BNI3L_BOVIN
ID BNI3L_BOVIN Reviewed; 219 AA.
AC Q3T013; A5D9C5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like;
GN Name=BNIP3L;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Induces apoptosis. Interacts with viral and cellular anti-
CC apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL,
CC although high levels of BCL-XL expression will inhibit apoptosis.
CC Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality
CC control via its interaction with SPATA18/MIEAP: in response to
CC mitochondrial damage, participates in mitochondrial protein catabolic
CC process (also named MALM) leading to the degradation of damaged
CC proteins inside mitochondria. 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). May function as
CC a tumor suppressor (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Self-associates. Interacts with BNIP3 and STEAP3. Interacts
CC (via BH3 domain) with SPATA18 (via coiled-coil domains) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250}. Endoplasmic
CC reticulum {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}.
CC Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC Note=Colocalizes with SPATA18 at the mitochondrion outer membrane.
CC {ECO:0000250}.
CC -!- PTM: Undergoes progressive proteolysis to an 11 kDa C-terminal
CC fragment, which is blocked by the proteasome inhibitor lactacystin.
CC -!- SIMILARITY: Belongs to the NIP3 family. {ECO:0000305}.
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DR EMBL; BT030544; ABQ12984.1; -; mRNA.
DR EMBL; BC102612; AAI02613.1; -; mRNA.
DR RefSeq; NP_001029786.1; NM_001034614.2.
DR AlphaFoldDB; Q3T013; -.
DR SMR; Q3T013; -.
DR STRING; 9913.ENSBTAP00000033770; -.
DR PaxDb; Q3T013; -.
DR PRIDE; Q3T013; -.
DR Ensembl; ENSBTAT00000033862; ENSBTAP00000033770; ENSBTAG00000021307.
DR GeneID; 534615; -.
DR KEGG; bta:534615; -.
DR CTD; 665; -.
DR VEuPathDB; HostDB:ENSBTAG00000021307; -.
DR VGNC; VGNC:26534; BNIP3L.
DR eggNOG; ENOG502R8Q5; Eukaryota.
DR GeneTree; ENSGT00390000013415; -.
DR HOGENOM; CLU_091463_1_1_1; -.
DR InParanoid; Q3T013; -.
DR OMA; LEMNRTH; -.
DR OrthoDB; 1250566at2759; -.
DR TreeFam; TF315424; -.
DR Reactome; R-BTA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000021307; Expressed in granulosa cell and 102 other tissues.
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:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IBA:GO_Central.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
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; Endoplasmic reticulum; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..219
FT /note="BCL2/adenovirus E1B 19 kDa protein-interacting
FT protein 3-like"
FT /id="PRO_0000269188"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 126..148
FT /note="BH3"
FT COMPBIAS 1..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60238"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2F7"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60238"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60238"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60238"
SQ 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
