Literature summary for 3.4.22.B25 extracted from

Singh, R.; Brewer, M.K.; Mashburn, C.B.; Lou, D.; Bondada, V.; Graham, B.; Geddes, J.W.
Calpain 5 is highly expressed in the central nervous system (CNS), carries dual nuclear localization signals, and is associated with nuclear promyelocytic leukemia protein bodies (2014), J. Biol. Chem., 289, 19383-19394.

Search for more literature for 3.4.22.B25

Cloned(Commentary)

Cloned (Comment)	Organism
gene Capn5, DNA and amino acid sequence determination and analysis	Mus musculus
gene Capn5, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis	Rattus norvegicus
gene Capn5, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
additional information	unlike findings in classical calpains, which are characterized as being mainly cytosolic, CAPN5 is predominantly a noncytosolic calpain, present in the nucleus in the nucleic acidbinding protein fraction. The enzyme CAPN5 is associated with one or more nuclear bodies. Non-nuclear, particularly perinuclear. CAPN5 is found in punctate domains associated with promyelocytic leukemia protein within the nucleus	Homo sapiens	-	-
additional information	unlike findings in classical calpains, which are characterized as being mainly cytosolic, CAPN5 is predominantly a noncytosolic calpain, present in the nucleus in the nucleic acidbinding protein fraction. The enzyme is associated with nuclear promyelocytic leukemia protein bodies	Rattus norvegicus	-	-
additional information	unlike findings in classical calpains, which are characterized as being mainly cytosolic, CAPN5 is predominantly a noncytosolic calpain, present in the nucleus in the nucleic acidbinding protein fraction. The enzyme is associated with nuclear promyelocytic leukemia protein bodies	Mus musculus	-	-
nucleus	the enzyme carries dual nuclear localization signals	Rattus norvegicus	5634	-
nucleus	the enzyme carries dual nuclear localization signals	Mus musculus	5634	-
nucleus	the enzyme carries the nuclear localization signal RRRK (aa 2124)	Homo sapiens	5634	-
perinuclear space	-	Rattus norvegicus	-	-
perinuclear space	-	Mus musculus	-	-
perinuclear space	-	Homo sapiens	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	dependent on	Rattus norvegicus
Ca2+	dependent on	Mus musculus
Ca2+	dependent on	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O15484	-	-
Mus musculus	O08688	gene Capn5	-
Mus musculus C57/BL6J	O08688	gene Capn5	-
Rattus norvegicus	Q8R4C0	gene Capn5	-
Rattus norvegicus Sprague-Dawley	Q8R4C0	gene Capn5	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
astrocyte	-	Mus musculus	-
brain	-	Rattus norvegicus	-
brain	-	Mus musculus	-
central nervous system	-	Mus musculus	-
central nervous system	-	Homo sapiens	-
central nervous system	high expression level	Rattus norvegicus	-
dentate granule cell	-	Mus musculus	-
hilar neuron	-	Mus musculus	-
hippocampus	-	Mus musculus	-
additional information	immunohistochemic analysis, ubiquitous expression in central nerous system cells, overview	Mus musculus	-
neuroblastoma cell	-	Homo sapiens	-
oligodendrocyte	-	Mus musculus	-
pyramidal neuron	-	Mus musculus	-
SH-SY5Y cell	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
CAPN5	-	Rattus norvegicus
CAPN5	-	Mus musculus
CAPN5	-	Homo sapiens

General Information

General Information	Comment	Organism
evolution	calpain 5 is a non-classical member of the calpain family. It lacks the EF hand motif characteristic of classical calpains but retains catalytic and Ca2 binding domains, and it contains a unique C-terminal domain	Rattus norvegicus
evolution	calpain 5 is a non-classical member of the calpain family. It lacks the EF hand motif characteristic of classical calpains but retains catalytic and Ca2 binding domains, and it contains a unique C-terminal domain	Mus musculus
evolution	calpain 5 is a non-classical member of the calpain family. It lacks the EF hand motif characteristic of classical calpains but retains catalytic and Ca2 binding domains, and it contains a unique C-terminal domain	Homo sapiens
additional information	the enzyme is associated with nuclear promyelocytic leukemia protein bodies	Rattus norvegicus
additional information	the enzyme is associated with nuclear promyelocytic leukemia protein bodies	Mus musculus
additional information	the enzyme is associated with nuclear promyelocytic leukemia protein bodies	Homo sapiens

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Release 2023.1 (January 2023)