BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like

UniProt data

UniProt name: BNI3L_HUMAN (O60238)

Gene name: BNIP3L; Synonyms=BNIP3A, BNIP3H, NIX

Organism: Homo sapiens (Human).

Function: Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor. {ECO:0000269|PubMed:10381623, ECO:0000269|PubMed:21264228}.

Subcellular location: Nucleus envelope. Endoplasmic reticulum. Mitochondrion outer membrane. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes with SPATA18 at the mitochondrion outer membrane.

Transmembrane domains:

  1. 188-208, 21 AA, Helical. {ECO:0000255}.

Sequence: 219 AA

10 20 30 40 50 60 MSSHLVEPPP PLHNNNNNCE ENEQSLPPPA GLNSSWVELP MNSSNGNDNG NGKNGGLEHV 70 80 90 100 110 120 PSSSSIHNGD MEKILLDAQH ESGQSSSRGS SHCDSPSPQE DGQIMFDVEM HTSRDHSSQS 130 140 150 160 170 180 EEEVVEGEKE VEALKKSADW VSDWSSRPEN IPPKEFHFRH PKRSVSLSMR KSGAMKKGGI 190 200 210 FSAEFLKVFI PSLFLSHVLA LGLGIYIGKR LSTPSASTY

CATM prediction

The sequence of BNI3L_HUMAN returned 2 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
       190       200       21
+    |    +    |    +    | 		 (Å) (°) (Å) (°)  
Model 1 FLKVFIASLFLSHVLALGLGIYIGKRL 6.3 -40.9° 0.0 59.0 -43.1
Model 2 FLKVFIASLFLSHVLALGLGIYIGKRL 7.0 -28.9° 2.5 60.1 -21.9
Prolines* FLKVFIPSLFLSHVLALGLGIYIGKRL          

* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


Click on the image to enlarge

Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 201, LEU, HA A, 200, ALA, O 2.97Å
B, 204, GLY, HA1 A, 201, LEU, O 2.72Å
B, 205, ILE, HA A, 204, GLY, O 2.45Å
B, 208, GLY, HA1 A, 205, ILE, O 3.37Å
A, 201, LEU, HA B, 200, ALA, O 2.97Å
A, 204, GLY, HA1 B, 201, LEU, O 2.72Å
A, 205, ILE, HA B, 204, GLY, O 2.45Å
A, 208, GLY, HA1 B, 205, ILE, O 3.37Å