title: Calmin, a protein with calponin homology and transmembrane domains expressed in maturing spermatogenic cells.
abstract: A cDNA named calmin of approximately 3.2 kb was isolated by RNA differential display applied to developing mouse skin. Calmin cDNA encodes 1021 amino acids with two calponin homology (CH) domains in tandem on the N-terminal side and a transmembrane domain on the C-terminal side. The region covering the CH domains showed a high level of homology with beta-spectrin, alpha-actinin, and dystrophin. Among the proteins with the tandem CH domains, calmin is unique in having a transmembrane domain. Three alternative splicing sites were identified at the 3'-side of calmin, giving rise to polymorphic protein products with or without the transmembrane domain. The calmin transcript was detected in adult testis, liver, kidney, and large intestine; the expression in testis was far stronger than that in the other tissues. In situ hybridization and immunostaining revealed that calmin was expressed in maturing spermatogenic cells at later stages. Human calmin cDNA was also isolated, and its exon/intron organization was determined.
authors.affiliation: Department of Biochemistry, Faculty of Medicine, Toyama Medical and Pharmaceutical University, Sugitani, Toyama-shi 930-0194, Japan.
authors.forename: Z
authors.initials: Z
authors.lastname: Ishisaki
authors.forename: M
authors.initials: M
authors.lastname: Takaishi
authors.forename: I
authors.initials: I
authors.lastname: Furuta
authors.forename: N
authors.initials: N
authors.lastname: Huh
mesh_terms: D000185:Actinin / Q000737:chemistry; D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D015153:Blotting, Western; D019556:COS Cells; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D002462:Cell Membrane / Q000378:metabolism; D018076:DNA, Complementary / Q000378:metabolism; D016189:Dystrophin / Q000737:chemistry; D005091:Exons; D006801:Humans; D017403:In Situ Hybridization; D007438:Introns; D008297:Male; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics*; D051379:Mice; D008840:Microfilament Proteins; D008957:Models, Genetic; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012867:Skin / Q000196:embryology; D013049:Spectrin / Q000737:chemistry; D013090:Spermatocytes / Q000378:metabolism; D013737:Testis / Q000378:metabolism; D013997:Time Factors; D014018:Tissue Distribution; D000096985:Calponins
chemical_list: D000185:Actinin; D002135:Calcium-Binding Proteins; D018076:DNA, Complementary; D016189:Dystrophin; D008565:Membrane Proteins; D008840:Microfilament Proteins; D013049:Spectrin; D000096985:Calponins; C435688:CLMN protein, human; C486659:Clmn protein, mouse