| IED ID | IndEnz0002016128 |
| Enzyme Type ID | protease016128 |
| Protein Name |
Endoplasmic reticulum aminopeptidase 2 EC 3.4.11.- |
| Gene Name | ERAP2 |
| Organism | Bos taurus (Bovine) |
| 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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MANSCRKLIFNIYVVFYCSAVIMPQICICSQFTSSPIDQFNKDPKAFPVATNGEIFPWHELRLPTVVIPLHYDLLIHPNLTSLDFVASEKIEVLVRDATQFIILHSKDLEILNASLQSEEDVRYKKPGENLTVLSYPAHQQIALLVPEKLRAHLRYSVAIDFQAKLADGFEGFYKSTYRTLGGETRTIAVTDFEPTEARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVRMSTYLVAYIVCDFTSVSGTASSGVKVSIYASPDKWSQTHYALEASVKLLDFYENYFDIHYPLPKLDLVAIPDFASGAMENWGLITYRETSLLFDPKTSSTSDKLWVTKVIAHELAHQWFGNLVTMEWWNDIWLNEGFARYMELISLNITYPELQFDDSFSNTCFEVIKRDSLNSSHPISNEAKTATQIKEMFDAVSYNKGACILNMLKDFLSEETFRKGIIHYLKKFTYRNAKNDDLWHSLSNNCLEGDSTSGGFCYSDSRKTSNTLAFLRENVELKEMMATWTLQKGIPLVVVKREGRSLRLQQERFLSGVFKEDPEWGTLQERYLWHIPVTYSTSSSQAIHRHILKLKTDTVDLSEKTDWVKFNVDSSGYYIVHYEGQGWDELITLLNQNHTLLRPKDRLGLIHDAFQLVSAGRLTLDKALDLTRYLQHETSIPALLKGLEYLELFYRMVERRNISDVTENLKHYLLQYFKPVIDTQSWLDEGSVWDRMLRSTVLKLACYLNHAPCIQKATELFSQWMESSGKLNIPADVLTIVYSVGAQTTAGWNYLLEQYELSLSGAEKNKILYALSTSKHQEKLMKLIELGMEGKVIKTQDLATLLFTTARNPKGQQLAWNFVKENWTHLLKKFELGSFPIRMIISGTTSHFSSKDELQEVKLFFESLKAQGSHLDIFQIILETISKNIKWLEKNLPTLRKWLLTSI |
| Enzyme Length | 954 |
| Uniprot Accession Number | A6QPT7 |
| Absorption | |
| Active Site | ACT_SITE 365; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 194; /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. Preferentially hydrolyzes the basic residues Arg and Lys (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (4); Metal binding (3); Region (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 | - |
| Motif | |
| Gene Encoded By | |
| Mass | 109,719 |
| Kinetics | |
| Metal Binding | METAL 364; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 368; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 387; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |