| IED ID | IndEnz0002002612 |
| Enzyme Type ID | protease002612 |
| Protein Name |
Aminopeptidase O AP-O EC 3.4.11.- |
| Gene Name | Aopep Onpep |
| Organism | Mus musculus (Mouse) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MDIKLDPSRDDLPLMANTSHMLVKHYILDLDVDFGNQVIEGNIVLFFGDGNRFKNQSRSTQETFQMESEEADIFRTAEPCHVPEMDSSTFSPKMGHRECAVCGKGDQDAFDNDGNHDNQERDSEISSSKYCCDTGNHGKRDFLLVLDCCDLSVLKVEEVDVAAVPGLEKFTKAPKLLATPEKLRCEIVRDLVALPADAWREQLDCYTRCSQAPGCGELLIDSDNWSLRIRKTGTSTPADFPRAIRIWYKTKPEGQSVAWTTDQNGRPCVYTMGSPINNRALFPCQEPPVAMSTWQATVRAAASFVVLMSGENSAKPTPLREGYMSWHYYVTMPMPASTFAIAVGCWTEMKPKASPPDDLMTEHSLPLSPSEADLRYDNTCNHMEYPCRFQSASAASQDIIPYRVFAPVCLEGACQEALLWLIPSCLSAAHSVLGTHPFSRLDILIVPTNFPSLGMASPHIIFLSQSTLTGTSHLCGTRLCHEIAHSWFGLAIGARDWTEEWLSEGFATHLEDIFWAEAQQLPPHEALEQQELRACLRWHRLQDELRNSPEGMQVLRPNKEETGHVSASGASVVKHGLNPEKGFMQVHYLKGYFLLRFLTRTLGEKIYFPFLRKFVHLFHGQLILSQDFLQMLLENIPENKRLGLSVENIVRDWLECSGIPKALQEERKAEDCSPSRLARQVGSEVAKWIRVNRRPRKRKRGKREVAFEKLSPDQIVLLLEWLLEQKTLSPQTLHCLQQTYHLPEQDAEVRHRWCELVIKHKYTKAYNQVERFLLEDQAMGIYLYGELMVSEDARLQQLAHRCFELVKEHMDRASAQVVTEMLF |
| Enzyme Length | 823 |
| Uniprot Accession Number | Q8BXQ6 |
| Absorption | |
| Active Site | ACT_SITE 482; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P15144, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Aminopeptidase which catalyzes the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. {ECO:0000250|UniProtKB:P15144}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (2); Chain (1); Metal binding (3); Motif (1); Sequence caution (1); Site (1) |
| Keywords | Alternative splicing;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17803194}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305|PubMed:17803194}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 12904583; 14610273; 17967808; 18799693; 21267068; 21677750; 24194600; 25187367; 26849429; 27755984; 29275848; 33430468; |
| Motif | MOTIF 693..703; /note=Nucleolar localization signal; /evidence=ECO:0000269|PubMed:17803194 |
| Gene Encoded By | |
| Mass | 93,579 |
| Kinetics | |
| Metal Binding | METAL 481; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15144; METAL 485; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15144; METAL 504; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15144 |
| Rhea ID | |
| Cross Reference Brenda |