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10.1093/bioinformatics/btx689

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suck abstract from ncbi


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pmid29088312
      Bioinformatics 2018 ; 34 (5 ): 721-724
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  • TMEM132: an ancient architecture of cohesin and immunoglobulin domains define a new family of neural adhesion molecules #MMPMID29088312
  • Sanchez-Pulido L ; Ponting CP
  • Bioinformatics 2018[Mar]; 34 (5 ): 721-724 PMID29088312 show ga
  • SUMMARY: The molecular functions of TMEM132 genes remain poorly understood and under-investigated despite their mutations associated with non-syndromic hearing loss, panic disorder and cancer. Here we show the full domain architecture of human TMEM132 family proteins solved using in-depth sequence and structural analysis. We reveal them to be five previously unappreciated cell adhesion molecules whose domain architecture has an early holozoan origin prior to the emergence of choanoflagellates and metazoa. The extra-cellular portions of TMEM132 proteins contain five conserved domains including three tandem immunoglobulin domains, and a cohesin domain homologue, the first such domain found in animals. These findings strongly predict a cellular adhesion function for TMEM132 family, connecting the extracellular medium with the intracellular actin cytoskeleton. CONTACT: luis.sanchez-pulido@igmm.ed.ac.uk. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
  • |*Multigene Family [MESH]
  • |Amino Acid Sequence [MESH]
  • |Animals [MESH]
  • |Cell Adhesion Molecules/*chemistry/genetics [MESH]
  • |Cell Cycle Proteins [MESH]
  • |Chromosomal Proteins, Non-Histone [MESH]
  • |Cohesins [MESH]
  • |Humans [MESH]
  • |Immunoglobulin Domains [MESH]
  • |Membrane Proteins/*chemistry/genetics [MESH]
  • |Protein Domains [MESH]


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