Amino acid sequence alignment of vertebrate CAPN3/calpain-3/p94

CAPN3 is a calpain superfamily member that is predominantly expressed in skeletal muscle. So far, clear CAPN3 orthologs were found only in vertebrates. CAPN3 is a unique protease in that it undergoes extremely rapid and exhaustive autolysis and that autolyzed fragments spontaneously associate each o...

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Main Authors: Yasuko Ono, Hiroyuki Sorimachi
Format: Article
Language:English
Published: Elsevier 2015-12-01
Series:Data in Brief
Online Access:http://www.sciencedirect.com/science/article/pii/S2352340915002152
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author Yasuko Ono
Hiroyuki Sorimachi
author_facet Yasuko Ono
Hiroyuki Sorimachi
author_sort Yasuko Ono
collection DOAJ
description CAPN3 is a calpain superfamily member that is predominantly expressed in skeletal muscle. So far, clear CAPN3 orthologs were found only in vertebrates. CAPN3 is a unique protease in that it undergoes extremely rapid and exhaustive autolysis and that autolyzed fragments spontaneously associate each other to reconstitute the proteolytic activity. These unique properties of CAPN3 are dependent on IS1 and IS2, two CAPN3-characterizing sequences that do not exist in other calpains or any other proteases. To understand how IS1 and IS2 are conserved among vertebrates, this data article provides amino acid sequence alignment of representative vertebrate CAPN3s. For further analysis and discussion, see Ono et al. [1]
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spelling doaj.art-e9f1e281a8184c9b98196e42998eb8e22022-12-22T01:20:58ZengElsevierData in Brief2352-34092015-12-015C36636710.1016/j.dib.2015.09.021Amino acid sequence alignment of vertebrate CAPN3/calpain-3/p94Yasuko OnoHiroyuki SorimachiCAPN3 is a calpain superfamily member that is predominantly expressed in skeletal muscle. So far, clear CAPN3 orthologs were found only in vertebrates. CAPN3 is a unique protease in that it undergoes extremely rapid and exhaustive autolysis and that autolyzed fragments spontaneously associate each other to reconstitute the proteolytic activity. These unique properties of CAPN3 are dependent on IS1 and IS2, two CAPN3-characterizing sequences that do not exist in other calpains or any other proteases. To understand how IS1 and IS2 are conserved among vertebrates, this data article provides amino acid sequence alignment of representative vertebrate CAPN3s. For further analysis and discussion, see Ono et al. [1]http://www.sciencedirect.com/science/article/pii/S2352340915002152
spellingShingle Yasuko Ono
Hiroyuki Sorimachi
Amino acid sequence alignment of vertebrate CAPN3/calpain-3/p94
Data in Brief
title Amino acid sequence alignment of vertebrate CAPN3/calpain-3/p94
title_full Amino acid sequence alignment of vertebrate CAPN3/calpain-3/p94
title_fullStr Amino acid sequence alignment of vertebrate CAPN3/calpain-3/p94
title_full_unstemmed Amino acid sequence alignment of vertebrate CAPN3/calpain-3/p94
title_short Amino acid sequence alignment of vertebrate CAPN3/calpain-3/p94
title_sort amino acid sequence alignment of vertebrate capn3 calpain 3 p94
url http://www.sciencedirect.com/science/article/pii/S2352340915002152
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