Aminopeptidase N AP-N hAPN EC 3.4.11.2 Alanyl aminopeptidase Aminopeptidase M AP-M Microsomal aminopeptidase Myeloid plasma membrane glycoprotein CD13 gp150 CD antigen CD13 |
| Gene Name | ANPEP APN CD13 PEPN |
| 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 | MAKGFYISKSLGILGILLGVAAVCTIIALSVVYSQEKNKNANSSPVASTTPSASATTNPASATTLDQSKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTCKEATDVIIIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLVVHLKGSLVKDSQYEMDSEFEGELADDLAGFYRSEYMEGNVRKVVATTQMQAADARKSFPCFDEPAMKAEFNITLIHPKDLTALSNMLPKGPSTPLPEDPNWNVTEFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLIRIWARPSAIAAGHGDYALNVTGPILNFFAGHYDTPYPLPKSDQIGLPDFNAGAMENWGLVTYRENSLLFDPLSSSSSNKERVVTVIAHELAHQWFGNLVTIEWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSTPASEINTPAQISELFDAISYSKGASVLRMLSSFLSEDVFKQGLASYLHTFAYQNTIYLNLWDHLQEAVNNRSIQLPTTVRDIMNRWTLQMGFPVITVDTSTGTLSQEHFLLDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDYWLIDVRAQNDLFSTSGNEWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQIINDAFNLASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSEVYGPMKNYLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSNGVPECEEMVSGLFKQWMENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAWEQFRNATLVNEADKLRAALACSKELWILNRYLSYTLNPDLIRKQDATSTIISITNNVIGQGLVWDFVQSNWKKLFNDYGGGSFSFSNLIQAVTRRFSTEYELQQLEQFKKDNEETGFGSGTRALEQALEKTKANIKWVKENKEVVLQWFTENSK |
| Enzyme Length | 967 |
| Uniprot Accession Number | P15144 |
| Absorption | |
| Active Site | ACT_SITE 389; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:22932899" |
| 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:22932899, ECO:0000269|PubMed:6149934, ECO:0000269|PubMed:7576235, ECO:0000269|PubMed:8887485}; |
| 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:P97449, ECO:0000269|PubMed:10605003, ECO:0000269|PubMed:10676659, ECO:0000269|PubMed:11384645, ECO:0000269|PubMed:12473585, ECO:0000269|PubMed:7576235, ECO:0000269|PubMed:8102610, ECO:0000269|PubMed:9056417}.; FUNCTION: (Microbial infection) Acts as a receptor for human coronavirus 229E/HCoV-229E. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. {ECO:0000269|PubMed:12551991, ECO:0000269|PubMed:1350662, ECO:0000269|PubMed:8887485, ECO:0000269|PubMed:9367365}.; FUNCTION: (Microbial infection) Mediates as well Human cytomegalovirus (HCMV) infection. {ECO:0000269|PubMed:8105105}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (32); Chain (1); Disulfide bond (2); Glycosylation (10); Helix (43); Initiator methionine (1); Metal binding (3); Modified residue (4); Mutagenesis (8); Natural variant (9); Region (5); Sequence conflict (2); Site (1); Topological domain (2); Transmembrane (1); Turn (11) |
| Keywords | 3D-structure;Aminopeptidase;Angiogenesis;Cell membrane;Developmental protein;Differentiation;Direct protein sequencing;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 | INDUCTION: Estradiol and IL8/interleukin-8 decrease enzymatic activity in vitro in endometrial stromal cells by 40% and 30%, respectively. {ECO:0000269|PubMed:11384645}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2564851, ECO:0000269|PubMed:9056417}; Single-pass type II membrane protein {ECO:0000305|PubMed:1350662}. Note=Also found as a soluble form. {ECO:0000269|PubMed:7902291}. |
| Modified Residue | MOD_RES 176; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 419; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 424; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 913; /note=Sulfotyrosine; /evidence=ECO:0000255 |
| Post Translational Modification | PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.; PTM: N- and O-glycosylated. {ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:1705556, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899, ECO:0000269|PubMed:9056417}.; PTM: May undergo proteolysis and give rise to a soluble form. {ECO:0000269|PubMed:7902291}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (11) |
| Cross Reference PDB | 4FYQ; 4FYR; 4FYS; 4FYT; 5LHD; 6ATK; 6U7E; 6U7F; 6U7G; 6XWD; 7AEW; |
| Mapped Pubmed ID | 11140838; 11774469; 11999577; 12406907; 12443882; 12634402; 12675232; 14507917; 14767532; 15166647; 15280478; 15687497; 15758076; 15812828; 15840518; 15883031; 15916720; 16216591; 16466852; 16469741; 16533817; 16685268; 16778789; 16818694; 17329256; 17363734; 17636545; 17655775; 17662271; 17803194; 17888402; 17897790; 17953966; 17999179; 18008160; 18085638; 18366676; 18431797; 18495788; 18605079; 18677709; 18794057; 19236378; 19330903; 19367725; 19373777; 19562339; 19597336; 1978675; 19908113; 20064928; 20360068; 20379614; 20689807; 20699358; 20711500; 21048031; 21376765; 21879266; 21881118; 22040956; 22065384; 22079983; 22307972; 22544935; 23206754; 23322201; 23488598; 23500679; 23643324; 23650620; 23677132; 24063007; 24411984; 24627994; 24991573; 25219368; 25246708; 25340499; 25461922; 25879366; 25885470; 25929234; 26208633; 26311161; 26449746; 26514774; 26655501; 26771355; 27467268; 28323433; 28387421; 28393915; 28708295; 28739875; 29048432; 29110838; 29145632; 29170370; 29789790; 30198568; 30994973; 31040262; 31056265; 31650956; 32249333; 32360796; 32457292; 32619880; 32938014; 33109610; 33778075; 34031489; 34349123; |
| Motif | |
| Gene Encoded By | |
| Mass | 109,540 |
| Kinetics | |
| Metal Binding | METAL 388; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:22932899, ECO:0007744|PDB:4FYQ, ECO:0007744|PDB:4FYR, ECO:0007744|PDB:4FYT"; METAL 392; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:22932899, ECO:0007744|PDB:4FYQ, ECO:0007744|PDB:4FYR, ECO:0007744|PDB:4FYT"; METAL 411; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:22932899, ECO:0007744|PDB:4FYQ, ECO:0007744|PDB:4FYR, ECO:0007744|PDB:4FYT" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.2; |