CED8_CAEBR
ID CED8_CAEBR Reviewed; 460 AA.
AC A8Y2U2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Cell death abnormality protein 8 {ECO:0000250|UniProtKB:O17386};
GN Name=ced-8 {ECO:0000312|EMBL:CAP39278.1}; ORFNames=CBG22761;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP39278.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP39278.1};
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: Acts downstream of ced-9 and caspase ced-3 to promote
CC phosphatidylserine exposure on apoptotic cell surface, possibly by
CC mediating phospholipid scrambling. Phosphatidylserine is a specific
CC marker only present at the surface of apoptotic cells and acts as a
CC specific signal for engulfment. Regulates apoptosis kinetics during
CC embryonic development. Not required for engulfment of germ cell
CC corpses. {ECO:0000250|UniProtKB:O17386}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O17386};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O17386}.
CC -!- PTM: Cleavage by ced-3 activates ced-8 function in promoting
CC phosphatidylserine exposure at the surface of apoptotic cells.
CC {ECO:0000250|UniProtKB:O17386}.
CC -!- SIMILARITY: Belongs to the XK family. {ECO:0000255}.
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DR EMBL; HE601156; CAP39278.1; -; Genomic_DNA.
DR RefSeq; XP_002645508.1; XM_002645462.1.
DR AlphaFoldDB; A8Y2U2; -.
DR SMR; A8Y2U2; -.
DR STRING; 6238.CBG22761; -.
DR EnsemblMetazoa; CBG22761.1; CBG22761.1; WBGene00041249.
DR GeneID; 8587507; -.
DR KEGG; cbr:CBG_22761; -.
DR CTD; 8587507; -.
DR WormBase; CBG22761; CBP20492; WBGene00041249; Cbr-ced-8.
DR eggNOG; KOG4790; Eukaryota.
DR HOGENOM; CLU_028534_5_0_1; -.
DR InParanoid; A8Y2U2; -.
DR OMA; NIWPHEA; -.
DR OrthoDB; 1230316at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0017128; F:phospholipid scramblase activity; IEA:EnsemblMetazoa.
DR GO; GO:1902742; P:apoptotic process involved in development; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IBA:GO_Central.
DR GO; GO:0097194; P:execution phase of apoptosis; ISS:UniProtKB.
DR GO; GO:0070782; P:phosphatidylserine exposure on apoptotic cell surface; IBA:GO_Central.
DR GO; GO:0012501; P:programmed cell death; ISS:UniProtKB.
DR InterPro; IPR018629; XK-rel.
DR Pfam; PF09815; XK-related; 1.
PE 3: Inferred from homology;
KW Apoptosis; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..460
FT /note="Cell death abnormality protein 8"
FT /id="PRO_0000379935"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..77
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..219
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..320
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..378
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT SITE 21..22
FT /note="Cleavage; by ced-3"
FT /evidence="ECO:0000250|UniProtKB:O17386"
SQ SEQUENCE 460 AA; 53816 MW; 498F682EE162A2CC CRC64;
MYLKKHESKL LLIPKNEDKE DAGIIAVLTD RVPSVLIVRW FDLFCFGFAM CSYVLDFFSD
IGIAIFHFWA GRHLSGALVL TFALIPSVII NIISMVWMLD DEMHWKRRAH PRRTGTFELN
QKRFISLGKM ITLCIFQMGP LFWYYKALYY GWMFTKNKKD DTDKEKRKFF MKMVEAERDA
TLLRFFEAFL ESAPQLIIQG SIAANYFQNY YISGKYPYWL YFQAASLTLS IISISWSVVV
QNRSLRMTRD DKVNIWPHEA VLQFCWRFLT ILARIITLVA FVLLFGIYVV FLIFGHLIVT
LVHVIFLQAL HIEACTHIEK LLLLINAMIH LFTPFNMAEG NTRYRYLVAY TVEFIEMMII
FLLLPTPLDA FPLIEKIRIG VPATFFIGIF IMLIYYKFFH PNRRQDLEAP NVERNEKLVV
SELNGIPSAA IEKAEHIEEI EEHSVPTTSE SLLEEDECHN
