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Information on EC 3.4.17.1 - carboxypeptidase A and Organism(s) Mus musculus and UniProt Accession Q5U901
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3.4.17.1 carboxypeptidase ASpecify your search results
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- 3.4.17.1
- agonist
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cerebellopontine
- cyclophosphamide
-
cyclopiazonic
- nerve
- artery
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cyproterone
- pulmonary
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n6-cyclopentyladenosine
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cryoprotective
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cryopreservation
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resect
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postoperative
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hearing
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facial
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sarcoplasmic
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cranial
- aspergillosis
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vestibular
- schwannomas
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aversion
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auditory
- meningioma
- ca2+-atpase
- dpcpx
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cardiopulmonary
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preoperative
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acoustic
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antiandrogenic
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vitrification
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fossa
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resuscitation
- rantes
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ryanodine
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ca2+-free
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craniotomy
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epidermoids
- chymase
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- hirsutism
- neuralgia
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post-thawing
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- 2-chloroadenosine
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radiosurgery
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mip-1beta
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hemifacial
- pharmacology
- drug development
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out-of-hospital
- biotechnology
- medicine
- analysis
- synthesis
- food industry
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cpa, carboxypeptidase a, mcp-2, mc-cpa, carboxypeptidase a1, carboxypeptidase a3, carboxypeptidase-a, mast cell carboxypeptidase a, carboxypeptidase a4, mecpa, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Carboxypeptidase A3
-
-
-
-
carboxypolypeptidase
-
-
-
-
MC-CPA
RMC-CP
-
-
-
-
MC-CPA
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
11075-17-5
-
9031-98-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
angiotensin I + H2O
angiotensin II + His-Leu
-
shown in an ex vivo system of peritoneal exudates cells
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cd2+
-
decreases carboxypeptidase A activity probably due to the direct inhibition by the metal
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
proteoglycan
-
there is evidence indicating that the processing of pro-MC-CPA into active protease is dependent on proteoglycan
-
additional information
-
infection with Ptf1a-expressing adenovirus vector induces the expression of the gene for carboxypeptidase in Pdx-1-positive pancreatic duct-derived (PPPD) cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
low expression levels in cingulate cortex, lateral septum, pontine nucleus, and inferior olivary nucleus
high CPA6 expression level, enriched in the mitral and granular layers
additional information
-
granulated mast cell derived from undifferentiated mast cells by treatment 2 monoclonal antibodies, mAb-AA4 and mAb-BGD6
additional information
tissue distribution of carboxypeptidase A-6, in situ hybridization, overview
additional information
-
tissue distribution of carboxypeptidase A-6, in situ hybridization, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
the mast cell CPA is activated by proteolytic cleavage of the pro-enzyme by cathepsins B, L, D, and E, overview
proteolytic modification
-
cleavage of the signal peptide and subsequent cleavage of the propeptide results in the formation of the mature enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E378A
-
Glu378 is crucial for ligand binding and hydrolysis of substrate peptide bond
Y356L
-
Tyr356 is crucial for ligand binding and hydrolysis of substrate peptide bond
Y356L/E378A
-
mutant expresses about 80% of the amount of Mc-cpa compared to the wild type enzyme, the mutant enzyme lacks activity
additional information
additional information
-
mice lacking Nna1/CCP1 show absence of the detyrosinylated form of alpha-tubulin in mitral cells
additional information
-
in agiotensin-converting enzyme -/- mice the addition of the carboxypeptidase A inhibitor benzylsuccinate essentially abolishs the formation of Ang(1-9) and increases the levels of angiotensin I in cardiac membranes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged pro-enzyme in Escherichia coli and in HEK293 cells also expressing the Epstein Barr virus nuclear antigen 1, induction by A23187
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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mc-CPA is an essential effector molecule providing a very rapid and life-saving response of toxin neutralization in vivo
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Serafin, W.E.; Dayton, E.T.; Gravallese, P.M.; Austen, K.F.; Stevens, R.L.
Carboxypeptidase A in mouse mast cells. Identification, characterization, and use as a differentiation marker
J. Immunol.
139
3771-3776
1987
Mus musculus
Shimada, H.; Funakoshi, T.; Waalkes, M.P.
Acute, nontoxic cadmium exposure inhibits pancreatic protease activities in the mouse
Toxicol. Sci.
53
474-480
2000
Mus musculus
Jamur, M.C.; Grodzki, A.C.; Berenstein, E.H.; Hamawy, M.M.; Siraganian, R.P.; Oliver, C.
Identification and characterization of undifferentiated mast cells in mouse bone marrow
Blood
105
4282-4289
2005
Mus musculus
Fontenele-Neto, J.D.; Kalinina, E.; Feng, Y.; Fricker, L.D.
Identification and distribution of mouse carboxypeptidase A-6
Brain Res. Mol. Brain Res.
137
132-142
2005
Mus musculus (Q5U901), Mus musculus
Henningsson, F.; Yamamoto, K.; Saftig, P.; Reinheckel, T.; Peters, C.; Knight, S.D.; Pejler, G.
A role for cathepsin E in the processing of mast-cell carboxypeptidase A
J. Cell Sci.
118
2035-2042
2005
Mus musculus
Garabelli, P.J.; Modrall, J.G.; Penninger, J.M.; Ferrario, C.M.; Chappell, M.C.
Distinct roles for angiotensin-converting enzyme 2 and carboxypeptidase A in the processing of angiotensins within the murine heart
Exp. Physiol.
93
613-621
2008
Mus musculus
Schneider, L.A.; Schlenner, S.M.; Feyerabend, T.B.; Wunderlin, M.; Rodewald, H.R.
Molecular mechanism of mast cell mediated innate defense against endothelin and snake venom sarafotoxin
J. Exp. Med.
204
2629-2639
2007
Mus musculus
Pejler, G.; Aabrink, M.; Ringvall, M.; Wernersson, S.
Mast cell proteases
Adv. Immunol.
95
167-255
2007
Homo sapiens, Mus musculus, Rattus norvegicus
Braga, T.; Grujic, M.; Lukinius, A.; Hellman, L.; Abrink, M.; Pejler, G.
Serglycin proteoglycan is required for secretory granule integrity in mucosal mast cells
Biochem. J.
403
49-57
2007
Mus musculus
Yamamoto, T.; Yamato, E.; Taniguchi, H.; Shimoda, M.; Tashiro, F.; Hosoi, M.; Sato, T.; Fujii, S.; Miyazaki, J.
Stimulation of cAMP signaling allows isolation of clonal pancreatic precursor cells from adult mouse pancreas
Diabetologia
49
2359-2367
2006
Mus musculus
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