Literature DB >> 15138637

Identification and characterization of human FHDC1, mouse Fhdc1 and zebrafish fhdc1 genes in silico.

Masuko Katoh1, Masaru Katoh.   

Abstract

Formin homology proteins, implicated in organogenesis and carcinogenesis, are actin regulators with scaffold function. FMNL1, FMNL2, FMNL3, DIAPH1, DIAPH2, DIAPH3, DAAM1 and DAAM2 are FDD-type Formin homology proteins, while FHOD1, FHOD3, GRID2IP, Fmn1 and Fmn2 are non-FDD-type Formin homology proteins. Here, we identified human FHDC1 gene and vertebrate FHDC1 orthologs by using bioinformatics. The complete coding sequence of human FHDC1 cDNA was determined by assembling 3'-recombinated FLJ35083 chimeric cDNA and 5'-truncated KIAA1727 (AB051514.1) partial cDNA. The complete coding sequence of mouse Fhdc1 cDNA was determined by assembling 3'-truncated CD555494 EST and 5'-truncated 6330505N24 (AK031946.1) partial cDNA. The complete coding sequence of zebrafish fhdc1 cDNA was determined by assembling fhdc1 exons within zebrafish genome clone DKEY-4A14 (BX571710.4). FHDC1 gene was located at human chromosome 4q31.3, and Fhdc1 gene at mouse chromosome 3F1. Human FHDC1 (1143 aa) showed 73.3% total amino-acid identity with mouse Fhdc1 (1148 aa), and 43.4% total amino-acid identity with zebrafish Fhdc1 (1165 aa). FDCH1-FDCH5 domains were identified as novel conserved regions among vertebrate FHDC1 orthologs. Human FHDC1, mouse Fhdc1, and zebrafish Fhdc1 were non-FDD-type Formin homology proteins with FH1 and FH2 domains in the N-terminal part as well as with FDCH1, FDCH2, FDCH3, FDCH4, and FDCH5 domains in the C-terminal part. This is the first report on the identification and characterization of the human FHDC1, mouse Fhdc1 and zebrafish fhdc1 genes.

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Year:  2004        PMID: 15138637

Source DB:  PubMed          Journal:  Int J Mol Med        ISSN: 1107-3756            Impact factor:   4.101


  5 in total

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Journal:  Mol Biol Cell       Date:  2008-09-24       Impact factor: 4.138

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Journal:  Cytoskeleton (Hoboken)       Date:  2013-05-24

Review 3.  Inverted formins: A subfamily of atypical formins.

Authors:  Anna Hegsted; Curtis V Yingling; David Pruyne
Journal:  Cytoskeleton (Hoboken)       Date:  2017-09-29

4.  The ability to induce microtubule acetylation is a general feature of formin proteins.

Authors:  Susan F Thurston; Wojciech A Kulacz; Sahir Shaikh; Jonathan M Lee; John W Copeland
Journal:  PLoS One       Date:  2012-10-24       Impact factor: 3.240

5.  Whole-transcriptome sequencing profiling identifies functional and prognostic signatures in patients with PTPRZ1-MET fusion-negative secondary glioblastoma multiforme.

Authors:  Bao-Shi Chen; Kuan-Yu Wang; Shu-Qing Yu; Chuan-Bao Zhang; Guan-Zhang Li; Zhi-Liang Wang; Zhao-Shi Bao
Journal:  Oncol Lett       Date:  2020-09-03       Impact factor: 2.967

  5 in total

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