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0CAN5_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCAPN5
DescriptionCalpain-5 (ec 3.4.22.-) (ncl-3) (htra-3).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004198 calpain activity (TAS)
0007165 signal transduction (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. Cysteine peptidases have characteristic molecular topologies.hich can be seen not only in their three-dimensional structures.ut commonly also in the two-dimensional structures. The peptidase domain is responsible for peptide bond hydrolysis; in Merops this is termed the peptidase unit. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins which are evolutionary related).nd further sub-divided into families.n the basis of the architecture of their catalytic dyad or triad : Clan CA contains the families of papain (C1).alpain (C2).treptopain (C10) and the ubiquitin-specific peptidases (C12.19).s well as many families of viral cysteine endopeptidases. Clan CD contains the families of clostripain (C11).ingipain R (C25).egumain (C13).aspase-1 (C14) and separin (C50). These enzymes have specificities dominated by the interactions of the S1 subsite. Clan CE contains the families of adenain (C5) from adenoviruses.he eukaryotic Ulp1 protease (C48) and the bacterial YopJ proteases (C55). Clan CF contains only pyroglutamyl peptidase I (C15). Clan PA contains the picornains (C3).hich have probably evolved from serine peptidases and which form the majority of enzymes in this clan. Clans PB and CH contain the autolytic cysteine peptidases. This group of cysteine peptidases belong to the MEROPS peptidase family C2 (calpain family.lan CA). A type example is calpain.hich is an intracellular protease involved in many important cellular functions that are regulated by calcium . The protein is a complex of 2polypeptide chains (light and heavy).ith three known forms in mammals. a highly calcium-sensitive (i.e..icro-molar range) form known as mu-calpain.u-CANP or calpain I; a form sensitive to calcium in the milli-molar range.nown as m-calpain.-CANP or calpain II; and a third form.nown as p94.hich is found in skeletal muscle only . All forms have identical light but different heavy chains. Both mu- and m-calpain are heterodimers containing an identical 28-kDa subunit and an 80-kDa subunit that shares 55-65% sequence homology between the two proteases . The crystallographic structure of m-calpain reveals six "domains" in the 80-kDa subunit: A 19-amino acid NH2-terminal sequence;Active site domain IIa;Active site domain IIb. Domain 2 showslow levels of sequence similarity to papain; although the catalytic His hasnot been located by biochemical means.t is likely that calpain and papainare related . Domain III;An 18-amino acid extended sequence linking domain III to domain IV;Domain IV.hich resembles the penta EF-hand family of polypeptides.inds calcium and regulates activity . />. Ca2+-binding causes a rearrangement of the protein backbone.he net effect of which is that a Trp side chain.hich acts as a wedge between catalytic domains IIa and IIb in the apo state.oves away from the active site cleft allowing for the proper formation of the catalytic triad . Calpain-like mRNAs have been identified in other organisms including bacteria.ut the molecules encoded by these mRNAs have not been isolated.o little is known about their properties. How calpain activity is regulated in these organisms cells is still unclear In metazoans.he activity of calpain is controlled by a single proteinase inhibitor.alpastatin (). The calpastatin gene can produce eight or more calpastatin polypeptides ranging from 17 to 85 kDa by use of different promoters and alternative splicing events. The physiological significance of these different calpastatins is unclear.lthough all bind to three different places on the calpain molecule; binding to at least two of the sites is Ca2+ dependent. The calpains ostensibly participate in a variety of cellular processes including remodelling of cytoskeletal/membrane attachments.ifferent signal transduction pathways.nd apoptosis. Deregulated calpain activity following loss of Ca2+ homeostasis results in tissue damage in response to events such as myocardial infarcts.troke.nd brain trauma .
  IPR001300:Peptidase C2, calpain
The C2 domain is a Ca2+-dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking. C2 domains are unique among membrane targeting domains in that they show wide range of lipid selectivity for the major components of cell membranes.ncluding phosphatidylserine and phosphatidylcholine. This C2 domain is about 116 amino-acid residues and is located between the two copies ofthe C1 domain in Protein Kinase C (that bind phorbol esters and diacylglycerol) (see )and the protein kinase catalytic domain (see ). Regions withsignificant homology to the C2-domain have been found in many proteins.The C2 domain is thought to be involved in calcium-dependent phospholipidbinding and in membrane targetting processes such as subcellular localisation. The 3D structure of theC2 domain of synaptotagmin has been reported.he domain forms an eight-stranded beta sandwich constructed around a conserved 4-stranded motif.esignated a C2 key . Calcium binds ina cup-shaped depression formed by the N- and C-terminal loops of theC2-key motif. Structural analyses of several C2 domains have shown them to consist of similar ternary structures in which three Ca2+-binding loops are located at the end of an 8 stranded antiparallel beta sandwich.
