| IED ID | IndEnz0002014622 |
| Enzyme Type ID | protease014622 |
| Protein Name |
Endoplasmic reticulum aminopeptidase 1 EC 3.4.11.- ARTS-1 Adipocyte-derived leucine aminopeptidase A-LAP Aminopeptidase PILS Puromycin-insensitive leucyl-specific aminopeptidase PILS-AP VEGF-induced aminopeptidase |
| Gene Name | Erap1 Appils Arts1 |
| 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 | MPSLLPLVLTFLSVSSPSWCQNSDIESLKASNGDSFPWNNMRLPEYMTPIHYDLMIHANLSTLTFWGKTEVEIIASRPTSTIIMHSHHLQISKATLRRGAGEMLSEEPLKVLEYPAHEQVALLAAQPLLAGSLYTVIIDYAANLSESFHGFYKSTYRTQEGEMRILAATQFEPTAARMAFPCFDEPALKASFSIKIKRDPRHLAISNMPLVKSVNVAEGLIEDHFDITVKMSTYLVAFIISDFKSVSKMTKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFNIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESSLLYDKEKSSASSKLGITMIVSHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVTVTHPELKVEDYFFGKCFNAMEVDALNSSHPVSTPVENPAQIREMFDDVSYEKGACILNMLRDYLSADTFKRGIVQYLQKYSYKNTKNEDLWNSMMHICPTDGTQTMDGFCSRSQHSSSTSHWRQEVVDVKTMMNTWTLQKGFPLITITVSGRNVHMKQEHYMKGSERFPETGYLWHVPLTFITSKSDSVQRFLLKTKTDVLILPEAVQWIKFNVGMNGYYIVHYADDGWASLSGLLKEAHTTISSNDRASLINNAFQLVSIEKLSIEKALDLTLYLKNETEIMPIFQALNELIPMYKLMEKRDMIEVETQFKDFLLKLLKDLIDKQTWTDEGSVSERMLRSQLLLLACVRNYQPCVQRAERYFREWKSSNGNMSIPIDVTLAVFAVGAQNTEGWDFLYSKYQSSLSSTEKSQIEFSLCTSKDPEKLQWLLDQSFKGEIIKTQEFPHILTLIGRNPVGYPLAWKFLRENWNKLVQKFELGSSSIAHMVMGTTDQFSTRARLEEVKGFFSSLKENGSQLRCVQQTIETIEENIRWMDKNFDKIRLWLQKEKPELL |
| Enzyme Length | 930 |
| Uniprot Accession Number | Q9EQH2 |
| Absorption | |
| Active Site | ACT_SITE 343; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 172; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (6); Metal binding (3); Region (1); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Adaptive immunity;Aminopeptidase;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Immunity;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12368856; 12466851; 15187024; 16299505; 16505142; 16602821; 16615898; 16754858; 16824192; 17088086; 17128277; 17277129; 17385722; 18587399; 18941218; 20173027; 20562862; 21252114; 21267068; 21531727; 21572029; 21677750; 22522492; 23386199; 23610143; 23863903; 23894499; 24248368; 24504800; 24688025; 24857659; 25087231; 25422414; 25577645; 25959394; 27371725; 28108559; 28814066; 29559473; 29567213; 30127455; 30365037; 31341163; 31672933; |
| Motif | |
| Gene Encoded By | |
| Mass | 106,599 |
| Kinetics | |
| Metal Binding | METAL 342; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 346; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 365; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.22; |