The Journal of Neuroscience, April 28, 2004, ():
gemini Encodes a Zebrafish L-Type Calcium Channel That Localizes at Sensory Hair Cell Ribbon Synapses
J. Neurosci. Sidi et al.
24: 4213
Supplemental data
Supplementary Figure
Files in this Data Supplement:
- Supplemental Fig. 1
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Figure 1. Clustal alignment of the RACE-deduced zebrafish (Dr) Cav1.3a amino acid sequence with human (Hs) and avian (Gg) orthologous proteins and with the product of its zebrafish duplicate (Dr Cav1.3b). Residue identities and similarities are indicated by black and gray boxes, respectively. Putative transmembrane domains and pore loops of each transmembrane repeat (IS--IVS) are indicated by black and gray rectangles, respectively. Other domains of known biological significance are denoted by white rectangles. Note that all S4 transmembrane segments, which are the voltage-sensing domains of the channel (consisting of XXY repeats in which Y is a positively charged residue), are identical across species. Divergent regions between Dr Cav1.3a and Hs and Gg proteins include the extremity of the N terminus, which is shorter in zebrafish (see Materials and Methods), a region of the II--III intracellular loop in which the zebrafish gene lacks an exon found in higher vertebrates, and a C-terminal region encompassing an unusual, zebrafish-specific, histidine repeat domain (termed His box). Several Cav1.3 domains are 100% identical across species. These domains are known to interact with (1) the ? subunit of LTCCs (involved in channel modulation) (Pragnell et al., 1994), (2) calmodulin and Ca2+ (involved in channel inactivation and LTCC signal transduction) (de Leon et al., 1995; Zuhlke et al., 1999; Dolmetsch et al., 2001), and (3) RIM binding protein 2 (RBP2; potentially involved in tethering the channel to the vesicle fusion machinery) (Hibino et al., 2002). bd, Binding domain; ?bd, ? subunit binding domain; Cambd, calmodulin binding domain; RBP, RIM binding protein binding domain. Also shown are domains subjected to alternative splicing, the Ca2+ binding EF hand, and the His box. The Cav1.3a residues that are mutated in gem alleles are indicated by asterisks. The position of the Gem25.2 epitope is also indicated.
