(data stored in ACNUC9552 zone)

HOGENOM: CHICK2_PE1048

ID   CHICK2_PE1048                        STANDARD;      PRT;   233 AA.
AC   CHICK2_PE1048; Q00709;
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   RecName: Full=Apoptosis regulator Bcl-2; (CHICK2.PE1048).
GN   Name=BCL2; Synonyms=BCL-2;
OS   GALLUS GALLUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Sauropsida; Sauria; Archosauria;
OC   Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae;
OC   Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHICK2.PE1048.
CC       Gallus gallus chromosome 2 WASHUC2  sequence 1..154873767 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:BCL2_CHICK
CC   -!- FUNCTION: Suppresses apoptosis in a variety of cell systems
CC       including factor-dependent lymphohematopoietic and neural cells.
CC       Regulates cell death by controlling the mitochondrial membrane
CC       permeability. Appears to function in a feedback loop system with
CC       caspases. Inhibits caspase activity either by preventing the
CC       release of cytochrome c from the mitochondria and/or by binding to
CC       the apoptosis-activating factor (APAF-1).
CC   -!- SUBUNIT: Forms homodimers, and heterodimers with BAX, BAD, BAK and
CC       Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2
CC       motifs, and is necessary for anti-apoptotic activity (By
CC       similarity). Also interacts with APAF1 and RAF-1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       membrane protein. Nucleus membrane; Single-pass membrane protein.
CC       Endoplasmic reticulum membrane; Single-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: In adult chicken expressed, in thymus, spleen,
CC       kidney, heart, ovary and brain, with the highest levels in the
CC       thymus. In the embryo, highly levels expressed in all tissues with
CC       high levels in the bursa of Fabricius.
CC   -!- DOMAIN: The BH4 motif is required for anti-apoptotic activity and
CC       for interaction with RAF-1 (By similarity).
CC   -!- SIMILARITY: Belongs to the Bcl-2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA78018.1; Type=Frameshift; Positions=63, 82;
CC   -!- GENE_FAMILY: HOG000056452 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Gallus_gallus;ENSGALG00000012885;ENSGALT00000021014;ENSGALP00000020984.
DR   EMBL; D11382; - ;
DR   EMBL; Z11961; - ;
DR   UniProtKB/Swiss-Prot; Q00709; -.
DR   EMBL; D11382; BAA01978.1; -; Genomic_DNA.
DR   EMBL; Z11961; CAA78018.1; ALT_FRAME; mRNA.
DR   IPI; IPI00601515; -.
DR   PIR; A37332; A37332.
DR   PIR; S24390; S24390.
DR   RefSeq; NP_990670.1; NM_205339.1.
DR   UniGene; Gga.43243; -.
DR   ProteinModelPortal; Q00709; -.
DR   SMR; Q00709; 3-201.
DR   STRING; Q00709; -.
DR   Ensembl; ENSGALT00000021014; ENSGALP00000020984; ENSGALG00000012885.
DR   GeneID; 396282; -.
DR   KEGG; gga:396282; -.
DR   CTD; 596; -.
DR   eggNOG; veNOG14794; -.
DR   GeneTree; ENSGT00530000062935; -.
DR   InParanoid; Q00709; -.
DR   OMA; EWDAGDA; -.
DR   PhylomeDB; Q00709; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006916; P:anti-apoptosis; ISS:UniProtKB.
DR   GO; GO:0032848; P:negative regulation of cellular pH reduction; ISS:UniProtKB.
DR   GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:HGNC.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:HGNC.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; ISS:HGNC.
DR   InterPro; IPR013278; Apop_reg_Bcl2.
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; IPR020728; Bcl2_BH3_motif_CS.
DR   InterPro; IPR003093; Bcl2_BH4.
DR   InterPro; IPR020731; Bcl2_BH4_motif_CS.
DR   InterPro; IPR004725; Bcl2_reg.
DR   Pfam; PF00452; Bcl-2; 1.
DR   Pfam; PF02180; BH4; 1.
DR   PRINTS; PR01863; APOPREGBCL2.
DR   PRINTS; PR01862; BCL2FAMILY.
DR   SMART; SM00337; BCL; 1.
DR   SMART; SM00265; BH4; 1.
DR   TIGRFAMs; TIGR00865; Bcl-2; 1.
DR   PROSITE; PS50062; BCL2_FAMILY; 1.
DR   PROSITE; PS01080; BH1; 1.
DR   PROSITE; PS01258; BH2; 1.
DR   PROSITE; PS01259; BH3; 1.
DR   PROSITE; PS01260; BH4_1; 1.
DR   PROSITE; PS50063; BH4_2; 1.
DR   HOGENOMDNA; CHICK2.PE1048; -.
KW   ENSGALG00000012885fold_1320000031; ENSGALP00000020984fold_1320000031;
KW   D11382; Z11961;
KW   Apoptosis; Complete proteome; Endoplasmic reticulum; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Nucleus;
KW   Reference proteome; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   233 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAHPGRRGYD NREIVLKYIH YKLSQRGYDW AAGEDRPPVP PAPAPAAAPA AVAAAGASSH
     HRPEPPGSAA ASEVPPAEGL RPAPPGVHLA LRQAGDEFSR RYQRDFAQMS GQLHLTPFTA
     HGRFVAVVEE LFRDGVNWGR IVAFFEFGGV MCVESVNREM SPLVDNIATW MTEYLNRHLH
     NWIQDNGGWD AFVELYGNSM RPLFDFSWIS LKTILSLVLV GACITLGAYL GHK
//

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