Detail Information for IndEnz0002019400
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;