| IED ID | IndEnz0002005225 |
| Enzyme Type ID | protease005225 |
| 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 Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator |
| Gene Name | ERAP1 APPILS ARTS1 KIAA0525 UNQ584/PRO1154 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTDGVKGMDGFCSRSQHSSSSSHWHQEGVDVKTMMNTWTLQKGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERM |
| Enzyme Length | 941 |
| Uniprot Accession Number | Q9NZ08 |
| Absorption | |
| Active Site | ACT_SITE 354; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 183; /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. {ECO:0000269|PubMed:15908954, ECO:0000269|PubMed:16286653, ECO:0000269|PubMed:21478864}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Beta strand (32); Binding site (1); Chain (1); Disulfide bond (2); Erroneous initiation (1); Glycosylation (5); Helix (39); Metal binding (3); Mutagenesis (1); Natural variant (10); Region (1); Sequence conflict (4); Site (1); Topological domain (2); Transmembrane (1); Turn (10) |
| Keywords | 3D-structure;Adaptive immunity;Alternative splicing;Aminopeptidase;Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Immunity;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | INDUCTION: By IFNG/IFN-gamma. {ECO:0000269|PubMed:15908954}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:15908954}; Single-pass type II membrane protein {ECO:0000305|PubMed:15908954}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:21478864, ECO:0000269|Ref.16}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (13) |
| Cross Reference PDB | 2YD0; 3MDJ; 3QNF; 3RJO; 5J5E; 6M8P; 6MGQ; 6Q4R; 6RQX; 6RYF; 6T6R; 7MWB; 7MWC; |
| Mapped Pubmed ID | 11857741; 12189246; 12368856; 12436109; 12436110; 12748171; 14662887; 15314084; 16054015; 16407280; 16585582; 17015730; 17088086; 17390085; 17952073; 17999179; 18393273; 18593381; 18987748; 19110536; 19202550; 19404951; 19414429; 19433412; 19463016; 19578876; 19581569; 19692350; 19828632; 19877036; 19913121; 19917163; 20032103; 20062062; 20103633; 20347630; 20367925; 20379614; 20419298; 20592285; 20595269; 20628086; 20711500; 20843824; 20953190; 21041274; 21068102; 21078719; 21229357; 21242517; 21281511; 21314638; 21362330; 21424381; 21508329; 21574996; 21833528; 21865284; 21877190; 22106953; 22253828; 22355701; 22466567; 22512642; 22632381; 22896742; 22918227; 22931917; 23264405; 23291587; 23452840; 23545452; 23656713; 23696916; 23733883; 23800305; 23864143; 23965983; 24028501; 24046467; 24223975; 24352655; 24504800; 24666027; 24928998; 25019531; 25142031; 25187574; 25354578; 25401226; 25422414; 25545008; 25591727; 25592150; 25665737; 25740711; 25817437; 25892735; 25994336; 26002026; 26097239; 26130142; 26146606; 26224046; 26321090; 26350268; 26360328; 26393469; 26399368; 26617903; 27095091; 27107845; 27108589; 27217550; 27514473; 27825049; 28049827; 28063628; 28083613; 28083616; 28161768; 28218509; 28446606; 28651467; 28746870; 28759104; 28814066; 28867178; 28901420; 29037997; 29108111; 29183862; 29278768; 29480940; 29632046; 29991817; 30144977; 30215709; 30313118; 30412714; 30461632; 30514861; 30518188; 30680818; 30740926; 30769005; 30794838; 30820838; 31097987; 31523044; 31601650; 31672933; 31711818; 31729751; 31790864; 31843903; 31873220; 32023277; 32109056; 32161166; 32184355; 32210971; 32239976; 32321463; 32647953; 32824160; 33216288; 33309189; 33617882; 33651148; 33762660; 33794716; 34247019; 34389743; 34395615; 34489420; 34580106; 34688668; 34727153; |
| Motif | |
| Gene Encoded By | |
| Mass | 107,235 |
| Kinetics | |
| Metal Binding | METAL 353; /note=Zinc; catalytic; METAL 357; /note=Zinc; catalytic; METAL 376; /note=Zinc; catalytic |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.1;3.4.11.22; |