BCL2/adenovirus E1B 19 kDa protein-interacting protein 3

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:

  1. 164-184, 21 AA, Helical. {ECO:0000255}.

Sequence: 194 AA

10 20 30 40 50 60 MSQNGAPGMQ EESLQGSWVE LHFSNNGNGG SVPASVSIYN GDMEKILLDA QHESGRSSSK 70 80 90 100 110 120 SSHCDSPPRS QTPQDTNRAS ETDTHSIGEK NSSQSEEDDI ERRKEVESIL KKNSDWIWDW 130 140 150 160 170 180 SSRPENIPPK EFLFKHPKRT ATLSMRNTSV MKKGGIFSAE FLKVFLPSLL LSHLLAIGLG 190 IYIGRRLTTS TSTF

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) (°)  
FLKVFLASLLLSHLLAIGLGIYIGRRL 7.0 -44.0° 1.8 45.3 -44.2
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:


Click on the image to enlarge

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