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 https://www.uniprot.org/uniprot/P79098.fasta
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.