B2CL2_BOVIN
ID B2CL2_BOVIN Reviewed; 193 AA.
AC Q1RMX3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Bcl-2-like protein 2;
DE Short=Bcl2-L-2;
DE AltName: Full=Apoptosis regulator Bcl-W;
GN Name=BCL2L2;
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=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) 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; BC114652; AAI14653.1; -; mRNA.
DR RefSeq; NP_001070001.1; NM_001076533.1.
DR RefSeq; XP_005211456.1; XM_005211399.3.
DR RefSeq; XP_015328534.1; XM_015473048.1.
DR PDB; 4K5A; X-ray; 1.50 A; A=2-171.
DR PDB; 4K5B; X-ray; 1.85 A; C/D=2-171.
DR PDBsum; 4K5A; -.
DR PDBsum; 4K5B; -.
DR AlphaFoldDB; Q1RMX3; -.
DR SMR; Q1RMX3; -.
DR STRING; 9913.ENSBTAP00000026248; -.
DR PaxDb; Q1RMX3; -.
DR PRIDE; Q1RMX3; -.
DR Ensembl; ENSBTAT00000026248; ENSBTAP00000026248; ENSBTAG00000019692.
DR GeneID; 767601; -.
DR KEGG; bta:767601; -.
DR CTD; 599; -.
DR VEuPathDB; HostDB:ENSBTAG00000019692; -.
DR VGNC; VGNC:55105; BCL2L2.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244953; -.
DR HOGENOM; CLU_085401_0_2_1; -.
DR InParanoid; Q1RMX3; -.
DR OMA; DVARWMT; -.
DR OrthoDB; 1218929at2759; -.
DR TreeFam; TF315834; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000019692; Expressed in prefrontal cortex and 104 other tissues.
DR GO; GO:0097136; C:Bcl-2 family protein complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
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 GO; GO:0060011; P:Sertoli cell proliferation; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Membrane; Mitochondrion;
KW 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_0000247324"
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"
FT HELIX 8..24
FT /evidence="ECO:0007829|PDB:4K5A"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4K5A"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4K5A"
FT HELIX 41..56
FT /evidence="ECO:0007829|PDB:4K5A"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4K5B"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:4K5A"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4K5A"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:4K5A"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:4K5A"
FT HELIX 93..112
FT /evidence="ECO:0007829|PDB:4K5A"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:4K5A"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:4K5A"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:4K5A"
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
