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1.A.21.1.3
The mitochondrial apoptosis-inducing channel-forming protein, BAK. 3-D structures are known (2IMT_A).  Functions like a holin when expressed in bacteria (Pang et al. 2011).  Formation of the apoptotic pore involves a flexible C-terminal domain (Iyer et al. 2015). Bax (and likely Bak) dimers assemble into oligomers with an even number of molecules that fully or partially delineate pores of different sizes to permeabilize the mitochondrial outer membrane (MOM) during apoptosis (Cosentino and García-Sáez 2016). BAK is a C-tail-anchored mitochondrial outer membrane protein (Setoguchi et al. 2006). BAK plays a role in peroxisomal permeability, similar to mitochondrial outer membrane permeabilization (Hosoi et al. 2017).  Uren et al. 2017 reviewed how clusters of dimers and their lipid-mediated interactions provide a molecular explanation for the heterogeneous assemblies of Bak and Bax observed during apoptosis.

Accession Number:Q16611
Protein Name:Bcl-2 homologous antagonist/killer
Length:211
Molecular Weight:23409.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Membrane1 / Single-pass membrane protein2
Substrate cytochrome c, small molecules

Cross database links:

Genevestigator: Q16611
eggNOG: prNOG06556
DIP: DIP-935N
RefSeq: NP_001179.1   
Entrez Gene ID: 578   
Pfam: PF00452   
OMIM: 600516  gene
KEGG: hsa:578   

Gene Ontology

GO:0005741 C:mitochondrial outer membrane
GO:0046930 C:pore complex
GO:0042802 F:identical protein binding
GO:0046872 F:metal ion binding
GO:0046982 F:protein heterodimerization activity
GO:0010248 P:establishment or maintenance of transmembra...
GO:0006917 P:induction of apoptosis
GO:0046902 P:regulation of mitochondrial membrane permea...
GO:0051881 P:regulation of mitochondrial membrane potential
GO:0043497 P:regulation of protein heterodimerization ac...
GO:0043496 P:regulation of protein homodimerization acti...
GO:0001836 P:release of cytochrome c from mitochondria

References (9)

[1] “Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K.”  Farrow S.N.et.al.   7715729
[2] “Induction of apoptosis by the Bcl-2 homologue Bak.”  Chittenden T.et.al.   7715730
[3] “Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak.”  Kiefer M.C.et.al.   7715731
[4] “The DNA sequence and analysis of human chromosome 6.”  Mungall A.J.et.al.   14574404
[5] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[6] “A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions.”  Chittenden T.et.al.   8521816
[7] “Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis.”  Sattler M.et.al.   9020082
[8] “The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site.”  Moldoveanu T.et.al.   17157251
[9] “A structural viral mimic of prosurvival Bcl-2: a pivotal role for sequestering proapoptotic Bax and Bak.”  Kvansakul M.et.al.   17386268
Structure:
1BXL   2IMS   2IMT   2JBY   2JCN   2YV6   3I1H   2LP8   2M5B   2XPX   [...more]

External Searches:

  • Search: DB with
  • 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)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MASGQGPGPP RQECGEPALP SASEEQVAQD TEEVFRSYVF YRHQQEQEAE GVAAPADPEM 
61:	VTLPLQPSST MGQVGRQLAI IGDDINRRYD SEFQTMLQHL QPTAENAYEY FTKIATSLFE 
121:	SGINWGRVVA LLGFGYRLAL HVYQHGLTGF LGQVTRFVVD FMLHHCIARW IAQRGGWVAA 
181:	LNLGNGPILN VLVVLGVVLL GQFVVRRFFK S