| IED ID | IndEnz0002019400 |
| Enzyme Type ID | protease019400 |
| Protein Name |
Endoplasmic reticulum aminopeptidase 2 EC 3.4.11.- Leukocyte-derived arginine aminopeptidase L-RAP |
| Gene Name | ERAP2 LRAP |
| 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 | MFHSSAMVNSHRKPMFNIHRGFYCLTAILPQICICSQFSVPSSYHFTEDPGAFPVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVPEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLKEGFAKYMELIAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSCLESDFTSGGVCHSDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNT |
| Enzyme Length | 960 |
| Uniprot Accession Number | Q6P179 |
| Absorption | |
| Active Site | ACT_SITE 371; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:22106953" |
| Activity Regulation | |
| Binding Site | BINDING 200; /note=Substrate; /evidence=ECO:0000269|PubMed:22106953 |
| 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. Preferentially hydrolyzes the basic residues Arg and Lys. {ECO:0000269|PubMed:12799365, ECO:0000269|PubMed:15908954, ECO:0000269|PubMed:16286653}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (5); Beta strand (39); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (5); Helix (41); Metal binding (3); Natural variant (4); Region (1); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1); Turn (6) |
| Keywords | 3D-structure;Adaptive immunity;Alternative splicing;Aminopeptidase;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:15691326, ECO:0000269|PubMed:15908954}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12799365}; Single-pass type II membrane protein {ECO:0000269|PubMed:12799365}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:12799365, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22106953}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 3SE6; 4E36; 4JBS; 5AB0; 5AB2; 5CU5; 5J6S; 5K1V; 6EA4; |
| Mapped Pubmed ID | 12436109; 12436110; 16054015; 17088086; 17129607; 18369178; 18393273; 19433412; 19578876; 20103633; 20419298; 20595269; 20711500; 20843824; 20976248; 21299892; 21314638; 21569342; 21719416; 22505422; 22837489; 23435305; 23545452; 23696916; 23988446; 24248368; 24928998; 24957906; 25142031; 25917849; 26088389; 26148615; 26381406; 26638075; 27110896; 27384923; 27514473; 27829666; 28029742; 28063628; 28083616; 28337326; 28759104; 29037997; 29108111; 29183862; 29324974; 29480940; 29769354; 29991817; 30446528; 30794838; 30933316; 31379846; 32210971; 32265295; 32321463; 32360304; 32847031; 32917832; 33309189; 33550689; 33619214; 33717175; 33762660; 34445292; 34727153; |
| Motif | |
| Gene Encoded By | |
| Mass | 110,462 |
| Kinetics | |
| Metal Binding | METAL 370; /note=Zinc; catalytic; METAL 374; /note=Zinc; catalytic; METAL 393; /note=Zinc; catalytic |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.1;3.4.11.6; |