| IED ID | IndEnz0002004227 |
| Enzyme Type ID | protease004227 |
| Protein Name |
Leucyl-cystinyl aminopeptidase Cystinyl aminopeptidase EC 3.4.11.3 GP160 Insulin-regulated membrane aminopeptidase Insulin-responsive aminopeptidase IRAP Oxytocinase OTase Placental leucine aminopeptidase P-LAP Vesicle protein of 165 kDa Vp165 |
| Gene Name | Lnpep Irap Otase |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | METFTNDRLQLPRNMIENSMFEEEPDVVDLAKEPCLHPLEPDEVEYEPRGSRLLVRGLGEHEMDEDEEDYESSAKLLGMSFMNRSSGLRNSATGYRQSPDGTCSVPSARTLVICVFVIVVAVSVIMVIYLLPRCTFTKEGCHKTNQSAELIQPIATNGKVFPWAQIRLPTAIIPQRYELSLHPNLTSMTFRGSVTISLQALQDTRDIILHSTGHNISSVTFMSAVSSQEKQVEILEYPYHEQIAVVAPESLLTGHNYTLKIEYSANISNSYYGFYGITYTDKSNEKKNFAATQFEPLAARSAFPCFDEPAFKATFIIKITRDEHHTALSNMPKKSSVPTEEGLIQDEFSESVKMSTYLVAFIVGEMRNLSQDVNGTLVSVYAVPEKIDQVYHALDTTVKLLEFYQNYFEIQYPLKKLDLVAIPDFEAGAMENWGLLTFREETLLYDNATSSVADRKLVTKIIAHELAHQWFGNLVTMQWWNDLWLNEGFATFMEYFSVEKIFKELNSYEDFLDARFKTMRKDSLNSSHPISSSVQSSEQIEEMFDSLSYFKGASLLLMLKSYLSEDVFQHAIILYLHNHSYAAIQSDDLWDSFNEVTGKTLDVKKMMKTWTLQKGFPLVTVQRKGTELLLQQERFFPSMQPEIQDSDTSHLWHIPISYVTDGRNYSEYRSVSLLDKKSDVINLTEQVQWVKVNTNMTGYYIVHYAHDGWAALINQLKRNPYVLSDKDRANLINNIFELAGLGKVPLQMAFDLIDYLRNETHTAPITEALFQTDLIYNLLEKLGHMDLSSRLVTRVHKLLQNQIQQQTWTDEGTPSMRELRSALLEFACAHSLENCTTMATKLFDGWMASNGTQSLPTDVMTTVFKVGARTEKGWLFLFSMYSSMGSEAEKDKILEALASSADAHKLYWLMKSSLDGDIIRTQKLSLIIRTVGRQFPGHLLAWDFVKENWNKLVHKFHLGSYTIQSIVAGSTHLFSTKTHLSEVQEFFENQSEATLQLRCVQEAFEVIELNIQWMARNLKTLTLWL |
| Enzyme Length | 1025 |
| Uniprot Accession Number | P97629 |
| Absorption | |
| Active Site | ACT_SITE 465; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 295; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Cys-|-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however.; EC=3.4.11.3; |
| DNA Binding | |
| EC Number | 3.4.11.3 |
| Enzyme Function | FUNCTION: Release of an N-terminal amino acid, cleave before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Glycosylation (17); Metal binding (3); Modified residue (4); Motif (2); Region (2); Sequence conflict (2); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Acetylation;Aminopeptidase;Cell membrane;Direct protein sequencing;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Endomembrane system; Single-pass type II membrane protein. Note=Localized mainly in intracellular vesicles together with GLUT4. Relocalizes to the plasma membrane in response to insulin. The dileucine internalization motif and/or the interaction with tankyrases may be involved in intracellular sequestration. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:Q9UIQ6; MOD_RES 70; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:Q8C129; MOD_RES 80; /note=Phosphoserine; by PKC/PRKCZ; in vitro; /evidence=ECO:0000269|PubMed:12061804; MOD_RES 91; /note=Phosphoserine; by PKC/PRKCZ; in vitro; /evidence=ECO:0000269|PubMed:12061804 |
| Post Translational Modification | PTM: N-glycosylated. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11282364; 11390024; 11489215; 11981039; 12709058; 15906313; 16343778; 16396496; 16420524; 16619500; 16771832; 16870704; 16967782; 17169335; 19468242; 20096929; 21207221; 26006037; 26311777; 27038740; 27881773; 28356324; 9224710; 9271094; |
| Motif | MOTIF 53..54; /note=Dileucine internalization motif; /evidence=ECO:0000255; MOTIF 76..77; /note=Dileucine internalization motif; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 117,201 |
| Kinetics | |
| Metal Binding | METAL 464; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 468; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 487; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.3; |