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

 BNI3L_BOVIN             Reviewed;         219 AA.
Q3T013; A5D9C5;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
25-OCT-2017, entry version 86.
RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like;
Name=BNIP3L;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
-!- 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 (By similarity). May function as a
tumor suppressor (By similarity). {ECO:0000250}.
-!- SUBUNIT: Self-associates. Interacts with BNIP3 and STEAP3.
Interacts (via BH3 domain) with SPATA18 (via coiled-coil domains)
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250}. Endoplasmic
reticulum {ECO:0000250}. Mitochondrion outer membrane
{ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane
protein {ECO:0000305}. Note=Colocalizes with SPATA18 at the
mitochondrion outer membrane. {ECO:0000250}.
-!- PTM: Undergoes progressive proteolysis to an 11 kDa C-terminal
fragment, which is blocked by the proteasome inhibitor
lactacystin.
-!- SIMILARITY: Belongs to the NIP3 family. {ECO:0000305}.
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EMBL; BT030544; ABQ12984.1; -; mRNA.
EMBL; BC102612; AAI02613.1; -; mRNA.
RefSeq; NP_001029786.1; NM_001034614.2.
UniGene; Bt.888; -.
ProteinModelPortal; Q3T013; -.
SMR; Q3T013; -.
STRING; 9913.ENSBTAP00000033770; -.
PaxDb; Q3T013; -.
PRIDE; Q3T013; -.
Ensembl; ENSBTAT00000033862; ENSBTAP00000033770; ENSBTAG00000021307.
GeneID; 534615; -.
KEGG; bta:534615; -.
CTD; 665; -.
eggNOG; ENOG410IK24; Eukaryota.
eggNOG; ENOG4111HIM; LUCA.
GeneTree; ENSGT00390000013415; -.
HOGENOM; HOG000232139; -.
HOVERGEN; HBG050707; -.
InParanoid; Q3T013; -.
KO; K15465; -.
OMA; PQDDGQI; -.
OrthoDB; EOG091G0REJ; -.
TreeFam; TF315424; -.
Reactome; R-BTA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
Proteomes; UP000009136; Chromosome 8.
Bgee; ENSBTAG00000021307; -.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
GO; GO:0005521; F:lamin binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IBA:GO_Central.
GO; GO:0035694; P:mitochondrial protein catabolic process; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0043069; P:negative regulation of programmed cell death; IBA:GO_Central.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; IEA:Ensembl.
GO; GO:1903214; P:regulation of protein targeting to mitochondrion; IEA:Ensembl.
InterPro; IPR010548; BNIP3.
PANTHER; PTHR15186; PTHR15186; 1.
Pfam; PF06553; BNIP3; 1.
2: Evidence at transcript level;
Apoptosis; Complete proteome; Endoplasmic reticulum; Membrane;
Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 219 BCL2/adenovirus E1B 19 kDa protein-
interacting protein 3-like.
/FTId=PRO_0000269188.
TRANSMEM 187 207 Helical. {ECO:0000255}.
MOTIF 126 148 BH3.
MOD_RES 62 62 Phosphoserine.
{ECO:0000250|UniProtKB:O60238}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2F7}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000250|UniProtKB:O60238}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000250|UniProtKB:O60238}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000250|UniProtKB:O60238}.
SEQUENCE 219 AA; 23846 MW; D4EB055BDB198BA6 CRC64;
MSSHLVEQPP PPHNNNNNCE EGEQSLPPPA GLNSSWVELP MNSSNGNDNG NGKNGGLEHV
PSSSSIHNGD MEKILLDAQH ESGQSSSRGS SHCDSPSPQE DGQIMFDVEM HTSKDHSSQS
EEEVAEGEKE VDALKKSVDW VSDWSSRPEN IPPKEFHFRH PKRSVSLSMR KSGAMKKGGI
FSAEFLKVFI PSLFLSHVLA LGLGIYIGKR LSTPSASTY


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