(data stored in ACNUC9552 zone)

HOGENOM: CANFA8_7_PE31

ID   CANFA8_7_PE31                        STANDARD;      PRT;   208 AA.
AC   CANFA8_7_PE31; Q45T69;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   Flags: Fragments;
DE   RecName: Full=Bcl-2-like protein 2; Short=Bcl2-L-2;AltName:
DE   Full=Apoptosis regulator Bcl-W; (CANFA8_7.PE31).
GN   Name=BCL2L2;
OS   CANIS LUPUS FAMILIARIS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CANFA8_7.PE31.
CC       Canis familiaris chromosome 8 BROADD2 partial sequence 5966512..6966511
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:B2CL2_CANFA
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   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Peripheral membrane
CC       protein (By similarity). Note=Loosely associated with the
CC       mitochondrial membrane in healthy cells. During apoptosis, tightly
CC       bound to the membrane (By similarity).
CC   -!- DOMAIN: The BH4 motif seems to be involved in the anti-apoptotic
CC       function (By similarity).
CC   -!- DOMAIN: The BH1 and BH2 motifs form a hydrophobic groove which
CC       acts as a docking site for the BH3 domain of some pro-apoptotic
CC       proteins. The C-terminal residues of BCL2L2 fold into the BH3-
CC       binding cleft and modulate pro-survival activity by regulating
CC       ligand access. When BH3 domain-containing proteins bind, they
CC       displace the C-terminus, allowing its insertion into the membrane
CC       and neutralizing the pro-survival activity of BCL2L2 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the Bcl-2 family.
CC   -!- GENE_FAMILY: HOG000056452 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Canis_familiaris;ENSCAFG00000011482;ENSCAFT00000018210;ENSCAFP00000016862.
DR   EMBL; DQ116955; - ;
DR   UniProtKB/Swiss-Prot; Q45T69; -.
DR   EMBL; DQ116955; AAZ22484.1; -; mRNA.
DR   UniGene; Cfa.19394; -.
DR   ProteinModelPortal; Q45T69; -.
DR   SMR; Q45T69; 1-183.
DR   STRING; Q45T69; -.
DR   eggNOG; maNOG17557; -.
DR   GeneTree; ENSGT00390000001517; -.
DR   OrthoDB; EOG4RBQKR; -.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0042981; P:regulation of apoptosis; IEA:InterPro.
DR   InterPro; IPR013280; Apop_reg_BclW.
DR   InterPro; IPR002475; Bcl2-like_apoptosis.
DR   InterPro; IPR000712; Bcl2_BH.
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   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   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.
DR   HOGENOMDNA; CANFA8_7.PE31; -.
KW   ENSCAFG00000011482fold_1320000031; ENSCAFP00000016862fold_1320000031;
KW   DQ116955;
KW   Apoptosis; Complete proteome; Membrane; Mitochondrion; Phosphoprotein;
KW   Reference proteome.
SQ   SEQUENCE   208 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     YIHASLSSLT LTAARMATPA SAPDTRALVA DFVGYKLRQK GYVCGAGPGE GPAADPLHQA
     MRAAGDEFET RFRRTFSDLA AQLHVTPGSA QQRFTQVSDE LFQGGPNWGR LVAFFVFGAA
     LCAESVNKEM EPLVGQVQEW MVAYLETRLA DWIHSSGGWA EFTALYGDGA LEEARRLREG
     NWASVRTVLT GAVALGALVT VGAFFASK
//

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