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1.A.21.2.4
BH3-interacting domain death agonist isoform 2, BID, of 195 aas and 2 or 3 TMSs. BCL-2 family proteins display structural homology to channel-forming bacterial toxins, such as colicins, the transmembrane domain of diphtheria toxin, and the N-terminal domain of delta-endotoxin. By analogy, it has been hypothesized the BCL-2 family proteins would unfold and insert into the lipid bilayer upon membrane association. Oh et al. 2005 showed that helices 6-8 maintain an alpha-helical conformation in membranes with a lipid composition resembling mitochondrial outer membrane contact sites. However, unlike colicins and the transmembrane domain of diphtheria toxin, these helices of BID are bound to the lipid bilayer without adopting a transmembrane orientation.

Accession Number:NP_001187.1
Protein Name:NP_001187.1 BH3-interacting domain death agonist isoform 2 [Homo sapiens]
Length:196
Molecular Weight:
Species:Homo sapiens [9606]
Substrate

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FASTA formatted sequence
1:	MDCEVNNGSS LRDECITNLL VFGFLQSCSD NSFRRELDAL GHELPVLAPQ WEGYDELQTD 
61:	GNRSSHSRLG RIEADSESQE DIIRNIARHL AQVGDSMDRS IPPGLVNGLA LQLRNTSRSE 
121:	EDRNRDLATA LEQLLQAYPR DMEKEKTMLV LALLLAKKVA SHTPSLLRDV FHTTVNFINQ 
181:	NLRTYVRSLA RNGMD