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Information on EC 3.4.22.52 - calpain-1 and Organism(s) Sus scrofa and UniProt Accession P35750

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.52 calpain-1
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This record set is specific for:
Sus scrofa
UNIPROT: P35750 not found.
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Word Map
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
broad endopeptidase specificity
Synonyms
mu-calpain, calpain-1, calpain i, capn1, calpain 1, capn2, micro-calpain, capns1, calpain1, calpain-i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
calpain 1A
calpain 1 catalytic subunit
calcium-activated neutral protease I
-
-
-
-
calpain 1
calpain I
-
-
-
-
CAPN1
-
-
CAPN1 g.p. (Homo sapiens)
-
-
-
-
EC 3.4.22.17
-
formerly
micro-calpain
mu-calpain
muCANP
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
689772-75-6
-
78990-62-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
-
-
-
?
Bax protein + H2O
?
show the reaction diagram
-
-
-
-
?
Bfl-1 protein + H2O
?
show the reaction diagram
-
mu-calpain cleaves Bfl-1 at two major sites in its N-terminus releasing three fragments of 28000 Da, 12000 Da and 17500 Da
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
COX-2 + H2O
?
show the reaction diagram
-
-
-
-
?
microtubule-associated protein 1
?
show the reaction diagram
-
-
-
-
?
myofibrillar protein + H2O
?
show the reaction diagram
-
-
-
-
?
NR2 subunit of NMDA subtype of glutamate receptor + H2O
?
show the reaction diagram
-
all three subtypes of NR2 subunits can be proteolyzed, cleavage of NR2A, NR2B and NR2C subunits is limited to their C-terminal region. Two cleavage sites at amino acids 1279 and 1330. Cleavage of NR2A-containing receptors does not alter basic NMDA receptor properties including calcium uptake, MK801 binding or electrophysiological measurement
-
-
?
recombinant procaspase-3 + H2O
?
show the reaction diagram
-
-
-
-
?
recombinant procaspase-9 + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
titin + H2O
?
show the reaction diagram
-
pH 7.5, absence or presence of 12 microM calcium
-
-
?
troponin + H2O
?
show the reaction diagram
-
-
-
-
?
[4-((4-(dimethylamino)phenyl)azo)benzoic acid, succinimidyl ester]-Thr-Pro-Leu-Lys-Ser-Pro-Pro-Pro-Ser-Pro-Arg-[5-((2-aminoethyl)amino)naphthalene-1-sulfonic acid] + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
recombinant procaspase-3 + H2O
?
show the reaction diagram
-
-
-
-
?
recombinant procaspase-9 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
calpastatin
-
-
([(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]oxy)ethynyl (2Z)-[(3R)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
-
-
benzyl (2Z)-[(3S)-3-sec-butyl-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetate
-
-
calpastatin
-
carbobenzoxy-valinyl-phenylalaninal
-
-
DPMSSTYIEELGKREVTIPPKYRELLA
-
2 hot spots are detected in which the residues critical for inhibitory function are clustered: Leu11-Gly12 and Thr17-Ile18-Pro19
EDTA
-
-
leupeptin
-
-
MDL-28170
-
-
methyl (2Z)-[(3S)-3-sec-butyl-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetate
-
-
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-isoleucyl-L-isoleucinate
-
-
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-isoleucyl-L-isoleucyl-L-isoleucinate
-
-
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-leucyl-L-phenylalaninate
-
-
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-valyl-L-phenylalaninate
-
-
N-[(1S)-1-benzyl-2-oxoethyl]-N2-[(benzyloxy)carbonyl]-L-leucinamide
-
-
NaCl
-
mu-calpain is more active at 165 mM NaCl than at 295 mM NaCl
PD150606
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
59
([(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]oxy)ethynyl (2Z)-[(3R)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
Sus scrofa
-
-
85
benzyl (2Z)-[(3S)-3-sec-butyl-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetate
Sus scrofa
-
-
0.000025
methyl (2Z)-[(3S)-3-sec-butyl-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetate
Sus scrofa
-
-
0.000447
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-isoleucyl-L-isoleucinate