  IPR000008:C2 calcium-dependent membrane targeting
The Ca2+-dependent.ipid-binding domain (CaLB) has been identified in a number of proteins.or example the amino-terminal.38 amino acid C2 domain of cytosolic phospholipase A2 (cPLA2-C2) which mediates an initial step in the production of lipid mediators of inflammation: the Ca2+-dependent translocation of the enzyme to intracellular membranes with subsequent liberation of arachidonic acid. The domain is composed of eight antiparallel beta-strands with six interconnecting loops that fits the "type II" topology for C2 domains. The structure has been identified as a beta-sandwich in the "Greek key" motif .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008973:C2 calcium/lipid-binding region, CaLB
IPR001300:CysPc 
Evalue:-221.031517051446 
Location:8-351IPR001300:Calpain_III 
Evalue:-78.9208221435547 
Location:353-496IPR000008:C2 
Evalue:-14.3565473556519 
Location:519-596IPR000169:THIOL_PROTEASE_ASN 
Evalue:0 
Location:0-0
SequencesProtein: CAN5_HUMAN (640 aa)
mRNA: AK094150 AK128124 BC018123
Local Annotation
Synapse Ontology
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentK01367
  Level 3 annotation:
    calpain-1
  Level 2 annotation:
    Apoptosis
    Focal adhesion
K03853
  Level 3 annotation:
    calpain-2
  Level 2 annotation:
    Apoptosis
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 51 residues, 76455639-76455789Exon2: 68 residues, 76473545-76473745Exon3: 46 residues, 76482375-76482507Exon4: 71 residues, 76501282-76501491Exon5: 66 residues, 76502935-76503128Exon6: 66 residues, 76504088-76504282Exon7: 28 residues, 76504919-76504997Exon8: 67 residues, 76506850-76507046Exon9: 43 residues, 76507723-76507846Exon10: 67 residues, 76509406-76509603Exon11: 40 residues, 76510627-76510743Exon12: 47 residues, 76511269-76511406Exon13: 289 residues, 76512381-76513242Exon14: 2 residues, -Jump to CAN5_HUMANExon1: 42 residues, 76455665-76455789Exon2: 51 residues, 76461684-76461831Exon3: 68 residues, 76473545-76473745Exon4: 46 residues, 76482375-76482507Exon5: 71 residues, 76501282-76501491Exon6: 66 residues, 76502935-76503128Exon7: 66 residues, 76504088-76504282Exon8: 28 residues, 76504919-76504997Exon9: 67 residues, 76506850-76507046Exon10: 43 residues, 76507723-76507846Exon11: 67 residues, 76509406-76509603Exon12: 40 residues, 76510627-76510743Exon13: 47 residues, 76511269-76511406Exon14: 393 residues, 76512381-76513554Exon15: 61 residues, 76514666-76514844Exon16: 2 residues, -Jump to CAN5_HUMANExon1: 35 residues, 76455687-76455789Exon2: 68 residues, 76473545-76473745Exon3: 42 residues, 76476635-76476755Exon4: 46 residues, 76482375-76482507Exon5: 71 residues, 76501282-76501491Exon6: 66 residues, 76502935-76503128Exon7: 66 residues, 76504088-76504282Exon8: 28 residues, 76504919-76504997Exon9: 67 residues, 76506850-76507046Exon10: 43 residues, 76507723-76507846Exon11: 67 residues, 76509406-76509603Exon12: 40 residues, 76510627-76510743Exon13: 47 residues, 76511269-76511406Exon14: 271 residues, 76512381-76513189Exon15: 2 residues, -Jump to CAN5_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2694 76516957-76603931 ~-87K 7455(MYO7A)(+)Loci: 2693 76455639-76514844 ~-59K 7451(CAPN5)(+)Link out to UCSC