Calpain-1 - Revision history

Wu3857: /* Reference */

2019-08-19T21:38:54Z

‎Reference

Wu3857 at 20:20, 29 July 2019

2019-07-29T20:20:17Z

Wu3857: /* Protein Function */

2019-07-29T20:18:36Z

‎Protein Function

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|CAPN1|[https://www.uniprot.org/uniprot/P97571 P97571]|Rattus norvegicus|Cys115|[http://pfam.xfam.org/family/PF0..."

2019-07-28T20:42:48Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|CAPN1|[https://www.uniprot.org/uniprot/P97571 P97571]|Rattus norvegicus|Cys115|[http://pfam.xfam.org/family/PF0..."

New page

{| align="left"
| __TOC__
|}
{{#invoke:InfoboxforTarget|run|CAPN1|[https://www.uniprot.org/uniprot/P97571 P97571]|Rattus norvegicus|Cys115|[http://pfam.xfam.org/family/PF00648 Peptidase C2 family]|[[:Category:Calpain-1|Ligand list]]}}
==Summary==

===Protein Function ===
Calpain-1 catalytic subunit is a protein that in humans is encoded by the CAPN1 gene. The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. (From Wikipedia) 
Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Broad endopeptidase specificity. (From Uniprot)
 

===Cys Function & Property===
Cys115 is one of the active sites of Cathepsin H, which is very close to His272 and Asn296 in space. These three residues formed a typical catalytic triad motif. 

* Hydrophobic property:
:[[File:491-hydro.png||600px]]
* SASA：
:Cys115: 12.816 A^2

==Protein Sequence==

MAEELITPVY CTGVSAQVQK QRDKELGLGR HENAIKYLGQ DYENLRARCL 
QNGVLFQDDA FPPVSHSLGF KELGPNSSKT YGIKWKRPTE LLSNPQFIVD 
GATRTDICQG ALGD'''C'''WLLAA IASLTLNETI LHRVVPYGQS FQEGYAGIFH 
FQLWQFGEWV DVVVDDLLPT KDGKLVFVHS AQGNEFWSAL LEKAYAKVNG 
SYEALSGGCT SEAFEDFTGG VTEWYDLQKA PSDLYQIILK ALERGSLLGC 
SINISDIRDL EAITFKNLVR GHAYSVTDAK QVTYQGQRVN LIRMRNPWGE 
VEWKGPWSDN SYEWNKVDPY EREQLRVKME DGEFWMSFRD FIREFTKLEI 
CNLTPDALKS RTLRNWNTTF YEGTWRRGST AGGCRNYPAT FWVNPQFKIR 
LEEVDDADDY DSRESGCSFL LALMQKHRRR ERRFGRDMET IGFAVYQVPR 
ELAGQPVHLK RDFFLANASR AQSEHFINLR EVSNRIRLPP GEYIVVPSTF 
EPNKEGDFLL RFFSEKKAGT QELDDQIQAN LPDEKVLSEE EIDDNFKTLF 
SKLAGDDMEI SVKELQTILN RIISKHKDLR TNGFSLESCR SMVNLMDRDG 
NGKLGLVEFN ILWNRIRNYL TIFRKFDLDK SGSMSAYEMR MAIEAAGFKL 
NKKLHELIIT RYSEPDLAVD FDNFVCCLVR LETMFRFFKI LDTDLDGVVT 
FDLFKWLQLT MFA 


==Structural Information==
*Known structures with covalent ligands: 
:[https://www.rcsb.org/structure/1TL9 1TL9], [https://www.rcsb.org/structure/1TLO 1TLO] 

*Protein structure:
[[File:491.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko04141 Protein processing in endoplasmic reticulum] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04210 Apoptosis] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04217 Necroptosis] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04218 Cellular senescence] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05010 Alzheimer disease] 

==Experimental Evidence==
:Crystallography

==Reference==
# Moldoveanu T, Campbell R L, Cuerrier D, et al. '''Crystal structures of calpain–E64 and–leupeptin inhibitor complexes reveal mobile loops gating the active site[J].''' Journal of molecular biology, 2004, 343(5): 1313-1326. [https://www.ncbi.nlm.nih.gov/pubmed/?term=15491615 15491615] 