Sus scrofa
-
-
0.000159
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-isoleucyl-L-isoleucyl-L-isoleucinate
Sus scrofa
-
-
0.000066
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-leucyl-L-phenylalaninate
Sus scrofa
-
-
0.000626
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-valyl-L-phenylalaninate
Sus scrofa
-
-
0.00024
N-[(1S)-1-benzyl-2-oxoethyl]-N2-[(benzyloxy)carbonyl]-L-leucinamide
Sus scrofa
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
mu-calpain
7.3
-
monomeric calpain I
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
mü-calpain
6.5 - 8
-
pH 6.5: about 35% of maximal activity, pH 8.0: about 50% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
dramatic muscle growth during the neonatal period may be partially controlled by down-regulated calpain-calpastatin system
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAN1_PIG
714
0
81739
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
80000
-
x * 80000
83000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 80000
dimer
heterodimer
-
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the 70000 Da monomeric calpain I is less pH stable than the parent heterodimeric calpain I
643981
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the 70000 Da monomeric calpain I is much less heat stable than the parent heterodimeric calpain I
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
large scale
-
mu-calpain
-
partial
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 289 bp fragment for mu-calpain is cloned into the EcoRV site of pBluescript II KS+ vector
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the steady-state mRNA level of calpain 1A decreases by 2-4fold at the age of 4 to 6 days compared to 1-day-old piglets. Expressions of calpain 1A is negatively correlated with birth weight and fractional rate of growth, decreased levels of calpain 1A expressions over development in neonatal pigs are associated with high protein accumulations
at 24 h postmortem the activity of the native mu-calpain decreases. A faster decrease in pH results in reduced level of mu-calpain activity and increased autolysis of the enzyme
-
low nutritional level diet treatment increases mRNA level of micro-calpain in skeletal muscle
-
Protein Never in Mitosis Gene A Interacting-1 reduces calpain activity and slows the degradation of COX-2 in MAEC cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sun, W.; Ji, S.Q.; Ebert, P.J.; Bidwell, C.A.; Hancock, D.L.
Cloning the partial cDNAs of mu-calpain and m-calpain from porcine skeletal muscle
Biochimie
75
931-936
1993
Sus scrofa (P35750), Sus scrofa
Manually annotated by BRENDA team
Fukui, I.; Toyohara, H.; Ito, K.; Hamakubo, T.; Murachi, T.
Molecular and catalytic characterization of intact heterodimeric and derived monomeric calpains isolated under different conditions from pig polymorphonuclear leukocytes
Biochemistry
27
3260-3267
1988
Sus scrofa
Manually annotated by BRENDA team
Yoshimura, N.; Tsukahara, I.; Murachi, T.
Calpain and calpastatin in porcine retina
Biochem. J.
223
47-51
1984
Sus scrofa
Manually annotated by BRENDA team
Kitahara, A.; Sasaki, T.; Kikuchi, T.; Yumoto, N.; Yoshimura, N.; Hatanaka, M.; Murachi, T.
Large-scale purification of porcine calpain I and calpain II and comparison of proteolytic fragments of their subunits
J. Biochem.
95
1759-1766
1984
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Murachi, T.
Intracellular regulatory system involving calpain and calpastatin
Biochem. Int.
18
263-294
1989
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Guttmann, R.P.; Baker, D.L.; Seifert, K.M.; Cohen, A.S.; Coulter, D.A.; Lynch, D.R.
Specific proteolysis of the NR2 subunit at multiple sites by calpain
J. Neurochem.
78
1083-1093
2001
Sus scrofa
Manually annotated by BRENDA team
Wolf, B.B.; Goldstein, J.C.; Stennicke, H.R.; Beere, H.; Amarante-Mendes, G.P.; Salvesen, G.S.; Green, D.R.
Calpain functions in a caspase-independent manner to promote apoptosis-like events during platelet activation
Blood
94
1683-1692
1999
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Betts, R.; Weinsheimer, S.; Blouse, G.E.; Anagli, J.
