{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1363670320479800448.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1016/j.cbd.2005.10.007"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S1744117X05000250?httpAccept=text/xml"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S1744117X05000250?httpAccept=text/plain"}},{"identifier":{"@type":"PMID","@value":"20483252"}}],"dc:title":[{"@value":"Evolution of the arginine kinase gene family"}],"description":[{"notation":[{"@value":"Arginine kinase (AK), catalyzing the reversible transfer of phosphate from MgATP to arginine yielding phosphoarginine and MgADP, is widely distributed throughout the invertebrates and is also present in certain protozoa. Typically, these proteins are found as monomers targeted to the cytoplasm, but true dimeric and contiguous dimeric AKs as well as mitochondrial AK activities have been observed. In the present study, we have obtained the sequences of the genes for AKs from two distantly related molluscs-the cephalopod Nautilus pompilius and the bivalve Crassostrea gigas. These new data were combined with available gene structure data (exon/intron organization) extracted from EST and genome sequencing project databases. These data, comprised of 23 sequences and gene structures from Protozoa, Cnidaria, Platyhelminthes, Mollusca, Arthropoda and Nematoda, provide great insight into the evolution and divergence of the AK family. Sequence and phylogenetic analyses clearly show that the AKs are homologous having arisen from some common ancestor. However, AK gene organization is highly divergent and variable. Molluscan AK genes typically have a highly conserved six-exon/five-intron organization, a structure that is very similar to that of the platyhelminth Schistosoma mansoni Arthropod and nematode AK genes have fewer introns, while the cnidarian and protozoan genes each display unique exon/intron organization when compared to the other AK genes. The non-conservative nature of the AK genes is in sharp contrast to the relatively high degree of conservation of intron positions seen in a homologous enzyme creatine kinase (CK). The present results also show that gene duplication and subsequent fusion events forming unusual two-domain AKs occurred independently at least four times as these contiguous dimers are present in Protozoa, Cnidaria, Platyhelminthes and Mollusca. Detailed analyses of the amino acid sequences indicate that two AKs (one each from Drosophila and Caenorhabditis) have what appear to be N-terminal mitochondrial targeting sequences, providing the first evidence for true mitochondrial AK genes. The AK gene family is ancient and the lineage has undergone considerable divergence as well as multiple duplication and fusion events."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1420845751147432448","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"10448392"},{"@type":"NRID","@value":"1000010448392"},{"@type":"NRID","@value":"9000258270499"},{"@type":"NRID","@value":"9000399771776"},{"@type":"NRID","@value":"9000022246522"},{"@type":"NRID","@value":"9000006032157"},{"@type":"NRID","@value":"9000326264026"},{"@type":"NRID","@value":"9000364733007"},{"@type":"NRID","@value":"9000347173159"},{"@type":"NRID","@value":"9000017317044"},{"@type":"NRID","@value":"9000022240211"},{"@type":"NRID","@value":"9000391552582"},{"@type":"NRID","@value":"9000006332749"},{"@type":"NRID","@value":"9000391894484"},{"@type":"NRID","@value":"9000364745190"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/udakouji"}],"foaf:name":[{"@value":"Kouji Uda"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320479800449","@type":"Researcher","foaf:name":[{"@value":"Naka Fujimoto"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320479800450","@type":"Researcher","foaf:name":[{"@value":"Youhei Akiyama"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320479800451","@type":"Researcher","foaf:name":[{"@value":"Kanae Mizuta"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320479800454","@type":"Researcher","foaf:name":[{"@value":"Kumiko Tanaka"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320479800453","@type":"Researcher","foaf:name":[{"@value":"W. Ross Ellington"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320479800448","@type":"Researcher","foaf:name":[{"@value":"Tomohiko Suzuki"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"1744117X"}],"prism:publicationName":[{"@value":"Comparative Biochemistry and Physiology Part D: Genomics and Proteomics"}],"dc:publisher":[{"@value":"Elsevier BV"}],"prism:publicationDate":"2006-06","prism:volume":"1","prism:number":"2","prism:startingPage":"209","prism:endingPage":"218"},"reviewed":"false","dc:rights":["https://www.elsevier.com/tdm/userlicense/1.0/"],"url":[{"@id":"https://api.elsevier.com/content/article/PII:S1744117X05000250?httpAccept=text/xml"},{"@id":"https://api.elsevier.com/content/article/PII:S1744117X05000250?httpAccept=text/plain"}],"createdAt":"2005-12-19","modifiedAt":"2021-07-21","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360004232038056576","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Arginine kinases from the marine feather star Tropiometra afra macrodiscus: The first finding of a prenylation signal sequence in metazoan phosphagen kinases"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004232374811904","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Phosphagen kinase in Schistosoma japonicum: II. Determination of amino acid residues essential for substrate catalysis using site-directed mutagenesis"}]},{"@id":"https://cir.nii.ac.jp/crid/1360285706948483072","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Arginine kinase in  Toxocara canis : Exon–intron organization, functional analysis of site-directed mutants and evaluation of putative enzyme inhibitors"}]},{"@id":"https://cir.nii.ac.jp/crid/1360285707120631936","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"The role of Y84 on domain 1 and Y87 on domain 2 of Paragonimus westermani taurocyamine kinase: Insights on the substrate binding mechanism of a trematode phosphagen kinase"}]},{"@id":"https://cir.nii.ac.jp/crid/1360565165891321472","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"A diverse array of creatine kinase and arginine kinase isoform genes is present in the starlet sea anemone Nematostella vectensis, a cnidarian model system for studying developmental evolution"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848656968179968","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Two arginine kinases of Tetrahymena pyriformis: Characterization and localization"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848657077378688","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Gene structure of the two‐domain taurocyamine kinase from <i>Paragonimus westermani</i>: Evidence for a distinct lineage of trematode phosphagen kinases"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848657118672896","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Characterization of four arginine kinases in the ciliate Paramecium tetraurelia : Investigation on the substrate inhibition mechanism"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1016/j.cbd.2005.10.007"},{"@type":"OPENAIRE","@value":"doi_dedup___::519b94f6d50a55fb86a4b11e1bc38749"},{"@type":"CROSSREF","@value":"10.1016/j.ijbiomac.2017.03.133_references_DOI_Ixp3l9oDSuHp0fHIqNfCcR6k1l8"},{"@type":"CROSSREF","@value":"10.1016/j.exppara.2013.10.008_references_DOI_Ixp3l9oDSuHp0fHIqNfCcR6k1l8"},{"@type":"CROSSREF","@value":"10.1016/j.gene.2012.01.036_references_DOI_Ixp3l9oDSuHp0fHIqNfCcR6k1l8"},{"@type":"CROSSREF","@value":"10.1016/j.febslet.2013.05.061_references_DOI_Ixp3l9oDSuHp0fHIqNfCcR6k1l8"},{"@type":"CROSSREF","@value":"10.1016/j.apjtm.2016.07.023_references_DOI_Ixp3l9oDSuHp0fHIqNfCcR6k1l8"},{"@type":"CROSSREF","@value":"10.1016/j.cbpb.2015.04.014_references_DOI_Ixp3l9oDSuHp0fHIqNfCcR6k1l8"},{"@type":"CROSSREF","@value":"10.1016/j.cbpb.2014.03.008_references_DOI_Ixp3l9oDSuHp0fHIqNfCcR6k1l8"},{"@type":"CROSSREF","@value":"10.1016/j.molbiopara.2014.04.010_references_DOI_Ixp3l9oDSuHp0fHIqNfCcR6k1l8"}]}