Detail Information for IndEnz0002016757
IED ID IndEnz0002016757
Enzyme Type ID protease016757
Protein Name Aminopeptidase N
AP-N
bAPN
EC 3.4.11.2
Alanyl aminopeptidase
Aminopeptidase M
AP-M
Microsomal aminopeptidase
CD antigen CD13
Gene Name ANPEP APN
Organism Bos taurus (Bovine)
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 Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MAKGFYISKALGILAILLGVAAVATIIALSVVYAQEKNKNAERGTAAPTSPTGPTTTSATTLDQSKPWNRYRLPTTLLPDSYRVTLRPYLTPNNNGLYIFTGSSTVRFTCKEPTDVIIIHSKKLNYTQHSGHLAALKGVGDTQAPEIDRTELVLLTEYLVVHLKSSLEAGKTYEMETTFQGELADDLAGFYRSEYMDGNVKKVLATTQMQSTDARKSFPCFDEPAMKATFNITLIHPKDLTALSNMPPKGPSVPFDGDSNWSVTEFETTPVMSTYLLAYIVSEFTSVESVAPNDVQIRIWARPKATADNHGLYALNVTGPILNFFANHYNTAYPLPKSDQIALPDFNAGAMENWGLVTYRENALLYDPQSSSSSNKERVVTVIAHELAHQWFGNLVTLAWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLMVPNDVYSVMAVDALVTSHPLTTPANEVNTPAQISEMFDTISYSKGASVIRMLSNFLTEDLFKKGLASYLQTFAYQNTTYLNLWEHLQMAVENQLSIRLPDTVSAIMDRWTLQMGFPVITVDTNTGTISQKHFLLDPNSTVTRPSQFNYLWIVPISSIRNGQPQEHYWLRGEERNQNELFKAAADDWVLLNINVTGYYQVNYDENNWKKIQNQLMSRRENIPVINRAQVIYDSFNLASAHMVPVTLALNNTLFLKNEMEYMPWQAAVSSLNYFKLMFDRTEVYGPMQNYLKNQVEPIFLYFENLTKNWTEIPENLMDQYSEINAISTACSNGLPKCEELAKTLFNQWMNNPNVNPIDPNLRSTIYCNAIAQGGQEEWDFAWNQLQQAELVNEADKLRSALACTNHVWLLNRYLSYTLNPDLIRKQDATSTITSIASNVIGQSLAWDFIRSNWKKLFEDYGGGSFSFSNLIQGVTRRFSTEFELQQLEEFKENNMDVGFGSGTRALEQALEKTKANINWVKENKEVVLNWFKDHS
Enzyme Length 965
Uniprot Accession Number P79098
Absorption
Active Site ACT_SITE 386; /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}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Compositional bias (1); Disulfide bond (2); Glycosylation (10); Metal binding (3); Modified residue (2); 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;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 173; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 416; /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 109,276
Kinetics
Metal Binding METAL 385; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 389; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 408; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Rhea ID
Cross Reference Brenda