ID   B2CL2_CANLF             Reviewed;         193 AA.
AC   Q45T69;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Bcl-2-like protein 2;
DE            Short=Bcl2-L-2;
DE   AltName: Full=Apoptosis regulator Bcl-W;
GN   Name=BCL2L2;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle; TISSUE=Kidney;
RA   Rickenbacher A.B., Schade B., Keller S.M., Guscetti F.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes cell survival. Blocks dexamethasone-induced
CC       apoptosis. Mediates survival of postmitotic Sertoli cells by
CC       suppressing death-promoting activity of BAX (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with HIF3A (via C-terminus domain). Interacts with
CC       BOP. {ECO:0000250|UniProtKB:P70345}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Note=Loosely associated with the
CC       mitochondrial membrane in healthy cells. During apoptosis, tightly
CC       bound to the membrane (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The BH4 motif seems to be involved in the anti-apoptotic
CC       function. {ECO:0000250}.
CC   -!- DOMAIN: The BH1 and BH2 motifs form a hydrophobic groove which acts as
CC       a docking site for the BH3 domain of some pro-apoptotic proteins. The
CC       C-terminal residues of BCL2L2 fold into the BH3-binding cleft and
CC       modulate pro-survival activity by regulating ligand access. When BH3
CC       domain-containing proteins bind, they displace the C-terminus, allowing
CC       its insertion into the membrane and neutralizing the pro-survival
CC       activity of BCL2L2 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ116955; AAZ22484.1; -; mRNA.
DR   RefSeq; NP_001026805.1; NM_001031635.2.
DR   RefSeq; XP_005623259.1; XM_005623202.2.
DR   AlphaFoldDB; Q45T69; -.
DR   SMR; Q45T69; -.
DR   STRING; 9612.ENSCAFP00000016862; -.
DR   PaxDb; Q45T69; -.
DR   Ensembl; ENSCAFT00030028970; ENSCAFP00030025256; ENSCAFG00030015644.
DR   Ensembl; ENSCAFT00040004280; ENSCAFP00040003678; ENSCAFG00040002254.
DR   Ensembl; ENSCAFT00845005930; ENSCAFP00845004717; ENSCAFG00845003335.
DR   GeneID; 490611; -.
DR   KEGG; cfa:490611; -.
DR   CTD; 599; -.
DR   VEuPathDB; HostDB:ENSCAFG00845003335; -.
DR   eggNOG; KOG4728; Eukaryota.
DR   GeneTree; ENSGT00940000154606; -.
DR   HOGENOM; CLU_085401_0_2_1; -.
DR   InParanoid; Q45T69; -.
DR   OMA; DVARWMT; -.
DR   OrthoDB; 1218929at2759; -.
DR   TreeFam; TF315834; -.
DR   Proteomes; UP000002254; Chromosome 8.
DR   Bgee; ENSCAFG00000011482; Expressed in testis and 47 other tissues.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR   GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR   CDD; cd06845; Bcl-2_like; 1.
DR   Gene3D; 1.10.437.10; -; 1.
DR   InterPro; IPR013280; Apop_reg_BclW.
DR   InterPro; IPR036834; Bcl-2-like_sf.
DR   InterPro; IPR046371; Bcl-2_BH1-3.
DR   InterPro; IPR026298; Bcl-2_fam.
DR   InterPro; IPR002475; Bcl2-like.
DR   InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR   InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR   InterPro; IPR003093; Bcl2_BH4.
DR   InterPro; IPR020731; Bcl2_BH4_motif_CS.
DR   PANTHER; PTHR11256; PTHR11256; 1.
DR   PANTHER; PTHR11256:SF51; PTHR11256:SF51; 1.
DR   Pfam; PF00452; Bcl-2; 1.
DR   Pfam; PF02180; BH4; 1.
DR   PRINTS; PR01865; APOPREGBCLW.
DR   PRINTS; PR01862; BCL2FAMILY.
DR   SMART; SM00337; BCL; 1.
DR   SMART; SM00265; BH4; 1.
DR   SUPFAM; SSF56854; SSF56854; 1.
DR   PROSITE; PS50062; BCL2_FAMILY; 1.
DR   PROSITE; PS01080; BH1; 1.
DR   PROSITE; PS01258; BH2; 1.
DR   PROSITE; PS01260; BH4_1; 1.
DR   PROSITE; PS50063; BH4_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Apoptosis; Membrane; Mitochondrion; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q92843"
FT   CHAIN           2..193
FT                   /note="Bcl-2-like protein 2"
FT                   /id="PRO_0000247325"
FT   MOTIF           9..29
FT                   /note="BH4"
FT   MOTIF           85..104
FT                   /note="BH1"
FT   MOTIF           136..151
FT                   /note="BH2"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92843"
SQ   SEQUENCE   193 AA;  20774 MW;  3792243A50281761 CRC64;
     MATPASAPDT RALVADFVGY KLRQKGYVCG AGPGEGPAAD PLHQAMRAAG DEFETRFRRT
     FSDLAAQLHV TPGSAQQRFT QVSDELFQGG PNWGRLVAFF VFGAALCAES VNKEMEPLVG
     QVQEWMVAYL ETRLADWIHS SGGWAEFTAL YGDGALEEAR RLREGNWASV RTVLTGAVAL
     GALVTVGAFF ASK