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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2015
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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] |
format | Online Article Text |
id | pubmed-4773371 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT onoyasuko aminoacidsequencealignmentofvertebratecapn3calpain3p94 AT sorimachihiroyuki aminoacidsequencealignmentofvertebratecapn3calpain3p94 |