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In mammals they are the products of four separate genes.\n                    <jats:styled-content style=\"fixed-case\">PMCA<\/jats:styled-content>\n                    types 1 and 4 are distributed ubiquitously;\n                    <jats:styled-content style=\"fixed-case\">PMCA<\/jats:styled-content>\n                    types 2 and 3 are restricted to some tissues, the most important being the nervous system. Alternative splicing at two sites greatly increases the number of pump isoforms. The two ubiquitous isoforms are no longer considered as only housekeeping pumps as they also perform tissue\u2010specific functions. The\n                    <jats:styled-content style=\"fixed-case\">PMCA<\/jats:styled-content>\n                    s are classical P\u2010type pumps, their reaction cycle repeating that of all other pumps of the family. Their 3D structure has not been solved, but molecular modeling on\n                    <jats:styled-content style=\"fixed-case\">SERCA<\/jats:styled-content>\n                    pump templates shows the essential structural pattern of the latter.\n                    <jats:styled-content style=\"fixed-case\">PMCA<\/jats:styled-content>\n                    s are regulated by calmodulin, which interacts with high affinity with their cytosolic C\u2010terminal tail. A second calmodulin\u2010binding domain with lower affinity is present in some splicing variants of the pump. The PMCAs are essential to the regulation of cellular Ca\n                    <jats:sup>2+<\/jats:sup>\n                    , but the all\u2010important Ca\n                    <jats:sup>2+<\/jats:sup>\n                    signal is ambivalent: defects in its control generate various pathologies, the most thoroughly studied being those of genetic origin. Genetic defects of\n                    <jats:styled-content style=\"fixed-case\">PMCA<\/jats:styled-content>\n                    function produce disease phenotypes: the best characterized is a form of deafness in mice and in humans linked to\n                    <jats:styled-content style=\"fixed-case\">PMCA<\/jats:styled-content>\n                    2 mutations. A cerebellar X\u2010linked human ataxia has recently been found to be caused by a mutation in the calmodulin\u2010binding domain of\n                    <jats:styled-content style=\"fixed-case\">PMCA<\/jats:styled-content>\n                    3.\n                  <\/jats:p>","DOI":"10.1111\/febs.12193","type":"journal-article","created":{"date-parts":[[2013,2,18]],"date-time":"2013-02-18T17:50:42Z","timestamp":1361209842000},"page":"5385-5397","source":"Crossref","is-referenced-by-count":161,"title":["The plasma membrane calcium pump in health and disease"],"prefix":"10.1111","volume":"280","author":[{"given":"Marisa","family":"Brini","sequence":"first","affiliation":[{"name":"Department of Comparative Biomedicine and Food Science University of Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tito","family":"Cal\u00ec","sequence":"additional","affiliation":[{"name":"Department of Comparative Biomedicine and Food Science University of Padova 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