Calpain-1 catalytic subunit

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• Broad endopeptidase specificity.By similarity

  Manual assertion inferred from sequence similarity toⁱ

  • UniProtKB:P07384 (CAN1_HUMAN)

  EC:3.4.22.52

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactorⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationⁱ

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• calcium-dependent cysteine-type endopeptidase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Calpain 2 activated through N-methyl-D-aspartic acid receptor signaling cleaves CPEB3 and abrogates CPEB3-repressed translation in neurons."
    Wang C.F., Huang Y.S.
    Mol. Cell. Biol. 32:3321-3332(2012) [PubMed] [Europe PMC] [Abstract]
• calcium ion binding Source: RGDInferred from direct assayⁱ
  • Ref.3

    "A Ca(2+) switch aligns the active site of calpain."
    Moldoveanu T., Hosfield C.M., Lim D., Elce J.S., Jia Z., Davies P.L.
    Cell 108:649-660(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 27-356, CALCIUM-BINDING REGIONS.
• cytoskeletal protein binding Source: RGDInferred from direct assayⁱ
  • "Calpain/calpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle."
    Enns D.L., Raastad T., Ugelstad I., Belcastro A.N.
    Eur. J. Appl. Physiol. 100:445-455(2007) [PubMed] [Europe PMC] [Abstract]
• enzyme binding Source: RGD <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Proteomic study of calpain interacting proteins during skeletal muscle aging."
    Brule C., Dargelos E., Diallo R., Listrat A., Bechet D., Cottin P., Poussard S.
    Biochimie 92:1923-1933(2010) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• aging Source: RGD <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Calpain-1 regulation of matrix metalloproteinase 2 activity in vascular smooth muscle cells facilitates age-associated aortic wall calcification and fibrosis."
    Jiang L., Zhang J., Monticone R.E., Telljohann R., Wu J., Wang M., Lakatta E.G.
    Hypertension 60:1192-1199(2012) [PubMed] [Europe PMC] [Abstract]
• brain development Source: RGDInferred from expression patternⁱ
  • "Calpain 1 and Calpastatin expression is developmentally regulated in rat brain."
    Li Y., Bondada V., Joshi A., Geddes J.W.
    Exp. Neurol. 220:316-319(2009) [PubMed] [Europe PMC] [Abstract]
• cellular response to hydrogen peroxide Source: RGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "High glucose-induced Ca2+ overload and oxidative stress contribute to apoptosis of cardiac cells through mitochondrial dependent and independent pathways."
    Kumar S., Kain V., Sitasawad S.L.
    Biochim. Biophys. Acta 1820:907-920(2012) [PubMed] [Europe PMC] [Abstract]
• mammary gland involution Source: RGDInferred from sequence orthologyⁱ
  • "Calpains mediate epithelial-cell death during mammary gland involution: mitochondria and lysosomal destabilization."
    Arnandis T., Ferrer-Vicens I., Garcia-Trevijano E.R., Miralles V.J., Garcia C., Torres L., Vina J.R., Zaragoza R.
    Cell Death Differ. 19:1536-1548(2012) [PubMed] [Europe PMC] [Abstract]
• negative regulation of actin filament polymerization Source: RGDInferred from mutant phenotypeⁱ
  • "Activity-dependent rapid local RhoA synthesis is required for hippocampal synaptic plasticity."
    Briz V., Zhu G., Wang Y., Liu Y., Avetisyan M., Bi X., Baudry M.
    J. Neurosci. 35:2269-2282(2015) [PubMed] [Europe PMC] [Abstract]
• negative regulation of NIK/NF-kappaB signaling Source: RGDInferred from mutant phenotypeⁱ
  • "A novel role for calpain in the endothelial dysfunction induced by activation of angiotensin II type 1 receptor signaling."
    Scalia R., Gong Y., Berzins B., Freund B., Feather D., Landesberg G., Mishra G.
    Circ. Res. 108:1102-1111(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cardiac muscle cell apoptotic process Source: RGDInferred from mutant phenotypeⁱ
  • "High glucose-induced Ca2+ overload and oxidative stress contribute to apoptosis of cardiac cells through mitochondrial dependent and independent pathways."
    Kumar S., Kain V., Sitasawad S.L.
    Biochim. Biophys. Acta 1820:907-920(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of leukocyte tethering or rolling Source: RGDInferred from mutant phenotypeⁱ
  • "A novel role for calpain in the endothelial dysfunction induced by activation of angiotensin II type 1 receptor signaling."
    Scalia R., Gong Y., Berzins B., Freund B., Feather D., Landesberg G., Mishra G.
    Circ. Res. 108:1102-1111(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of vascular permeability Source: RGDInferred from mutant phenotypeⁱ
  • "A novel role for calpain in the endothelial dysfunction induced by activation of angiotensin II type 1 receptor signaling."
    Scalia R., Gong Y., Berzins B., Freund B., Feather D., Landesberg G., Mishra G.
    Circ. Res. 108:1102-1111(2011) [PubMed] [Europe PMC] [Abstract]
• protein autoprocessing Source: RGDInferred from direct assayⁱ
  • "Differential localization of autolyzed calpains 1 and 2 in slow and fast skeletal muscles in the early phase of atrophy."
    Vermaelen M., Sirvent P., Raynaud F., Astier C., Mercier J., Lacampagne A., Cazorla O.
    Am. J. Physiol., Cell Physiol. 292:C1723-31(2007) [PubMed] [Europe PMC] [Abstract]
• proteolysis Source: UniProtKBInferred from direct assayⁱ
  • "Calpain 2 activated through N-methyl-D-aspartic acid receptor signaling cleaves CPEB3 and abrogates CPEB3-repressed translation in neurons."
    Wang C.F., Huang Y.S.
    Mol. Cell. Biol. 32:3321-3332(2012) [PubMed] [Europe PMC] [Abstract]
• receptor catabolic process Source: RGDInferred from sequence orthologyⁱ
  • "Cyclin-dependent kinase 5 governs learning and synaptic plasticity via control of NMDAR degradation."
    Hawasli A.H., Benavides D.R., Nguyen C., Kansy J.W., Hayashi K., Chambon P., Greengard P., Powell C.M., Cooper D.C., Bibb J.A.
    Nat. Neurosci. 10:880-886(2007) [PubMed] [Europe PMC] [Abstract]
• regulation of catalytic activity Source: UniProtKB
• response to angiotensin Source: RGDInferred from mutant phenotypeⁱ
  • "A novel role for calpain in the endothelial dysfunction induced by activation of angiotensin II type 1 receptor signaling."
    Scalia R., Gong Y., Berzins B., Freund B., Feather D., Landesberg G., Mishra G.
    Circ. Res. 108:1102-1111(2011) [PubMed] [Europe PMC] [Abstract]
• response to arsenic-containing substance Source: RGDInferred from expression patternⁱ
  • "[Effects of arsenic poisoning on neuronal cell apoptosis and mRNA and protein expression of calpain 1, calpain 2, and cdk5/p25]."
    Li X., Chan L., Zhang H., Zhang H., Niu Q.
    Zhonghua Lao Dong Wei Sheng Zhi Ye Bing Za Zhi 32:202-206(2014) [PubMed] [Europe PMC] [Abstract]
• self proteolysis Source: UniProtKB