Structural determinants of the calpain inhibitory activity of calpastatin peptide B27-WT
J. Biol. Chem.
278
7800-7809
2003
Sus scrofa
Manually annotated by BRENDA team
Maddock, K.R.; Huff-Lonergan, E.; Rowe, L.J.; Lonergan, S.M.
Effect of pH and ionic strength on mu- and m-calpain inhibition by calpastatin
J. Anim. Sci.
83
1370-1376
2005
Sus scrofa
Manually annotated by BRENDA team
Carlin, K.R.; Huff-Lonergan, E.; Rowe, L.J.; Lonergan, S.M.
Effect of oxidation, pH, and ionic strength on calpastatin inhibition of mu- and m-calpain
J. Anim. Sci.
84
925-937
2006
Sus scrofa
Manually annotated by BRENDA team
Chicharro, R.; Alonso, M.; Mazo, M.T.; Aran, V.J.; Herradon, B.
Derivatives of 3-sec-butyl-1-oxo-2,3-dihydroisoquinoline as inhibitors of micro mu-calpain
ChemMedChem
1
710-714
2006
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Coulis, G.; Becila, S.; Herrera-Mendez, C.H.; Sentandreu, M.A.; Raynaud, F.; Richard, I.; Benyamin, Y.; Ouali, A.
Calpain 1 binding capacities of the N1-line region of titin are significantly enhanced by physiological concentrations of calcium
Biochemistry
47
9174-9183
2008
Bos taurus, Sus scrofa
Manually annotated by BRENDA team
Li, Z.; Cao, B.; Zhao, B.; Yang, X.; Fan, M.Z.; Yang, J.
Decreased expression of calpain and calpastatin mRNA during development is highly correlated with muscle protein accumulation in neonatal pigs
Comp. Biochem. Physiol. A
152
498-503
2009
Sus scrofa (P35750)
Manually annotated by BRENDA team
Weaver, A.D.; Bowker, B.C.; Gerrard, D.E.
Sarcomere length influences mu-calpain-mediated proteolysis of bovine myofibrils
J. Anim. Sci.
87
2096-2103
2009
Sus scrofa
Manually annotated by BRENDA team
Liu, T.; Schneider, R.A.; Shah, V.; Huang, Y.; Likhotvorik, R.I.; Keshvara, L.; Hoyt, D.G.
Protein Never in Mitosis Gene A Interacting-1 regulates calpain activity and the degradation of cyclooxygenase-2 in endothelial cells
J. Inflamm.
6
20
2009
Sus scrofa
Manually annotated by BRENDA team
Pomponio, L.; Ertbjerg, P.; Karlsson, A.H.; Costa, L.N.; Lametsch, R.
Influence of early pH decline on calpain activity in porcine muscle
Meat Sci.
85
110-114
2010
Sus scrofa
Manually annotated by BRENDA team
Tang, R.; Yu, B.; Zhang, K.; Guo, X.; Tian, G.; Huang, Z.; Chen, X.; Chen, D.
Effects of nutritional level on pork quality and gene expression of micro-calpain and calpastatin in muscle of finishing pigs
Meat Sci.
85
768-771
2010
Sus scrofa
Manually annotated by BRENDA team
MacQueen, D.; Delbridge, M.; Manthri, S.; Johnston, I.
A newly classified vertebrate calpain protease, directly ancestral to CAPN1 and 2, episodically evolved a restricted physiological function in placental mammals
Mol. Biol. Evol.
27
1886-1902
2010
Anolis carolinensis, Danio rerio, Mus musculus, Notamacropus eugenii, Ornithorhynchus anatinus, Sus scrofa, Taeniopygia guttata, Xenopus laevis
Manually annotated by BRENDA team
Valero, J.G.; Cornut-Thibaut, A.; Juge, R.; Debaud, A.L.; Gimenez, D.; Gillet, G.; Bonnefoy-Berard, N.; Salgado, J.; Salles, G.; Aouacheria, A.; Kucharczak, J.
mu-Calpain conversion of antiapoptotic Bfl-1 (BCL2A1) into a prodeath factor reveals two distinct alpha-helices inducing mitochondria-mediated apoptosis
PLoS ONE
7
e38620
2012
Sus scrofa
Manually annotated by BRENDA team