UniProt data
UniProt name: BNIP3_HUMAN (Q12983)
Gene name: BNIP3; Synonyms=NIP3
Organism: Homo sapiens (Human).
Function: Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2. 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. Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway. {ECO:0000269|PubMed:19935772, ECO:0000269|PubMed:22292033}.
Subcellular location: Mitochondrion. Mitochondrion outer membrane; Single-pass membrane protein. Note=Coexpression with the EIB 19- kDa protein results in a shift in NIP3 localization pattern to the nuclear envelope. Colocalizes with ACAA2 in the mitochondria. Colocalizes with SPATA18 at the mitochondrion outer membrane.
Transmembrane domains:
- 164-184, 21 AA, Helical. {ECO:0000255}.
Sequence: 194 AA
CATM prediction
The sequence of BNIP3_HUMAN returned 1 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 |
|---|---|---|---|---|---|---|
| 170 180 + | + | + |
(Å) | (°) | (Å) | (°) | ||
| Model 1 | FLKVFLASLLLSHLLAIGLGIYIGRRL | 7.0 | -44.0° | 1.8 | 45.3 | -44.2 |
| Prolines* | FLKVFLPSLLLSHLLAIGLGIYIGRRL |
* 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:
Download model 1 structure: PDB, PyMOL session
List of hydrogen bonds:
| Donor | Acceptor | Distance |
|---|---|---|
| B, 173, HSE, HE2 | A, 172, SER, OG | 2.43Å |
| B, 177, ILE, HA | A, 176, ALA, O | 3.12Å |
| B, 180, GLY, HA1 | A, 177, ILE, O | 2.85Å |
| B, 181, ILE, HA | A, 180, GLY, O | 3.02Å |
| A, 173, HSE, HE2 | B, 172, SER, OG | 2.43Å |
| A, 177, ILE, HA | B, 176, ALA, O | 3.12Å |
| A, 180, GLY, HA1 | B, 177, ILE, O | 2.85Å |
| A, 181, ILE, HA | B, 180, GLY, O | 3.02Å |

