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1.A.46.1.6
Bestrophin-1 (Best1) of 689 aas and 4 TMSs in a 2 + 2 arrangement.  The x-ray structure has been determined at 2.85 Å resolution with permeant anions and Ca2+ bound (Kane Dickson et al. 2014).  The channel is formed from a pentameric assembly of subunits. Ca2+ binds to the channel's large cytosolic region. A single ion pore, approximately 95 Å in length, is located along the central axis and contains at least 15 binding sites for anions. A hydrophobic neck within the pore probably forms the gate. Phenylalanine residues within it may coordinate permeating anions via anion-π interactions. Conformational changes observed near the 'Ca2+ clasp' hint at the mechanism of Ca2+-dependent gating (Kane Dickson et al. 2014).

Accession Number:E1C3A0
Protein Name:Uncharacterized protein
Length:689
Molecular Weight:78195.00
Species:Gallus gallus (Chicken) [9031]
Number of TMSs:5
Substrate anions

Cross database links:

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  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MTVTYTNRVA DARLGTFSQL LLQWKGSIYK LLYSEFLIFI SLYFAISLVY RLILSESQRL 
61:	MFEKLALYCN SYAELIPVSF VLGFYVSLVV SRWWAQYESI PWPDRIMNLV SCNVDGEDEY 
121:	GRLLRRTLMR YSNLCSVLIL RSVSTAVYKR FPSMEHVVRA GLMTPEEHKK FESLNSPHNK 
181:	FWIPCVWFSN LAVKARNEGR IRDSVLLQGI LNELNTLRSQ CGRLYGYDWI SIPLVYTQVV 
241:	TVAVYSFFLA CLIGRQFLDP EKAYPGHELD LFVPVFTFLQ FFFYAGWLKV AEQLINPFGE 
301:	DDDDFETNWL IDRNLQVSLM AVDEMHQDLP ILEKDLYWNE PDPQPPYTAA TAEYKRPSFL 
361:	GSTFDISMQK EEMEFQPLEQ IKENEEANHS TPLLGHLGRL LGVQSPSFSR SSSRMNLLRR 
421:	RGEPTSPFSH YTYQDMGKSG NISHPRKLRE FDAFISTPFY ERPGFYSAPQ TPISSIPMIF 
481:	PSRRQGRKKP PALSSIAACS NSLKMSDTYK SQSSLGSGAK ETFIWPTERN KGPDSLVVMV 
541:	EEEKSNSSSK KSPDHEQQGS FKSLKSLKGS HPPWLTLENA ATTTSNCEQS SAFPQPGNIP 
601:	PSSSTSFCFS FTPVASPVLE RSPIEVSRSG RDTASRSSNA PPTRETRRAE SPSTNDSGIS 
661:	LAEGDYVGLM EVIMEASESV CEEQMDQCS