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Sites

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

GO - Molecular functionⁱ

• cytoskeletal protein binding Source: RGDInferred from direct assayⁱ
  • "Calpain/calpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle."
    Enns D.L., Raastad T., Ugelstad I., Belcastro A.N.
    Eur. J. Appl. Physiol. 100:445-455(2007) [PubMed] [Europe PMC] [Abstract]
• enzyme binding Source: RGDInferred from physical interactionⁱ
  • "Proteomic study of calpain interacting proteins during skeletal muscle aging."
    Brule C., Dargelos E., Diallo R., Listrat A., Bechet D., Cottin P., Poussard S.
    Biochimie 92:1923-1933(2010) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MAEELITPVY CTGVSAQVQK QRDKELGLGR HENAIKYLGQ DYENLRARCL 
        60         70         80         90        100
QNGVLFQDDA FPPVSHSLGF KELGPNSSKT YGIKWKRPTE LLSNPQFIVD 
       110        120        130        140        150
GATRTDICQG ALGDCWLLAA IASLTLNETI LHRVVPYGQS FQEGYAGIFH 
       160        170        180        190        200
FQLWQFGEWV DVVVDDLLPT KDGKLVFVHS AQGNEFWSAL LEKAYAKVNG 
       210        220        230        240        250
SYEALSGGCT SEAFEDFTGG VTEWYDLQKA PSDLYQIILK ALERGSLLGC 
       260        270        280        290        300
SINISDIRDL EAITFKNLVR GHAYSVTDAK QVTYQGQRVN LIRMRNPWGE 
       310        320        330        340        350
VEWKGPWSDN SYEWNKVDPY EREQLRVKME DGEFWMSFRD FIREFTKLEI 
       360        370        380        390        400
CNLTPDALKS RTLRNWNTTF YEGTWRRGST AGGCRNYPAT FWVNPQFKIR 
       410        420        430        440        450
LEEVDDADDY DSRESGCSFL LALMQKHRRR ERRFGRDMET IGFAVYQVPR 
       460        470        480        490        500
ELAGQPVHLK RDFFLANASR AQSEHFINLR EVSNRIRLPP GEYIVVPSTF 
       510        520        530        540        550
EPNKEGDFLL RFFSEKKAGT QELDDQIQAN LPDEKVLSEE EIDDNFKTLF 
       560        570        580        590        600
SKLAGDDMEI SVKELQTILN RIISKHKDLR TNGFSLESCR SMVNLMDRDG 
       610        620        630        640        650
NGKLGLVEFN ILWNRIRNYL TIFRKFDLDK SGSMSAYEMR MAIEAAGFKL 
       660        670        680        690        700
NKKLHELIIT RYSEPDLAVD FDNFVCCLVR LETMFRFFKI LDTDLDGVVT 
       710 
FDLFKWLQLT MFA                                         

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families
3. Peptidase families
   Classification of peptidase families and list of entries