3.4.11.3: cystinyl aminopeptidase
This is an abbreviated version!
For detailed information about cystinyl aminopeptidase, go to the full flat file.
Word Map on EC 3.4.11.3
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3.4.11.3
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envelope
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pregnancy
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cd4
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epitope
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lymphocyte
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angiotensin
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vaccinia
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viruses
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women
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aminopeptidases
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hiv-1-infected
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humoral
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t-cells
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virion
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simian
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macaque
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hiv-specific
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immunodominant
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nef
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seroconversion
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chimpanzee
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anti-hiv-1
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seronegative
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insipidus
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syncytium
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prime-boost
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furin
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vaccinees
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seropositive
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vaccine-induced
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glut4-containing
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hiv-seronegative
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desmopressin
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shiv
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ddavp
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hiv-1iiib
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anti-cd4
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intrarectal
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sivmac239
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medicine
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alum
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seroconverted
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1-infected
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non-neutralizing
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diagnostics
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oligosaccharyltransferase
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virus-neutralizing
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cross-neutralizing
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pharmacology
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coreceptors
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cross-presentation
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nephrogenic
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radioimmunoprecipitation
- 3.4.11.3
- envelope
- pregnancy
- cd4
- epitope
- lymphocyte
- angiotensin
- vaccinia
- viruses
- women
- aminopeptidases
-
hiv-1-infected
-
humoral
- t-cells
- virion
-
simian
- macaque
-
hiv-specific
-
immunodominant
- nef
- seroconversion
- chimpanzee
-
anti-hiv-1
-
seronegative
- insipidus
-
syncytium
-
prime-boost
- furin
-
vaccinees
-
seropositive
-
vaccine-induced
-
glut4-containing
-
hiv-seronegative
- desmopressin
- shiv
-
ddavp
-
hiv-1iiib
-
anti-cd4
-
intrarectal
-
sivmac239
- medicine
-
alum
-
seroconverted
-
1-infected
-
non-neutralizing
- diagnostics
-
oligosaccharyltransferase
-
virus-neutralizing
-
cross-neutralizing
- pharmacology
-
coreceptors
-
cross-presentation
-
nephrogenic
-
radioimmunoprecipitation
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 =
Synonyms
alpha-Aminoacyl-peptide hydrolase, aminopeptidase, cystyl, AT4 receptor, CAP, CAP-I, CAP-II, CysAP, cysteine aminopeptidase, cystine aminopeptidase, Cystinyl aminopeptidase, cystinylaminopeptidase, cystyl aminopeptidase, cystyl-aminopeptidase, GP160, insulin regulated aminopeptidase, insulin-regulated aminopeptidase, insulin-regulated aminopeptidase IRAP, Insulin-regulated membrane aminopeptidase, Insulin-responsive aminopeptidase, IRAP, IRAP/P-LAP, L-cystine aminopeptidase, LCAP, LeuAP, leucine aminopeptidase/oxytocinase, leucyl-aminopeptidase, leucyl-cystinyl aminopeptidase, LNPEP, M1 aminopeptidase, OTase, oxytocin peptidase, oxytocinase, oxytocinase/insulin-regulated aminopeptidase, oxytocinase/vasopressinase-like leucyl-cystinyl aminopeptidase LNPEP, P-LAP, P-LAP/IRAP, P-LAP/OTase, placental leucil aminopeptidase, Placental leucine aminopeptidase, placental leucine aminopeptidase/oxytocinase, placental leucine aminopeptidase/oxytocinase/insulin-regulated membrane aminopeptidase, vasopressinase, vasopresssinase, Vesicle protein of 165 kDa, Vp165, yscXVI
ECTree
3.4.11.3 cystinyl aminopeptidaseAdvanced search results
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results (Localization
Localization on EC 3.4.11.3 - cystinyl aminopeptidase
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LOCALIZATION 
ORGANISM
UNIPROT
COMMENTARY 
GeneOntology No.