[[Category:Targets|Targets]]
[[Category:Rattus norvegicus|Rattus norvegicus]]
[[Category:Peptidase C2 family|Peptidase C2 family]]
[[Category:Protein processing in endoplasmic reticulum|Protein processing in endoplasmic reticulum]]
[[Category:Apoptosis|Apoptosis]]
[[Category:Necroptosis|Necroptosis]]
[[Category:Cellular senescence|Cellular senescence]]
[[Category:Alzheimer disease|Alzheimer disease]]

@@ Line 57: / Line 57: @@
 # Moldoveanu T, Campbell R L, Cuerrier D, et al. '''Crystal structures of calpain–E64 and–leupeptin inhibitor complexes reveal mobile loops gating the active site[J].''' Journal of molecular biology, 2004, 343(5): 1313-1326. [https://www.ncbi.nlm.nih.gov/pubmed/?term=15491615 15491615]<br/>
-[[Category:Targets|Targets]]
+[[Category:Targets]]
-[[Category:Rattus norvegicus|Rattus norvegicus]]
+[[Category:Rattus norvegicus]]
-[[Category:Protease|Protease]]
+[[Category:Protease]]
-[[Category:Peptidase C2 family|Peptidase C2 family]]
+[[Category:Peptidase C2 family]]
-[[Category:Protein processing in endoplasmic reticulum|Protein processing in endoplasmic reticulum]]
+[[Category:Protein processing in endoplasmic reticulum]]
-[[Category:Apoptosis|Apoptosis]]
+[[Category:Apoptosis]]
-[[Category:Necroptosis|Necroptosis]]
+[[Category:Necroptosis]]
-[[Category:Cellular senescence|Cellular senescence]]
+[[Category:Cellular senescence]]
-[[Category:Alzheimer disease|Alzheimer disease]]
+[[Category:Alzheimer disease]]

@@ Line 6: / Line 6: @@
 ===Protein Function ===
-Calpain-1 catalytic subunit is a protein that in humans is encoded by the CAPN1 gene. The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. (From Wikipedia)<br/>
+Calpain-1 catalytic subunit, encoded by the CAPN1 gene, is  one type of non-lysosomal, intracellular cysteine proteases. And Calpain-1 is calcium-activated neutral protease. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. (From Wikipedia)<br/>
 Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Broad endopeptidase specificity. (From Uniprot)
 <br/>

@@ Line 2: / Line 2: @@
    | __TOC__
    |}
-{{#invoke:InfoboxforTarget|run|CAPN1|[https://www.uniprot.org/uniprot/P97571 P97571]|Rattus norvegicus|Cys115|[http://pfam.xfam.org/family/PF00648 Peptidase C2 family]|[[:Category:Calpain-1|Ligand list]]}}
+{{#invoke:InfoboxforTarget|run|CAPN1|[https://www.uniprot.org/uniprot/P97571 P97571]|Rattus norvegicus|Cys115|[http://pfam.xfam.org/family/PF00648 Peptidase C2 family]|[[:Category:Calpain-1|Ligand list]]|Protease}}
 ==Summary==
@@ Line 59: / Line 59: @@
 [[Category:Targets|Targets]]
 [[Category:Rattus norvegicus|Rattus norvegicus]]
 [[Category:Peptidase C2 family|Peptidase C2 family]]
 [[Category:Protein processing in endoplasmic reticulum|Protein processing in endoplasmic reticulum]]

Calpain-1 - Revision history

Wu3857: /* Reference */

Wu3857 at 20:20, 29 July 2019

Wu3857: /* Protein Function */

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|CAPN1|[https://www.uniprot.org/uniprot/P97571 P97571]|Rattus norvegicus|Cys115|[http://pfam.xfam.org/family/PF0..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|CAPN1|[https://www.uniprot.org/uniprot/P97571 P97571]|Rattus norvegicus|Cys115|[http://pfam.xfam.org/family/PF0..."