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1.A.62.1.4
TRICB1 and TRICB2 of 313 aas and 295 aas, respectively. Yang et al. 2016 presented the structures of TRIC-B1 and TRIC-B2 channels from Caenorhabditis elegans in complex with endogenous phosphatidylinositol-4,5-biphosphate (PtdIns(4,5)P2, also known as PIP2) lipid molecules. The TRIC-B1/B2 proteins and PIP2 assemble into a symmetrical homotrimeric complex. Each monomer contains an hourglass-shaped hydrophilic por within a seven-transmembrane-helix domain. Structural and functional analyses revealed the central role of PIP2 in stabilizing the cytoplasmic gate of the ion permeation pathway and showed a marked Ca2+-induced conformational change in a cytoplasmic loop above the gate. A mechanistic model was proposed to account for the complex gating mechanism of TRIC channels (Yang et al. 2016).

Accession Number:Q9NA73
Protein Name:Uncharacterized protein
Length:313
Molecular Weight:35019.00
Species:Caenorhabditis elegans [6239]
Number of TMSs:7
Substrate Ca2+

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FASTA formatted sequence
1:	MGWVPDEWSI DHDTLIDAGG YVQKLKLYPY FDAAHYVLTC LSVRHDLGPD AISFSRKHPF 
61:	SCWLSCMLMS FAGSFLSCFL LGEPIISPLK QHADILLGSI VWYLVFYSPF DVVFRLATWF 
121:	PVKLGLSVLK EVQRTHKIAA GVKHAVRIYP ESYLVQILVG VAKGAGSGVV KIVEQLARGT 
181:	WHPTNHEILR PSFTTKACVI ASIVFTLERH SMYVTAPHDL VYLCVVGFFI YFKLASLCLS 
241:	VHDVLMPIEN VLCAVFMGGI IDAFAKAVDA TKKAIHSNRV LSEEEILSKE REKVLKKKKL 
301:	LAQMSNGTDK KNN