Search by BoMiProt ID - Bomi3858


Primary Information

BoMiProt ID Bomi3858
Protein Name Aminopeptidase N/Alanyl aminopeptidase/Microsomal aminopeptidase/CD_antigen: CD13
Organism Bos taurus
Uniprot IDP79098
Milk FractionExosomes
Ref Sequence ID NP_001068612.1
Aminoacid Length 965
Molecular Weight 109276
FASTA Sequence Download
Gene Name ANPEP
Gene ID 404191
Protein Existence Status Reviewed

Secondary Information

Protein Function CD13 regulates activities of numerous cytokines by cleaving their N-terminals and is involved in Ag processing by trimming the peptides bound to MHC class II. 
Biochemical Properties CD13, also known as aminopeptidase N or membrane alanyl aminopeptidase, is a type II membrane 150kDa metalloprotease with an extracellular oriented catalytic domain.It is a seahorse-shaped molecule and usually forms a head-to-head homodimer by means of hydrophobic interactions.Each monomeric molecule of CD13 possesses a 7-domain organization, which is characteristic of M1 metallopeptidases.
PTMs Disulfide bond formation,N-Linked Glycosylation at Asn, Sulfation at Tyr
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P79098|AMPN_BOVIN Aminopeptidase N OS=Bos taurus OX=9913 GN=ANPEP PE=2 SV=4 MAKGFYISKALGILAILLGVAAVATIIALSVVYAQEKNKNAERGTAAPTSPTGPTTTSAT TLDQSKPWNRYRLPTTLLPDSYRVTLRPYLTPNNNGLYIFTGSSTVRFTCKEPTDVIIIH SKKLN*125YTQHSGHLAALKGVGDTQAPEIDRTELVLLTEYLVVHLKSSLEAGKTYEMETTFQ GELADDLAGFYRSEYMDGNVKKVLATTQMQSTDARKSFPCFDEPAMKATFN*231ITLIHPKDL TALSNMPPKGPSVPFDGDSN*260WSVTEFETTPVMSTYLLAYIVSEFTSVESVAPNDVQIRIW ARPKATADNHGLYALN*316VTGPILNFFANHYNTAYPLPKSDQIALPDFNAGAMENWGLVTYR ENALLYDPQSSSSSNKERVVTVIAHELAHQWFGNLVTLAWWNDLWLNEGFASYVEYLGAD YAEPTWNLKDLMVPNDVYSVMAVDALVTSHPLTTPANEVNTPAQISEMFDTISYSKGASV IRMLSNFLTEDLFKKGLASYLQTFAYQN*508TTYLNLWEHLQMAVENQLSIRLPDTVSAIMDR WTLQMGFPVITVDTNTGTISQKHFLLDPN*569STVTRPSQFNYLWIVPISSIRNGQPQEHYWL RGEERNQNELFKAAADDWVLLNIN*624VTGYYQVNYDENNWKKIQNQLMSRRENIPVINRAQV IYDSFNLASAHMVPVTLALN*680NTLFLKNEMEYMPWQAAVSSLNYFKLMFDRTEVYGPMQNY LKNQVEPIFLYFEN*734LTKN*738WTEIPENLMDQYSEINAISTACSNGLPKCEELAKTLFNQWMN NPNVNPIDPNLRSTIYCNAIAQGGQEEWDFAWNQLQQAELVNEADKLRSALACTNHVWLL NRYLSYTLNPDLIRKQDATSTITSIASNVIGQSLAWDFIRSNWKKLFEDYGGGSFSFSNL IQGVTRRFSTEFELQQLEEFKENNMDVGFGSGTRALEQALEKTKANINWVKENKEVVLNW FKDHS
Predicted Disorder Regions (41-65)
DisProt Annotation
TM Helix Prediction 1TMH;(11-33)
Significance of PTMs May undergo proteolysis and give rise to a soluble form.
Bibliography 1.Lu C, Amin MA, Fox DA. CD13/Aminopeptidase N Is a Potential Therapeutic Target for Inflammatory Disorders. J Immunol. 2020 Jan 1;204(1):3-11. doi: 10.4049/jimmunol.1900868. PMID: 31848300; PMCID: PMC6997018. 2. Wong AH, Zhou D, and Rini JM. 2012. The X-ray crystal structure of human aminopeptidase N reveals a novel dimer and the basis for peptide processing. J. Biol. Chem 287: 36804–36813.3.Chen L, Lin Y, Peng G, and Li F. 2012. Structural basis for multifunctional roles of mammalian aminopeptidase N. Proc. Natl. Acad. Sci. U. S. A 109: 17966–17971. 4.Sjöström H, Norén O, and Olsen J. 2000. Structure and function of aminopeptidase N. Adv. Exp. Med. Biol 477: 25–34.