CED9_CAEBR
ID CED9_CAEBR Reviewed; 266 AA.
AC P41957; A8WL37; Q60JB2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Apoptosis regulator ced-9;
DE AltName: Full=Cell death protein 9;
GN Name=ced-9; ORFNames=CBG24606;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7907274; DOI=10.1016/0092-8674(94)90506-1;
RA Hengartner M.O., Horvitz H.R.;
RT "C. elegans cell survival gene ced-9 encodes a functional homolog of the
RT mammalian proto-oncogene bcl-2.";
RL Cell 76:665-676(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Plays a major role in programmed cell death (PCD, apoptosis).
CC egl-1 binds to and directly inhibits the activity of ced-9, releasing
CC the cell death activator ced-4 from a ced-9/ced-4 containing protein
CC complex and allowing ced-4 to activate the cell-killing caspase ced-3.
CC During larval development, required for the elimination of transient
CC presynaptic components downstream of egl-1 and upstream of ced-4 and
CC ced-3 apoptotic pathway. {ECO:0000250|UniProtKB:P41958}.
CC -!- SUBUNIT: Interacts with asymmetric homodimer ced-4; the interaction
CC sequesters ced-4. Interacts with egl-1; the interaction results in ced-
CC 4 release. Interacts with dre-1; the interaction inhibits ced-9
CC activity, either directly or indirectly. Interacts with dct-1. May form
CC a complex composed of ced-9, ced-4 and mac-1.
CC {ECO:0000250|UniProtKB:P41958}.
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000250|UniProtKB:P41958}.
CC Synapse {ECO:0000250|UniProtKB:P41958}. Endomembrane system
CC {ECO:0000250|UniProtKB:P41958}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P41958}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P41958}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P41958}. Note=Intracellular membranes,
CC mitochondrial, and perinuclear region. Localizes to synapses of DD
CC motor neurons. Synaptic localization is dependent on axonal
CC mitochondria. {ECO:0000250|UniProtKB:P41958}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20077.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L26546; AAA20077.1; ALT_INIT; Unassigned_DNA.
DR EMBL; HE601354; CAP21182.3; -; Genomic_DNA.
DR RefSeq; XP_002641306.1; XM_002641260.1.
DR AlphaFoldDB; P41957; -.
DR SMR; P41957; -.
DR STRING; 6238.CBG24606; -.
DR EnsemblMetazoa; CBG24606.1; CBG24606.1; WBGene00042676.
DR GeneID; 8583298; -.
DR KEGG; cbr:CBG_24606; -.
DR CTD; 8583298; -.
DR WormBase; CBG24606; CBP12970; WBGene00042676; Cbr-ced-9.
DR eggNOG; KOG4728; Eukaryota.
DR HOGENOM; CLU_1046733_0_0_1; -.
DR InParanoid; P41957; -.
DR OMA; KEHNRSW; -.
DR OrthoDB; 1218929at2759; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
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; 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; IPR003093; Bcl2_BH4.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR Pfam; PF02180; BH4; 1.
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; PS50063; BH4_2; 1.
PE 3: Inferred from homology;
KW Apoptosis; Membrane; Mitochondrion; Reference proteome; Synapse.
FT CHAIN 1..266
FT /note="Apoptosis regulator ced-9"
FT /id="PRO_0000143096"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 75..94
FT /note="BH4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00025"
FT MOTIF 156..174
FT /note="BH1"
FT /evidence="ECO:0000255"
FT MOTIF 208..223
FT /note="BH2"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 266 AA; 30640 MW; FF30C60C399322C1 CRC64;
MVDSMDMANS SQNTFRRRTM ATSEMREFLS TKDAEPNNFG MQTIPESPTP STPTRRMSIG
DSTRIYDWEE PRFNIQGFVV DYFTYRIAQN GLDWYDAPAL PDGVQKEHEM MRSLGTIFEK
RHMEMFENFS EQLLAVPKIS FSLYQEVVQT VGNSSNTPCP MSYGRLIGLI SFGGMVAAKM
MESAELQGQV RNLLMYTSLF IKTRIRQSWK EHNRSWADFM KLGQQMKEDY EKEKDAEEGK
RLKSWSIIGA SVIAVIVCGR IIFSFK
