ID:LCAP_HUMAN DESCRIPTION: RecName: Full=Leucyl-cystinyl aminopeptidase; Short=Cystinyl aminopeptidase; EC=3.4.11.3; AltName: Full=Insulin-regulated membrane aminopeptidase; AltName: Full=Insulin-responsive aminopeptidase; Short=IRAP; AltName: Full=Oxytocinase; Short=OTase; AltName: Full=Placental leucine aminopeptidase; Short=P-LAP; Contains: RecName: Full=Leucyl-cystinyl aminopeptidase, pregnancy serum form; FUNCTION: Release of an N-terminal amino acid, cleaves 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. CATALYTIC ACTIVITY: 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. COFACTOR: Binds 1 zinc ion per subunit (By similarity). SUBUNIT: Homodimer. Binds tankyrases 1 and 2. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Note=In brain only the membrane-bound form is found. The protein resides in intracellular vesicles together with GLUT4 and can then translocate to the cell surface in response to insulin and/or oxytocin. Localization may be determined by dileucine internalization motifs, and/or by interaction with tankyrases. SUBCELLULAR LOCATION: Leucyl-cystinyl aminopeptidase, pregnancy serum form: Secreted. Note=During pregnancy serum levels are low in the first trimester, rise progressively during the second and third trimester and decrease rapidly after parturition. TISSUE SPECIFICITY: Highly expressed in placenta, heart, kidney and small intestine. Detected at lower levels in neuronal cells in the brain, in skeletal muscle, spleen, liver, testes and colon. PTM: The pregnancy serum form is derived from the membrane-bound form by proteolytic processing. PTM: N-glycosylated. SIMILARITY: Belongs to the peptidase M1 family. SEQUENCE CAUTION: Sequence=BAA09436.1; Type=Erroneous initiation; Sequence=BAD92120.1; Type=Frameshift; Positions=405;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9UIQ6
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0000209 protein polyubiquitination GO:0002480 antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent GO:0006508 proteolysis GO:0007165 signal transduction GO:0007267 cell-cell signaling GO:0007565 female pregnancy GO:0008217 regulation of blood pressure GO:0030163 protein catabolic process GO:0043171 peptide catabolic process GO:0060395 SMAD protein signal transduction
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Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