LITERATURE
SOURCE
enzyme IRAP is localized in intracellular vesicles which can translocate to the cell membrane under insulin stimulation
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P-LAP is translocated from the cytosol to the plasma membrane by oxytocin stimulation in vascular endothelial cells and by vasopressin in renal cells
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insulin-stimulated translocation of IRAP remains intact despite substantial knock-down of glucose transporter GLUT4. By contrast, insulin-stimulated GLUT4 translocation is impaired upon IRAP knock-down. Tankyrase knock-down alters the basal partitioning of GLUT4 and IRAP within endosomal compartments
additional information
TUG regulates IRAP cell surface targeting in 3T3-L1 adipocytes
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TUG regulates IRAP cell surface targeting in 3T3-L1 adipocytes
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the enzyme translocates to the cell surface within GLUT4 vesicles in response to insulin
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GLUT4-containing; defects in the intracellular trafficking of P-LAP/IRAP-containing GLUT4 vesicle are associated with type 2 diabetes
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GLUT4-containing. Insulin-regulated aminopeptidase is a marker protein for specialized vesicles containing the insulin-responsive glucose transporter, GLUT4. The enzyme is thought to be involved in the tethering of GLUT4 vesicles to intracellular compartments
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GLUT4-containing; the enzyme colocalizes with GLUT4 in specific intracellular vesicles
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comparison of enzyme activity in membranes of COS-7 cells, HEK-293 cells, SK-N-MC cells, CHO-K1 cells and MDBK cells. Comparatively, CHO-K1 cells display the highest level of enzyme. In all cell types, the enzyme predominates over aminopeptidase N
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comparison of enzyme activity in membranes of COS-7 cells, HEK-293 cells, SK-N-MC cells, CHO-K1 cells and MDBK cells. Comparatively, CHO-K1 cells display the highest level of enzyme. In all cell types, the enzyme predominates over aminopeptidase N
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membrane-bound placental enzyme is released into maternal blood flow via proteolytic cleavage by metalloproteases and metalloproteinases
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the soluble form present in maternal serum is converted from the membrane-bound form in placenta by an enzyme with metalloprotease activity by posttranslational proteolytic cleavage between Phe154 and Ala155. P-LAP is translocated from the cytosol to the plasma membrane by oxytocin stimulation in vascular endothelial cells and by vasopressin in renal cells
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type III integral membrane protein, converted to a soluble form existing in maternal serum by metalloproteases
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comparison of enzyme activity in membranes of COS-7 cells, HEK-293 cells, SK-N-MC cells, CHO-K1 cells and MDBK cells. Comparatively, CHO-K1 cells display the highest level of enzyme. In all cell types, the enzyme predominates over aminopeptidase N
insulin-regulated aminopeptidase (IRAP) is a membrane-bound zinc metallopeptidase
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after exposure of 3T3-L1 adipocytes to insulin, IRAP translocates to the plasma membrane
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comparison of enzyme activity in membranes of COS-7 cells, HEK-293 cells, SK-N-MC cells, CHO-K1 cells and MDBK cells. Comparatively, CHO-K1 cells display the highest level of enzyme. In all cell types, the enzyme predominates over aminopeptidase N
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enzyme is enriched in low density microsome, and exhibits lower levels in high density microsomes. Co-localization with the vesicular marker VAMP2
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enzyme is enriched in low density microsome, and exhibits lower levels in high density microsomes. Co-localization with the vesicular marker VAMP2
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high (HDM) and low (LDM) density microsomal fractions. LDM consists of microsomes without ribosomes and with portions of endoplasmatic reticulum (ER) and fragments of Golgi apparatus. HDM consists of microsomes with ribosomes adhered to its outer surface. The inner side of microsomes is biochemically equivalent to the lumen of the ER
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high (HDM) and low (LDM) density microsomal fractions. LDM consists of microsomes without ribosomes and with portions of endoplasmatic reticulum (ER) and fragments of Golgi apparatus. HDM consists of microsomes with ribosomes adhered to its outer surface. The inner side of microsomes is biochemically equivalent to the lumen of the ER
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insulin induces a translocation of the enzyme from GLUT4 vesicles to plasma membrane by increasing the recycling rate
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translocated with GLUT4 to the plasma membrane unedr insulin stimulation
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the soluble form present in maternal serum is converted from the membrane-bound form in placenta by an enzyme with metalloprotease activity
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in adipose and muscle cells, insulin stimulates the exocytic translocation of vesicles containing GLUT4, a glucose transporter, and insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. TUG regulates IRAP cell surface targeting in 3T3-L1 adipocytes
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in adipose and muscle cells, insulin stimulates the exocytic translocation of vesicles containing GLUT4, a glucose transporter, and insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. TUG regulates IRAP cell surface targeting in 3T3-L1 adipocytes
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IRAP vesicles represent a IgE-sensitive exocytotic compartment in mast cells, which is regulated differently from secretory granules
enzyme IRAP is localized in intracellular vesicles which can translocate to the cell membrane under insulin stimulation
additional information
at the cellular level, IRAP immunoreactivity in neurons is associated with the trans-Golgi apparatus and vesicular structures in the proximity of the Golgi cisternae
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additional information
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at the cellular level, IRAP immunoreactivity in neurons is associated with the trans-Golgi apparatus and vesicular structures in the proximity of the Golgi cisternae
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