Primary Information |
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| BoMiProt ID | Bomi3858 |
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| Protein Name | Aminopeptidase N/Alanyl aminopeptidase/Microsomal aminopeptidase/CD_antigen: CD13 |
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| Organism | Bos taurus |
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| Uniprot ID | P79098 |
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| Milk Fraction | Exosomes |
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| Ref Sequence ID | NP_001068612.1 |
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| Aminoacid Length | 965 |
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| Molecular Weight | 109276 |
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| FASTA Sequence |
Download |
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| Gene Name | ANPEP |
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| Gene ID | 404191 |
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| Protein Existence Status | Reviewed |
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Secondary Information |
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| 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. |
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| 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. |
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| PTMs | Disulfide bond formation,N-Linked Glycosylation at Asn, Sulfation at Tyr |
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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
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| Predicted Disorder Regions | (41-65) |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH;(11-33) |
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| Significance of PTMs | May undergo proteolysis and give rise to a soluble form. |
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| 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. |
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