BNIP3_BOVIN
ID BNIP3_BOVIN Reviewed; 196 AA.
AC Q32KN2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 {ECO:0000250|UniProtKB:Q12983};
GN Name=BNIP3 {ECO:0000250|UniProtKB:Q12983};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Apoptosis-inducing protein that can overcome BCL2
CC suppression. May play a role in repartitioning calcium between the two
CC major intracellular calcium stores in association with BCL2 (By
CC similarity). Involved in mitochondrial quality control via its
CC interaction with SPATA18/MIEAP: in response to mitochondrial damage,
CC participates in mitochondrial protein catabolic process (also named
CC MALM) leading to the degradation of damaged proteins inside
CC mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and
CC BNIP3L/NIX at the mitochondrial outer membrane may play a critical role
CC in the translocation of lysosomal proteins from the cytoplasm to the
CC mitochondrial matrix (By similarity). The physical interaction of
CC SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane
CC regulates the opening of a pore in the mitochondrial double membrane in
CC order to mediate the translocation of lysosomal proteins from the
CC cytoplasm to the mitochondrial matrix (By similarity). Plays an
CC important role in the calprotectin (S100A8/A9)-induced cell death
CC pathway (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Binds to BCL2. Interacts with BNIP3L and ACAA2.
CC Interacts (via BH3 domain) with SPATA18 (via coiled-coil domains).
CC Interacts with BOK; promotes BOK oligomerization.
CC {ECO:0000250|UniProtKB:Q12983}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion outer membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC Note=Coexpression with the EIB 19-kDa protein results in a shift in
CC NIP3 localization pattern to the nuclear envelope. Colocalizes with
CC ACAA2 in the mitochondria. Colocalizes with SPATA18 at the
CC mitochondrion outer membrane (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NIP3 family. {ECO:0000305}.
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DR EMBL; BC110012; AAI10013.1; -; mRNA.
DR RefSeq; NP_001069834.1; NM_001076366.1.
DR AlphaFoldDB; Q32KN2; -.
DR BMRB; Q32KN2; -.
DR STRING; 9913.ENSBTAP00000023684; -.
DR PaxDb; Q32KN2; -.
DR PRIDE; Q32KN2; -.
DR GeneID; 615342; -.
DR KEGG; bta:615342; -.
DR CTD; 664; -.
DR eggNOG; ENOG502QQ4B; Eukaryota.
DR InParanoid; Q32KN2; -.
DR OrthoDB; 1250566at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IBA:GO_Central.
DR GO; GO:0043067; P:regulation of programmed cell death; IBA:GO_Central.
DR InterPro; IPR010548; BNIP3.
DR PANTHER; PTHR15186; PTHR15186; 1.
DR Pfam; PF06553; BNIP3; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..196
FT /note="BCL2/adenovirus E1B 19 kDa protein-interacting
FT protein 3"
FT /id="PRO_0000269189"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 47..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 100..125
FT /note="BH3"
FT COMPBIAS 60..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12983"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12983"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12983"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55003"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12983"
SQ SEQUENCE 196 AA; 21886 MW; 0AB2E1AFFEC2AC1C CRC64;
MSQSESPGLQ EESLHGSWVE LHFGSNGNGS SVPDSVSIYK GDMEKILLDA QHESGRSSSK
SSHCDSPPRS QTPQDTNRAS ETDTHSLGEK NSSQSEEDYM ERRKEVESIL KKNSDWIWDW
SSRPENVPPA KEFLLFKHPK RTPTLSMRNT SVMKKGGIFS AEFLKVFLPS LLLSHLLAIG
LGIYIGRRLT TSTSTF
