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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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Autores principales: Ono, Yasuko, Sorimachi, Hiroyuki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4773371/
https://www.ncbi.nlm.nih.gov/pubmed/26958593
http://dx.doi.org/10.1016/j.dib.2015.09.021
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author Ono, Yasuko
Sorimachi, Hiroyuki
author_facet Ono, Yasuko
Sorimachi, Hiroyuki
author_sort Ono, Yasuko
collection PubMed
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 pubmed-47733712016-03-08 Amino acid sequence alignment of vertebrate CAPN3/calpain-3/p94 Ono, Yasuko Sorimachi, Hiroyuki Data Brief Data Article 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] Elsevier 2015-10-04 /pmc/articles/PMC4773371/ /pubmed/26958593 http://dx.doi.org/10.1016/j.dib.2015.09.021 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Ono, Yasuko
Sorimachi, Hiroyuki
Amino acid sequence alignment of vertebrate CAPN3/calpain-3/p94
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
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4773371/
https://www.ncbi.nlm.nih.gov/pubmed/26958593
http://dx.doi.org/10.1016/j.dib.2015.09.021
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