CED6_CAEEL
ID CED6_CAEEL Reviewed; 492 AA.
AC O76337; O01421;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cell death protein 6;
DE AltName: Full=Candidate adapter protein ced-6;
GN Name=ced-6 {ECO:0000312|WormBase:F56D2.7};
GN ORFNames=F56D2.7 {ECO:0000312|WormBase:F56D2.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9635426; DOI=10.1016/s0092-8674(00)81202-7;
RA Liu Q.A., Hengartner M.O.;
RT "Candidate adaptor protein CED-6 promotes the engulfment of apoptotic cells
RT in C. elegans.";
RL Cell 93:961-972(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP SUBUNIT, AND MUTAGENESIS OF LEU-208 AND LEU-215.
RX PubMed=10734103; DOI=10.1074/jbc.275.13.9542;
RA Su H.P., Brugnera E., Van Criekinge W., Smits E., Hengartner M.,
RA Bogaert T., Ravichandran K.S.;
RT "Identification and characterization of a dimerization domain in CED-6, an
RT adapter protein involved in engulfment of apoptotic cells.";
RL J. Biol. Chem. 275:9542-9549(2000).
RN [4]
RP INTERACTION WITH CED-1.
RX PubMed=11729193; DOI=10.1074/jbc.m109336200;
RA Su H.P., Nakada-Tsukui K., Tosello-Trampont A.-C., Li Y., Bu G.,
RA Henson P.M., Ravichandran K.S.;
RT "Interaction of CED-6/GULP, an adapter protein involved in engulfment of
RT apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-
RT related protein (LRP).";
RL J. Biol. Chem. 277:11772-11779(2002).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15744306; DOI=10.1038/nature03263;
RA Kinchen J.M., Cabello J., Klingele D., Wong K., Feichtinger R.,
RA Schnabel H., Schnabel R., Hengartner M.O.;
RT "Two pathways converge at CED-10 to mediate actin rearrangement and corpse
RT removal in C. elegans.";
RL Nature 434:93-99(2005).
RN [6]
RP FUNCTION.
RX PubMed=29346382; DOI=10.1371/journal.pgen.1007125;
RA Offenburger S.L., Ho X.Y., Tachie-Menson T., Coakley S., Hilliard M.A.,
RA Gartner A.;
RT "6-OHDA-induced dopaminergic neurodegeneration in Caenorhabditis elegans is
RT promoted by the engulfment pathway and inhibited by the transthyretin-
RT related protein TTR-33.";
RL PLoS Genet. 14:E1007125-E1007125(2018).
CC -!- FUNCTION: May function as an adapter protein in a pathway that mediates
CC recognition and phagocytosis of apoptotic cells during normal
CC development. Promotes engulfment of cells at both early and late stages
CC of apoptosis. Required for actin reorganization around apoptotic cells.
CC Plays a role in protecting dopaminergic neurons from oxidative stress-
CC induced degeneration (PubMed:29346382). {ECO:0000269|PubMed:15744306,
CC ECO:0000269|PubMed:29346382, ECO:0000269|PubMed:9635426}.
CC -!- SUBUNIT: Homodimer. Interacts with ced-1. {ECO:0000269|PubMed:10734103,
CC ECO:0000269|PubMed:11729193}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15744306}.
CC -!- TISSUE SPECIFICITY: Detected in gonadal sheath cells.
CC {ECO:0000269|PubMed:9635426}.
CC -!- SIMILARITY: Belongs to the ced-6 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; AF061513; AAC24362.1; -; mRNA.
DR EMBL; BX284603; CCD63140.1; -; Genomic_DNA.
DR PIR; T16484; T16484.
DR PIR; T43064; T43064.
DR RefSeq; NP_498203.2; NM_065802.8.
DR AlphaFoldDB; O76337; -.
DR SMR; O76337; -.
DR BioGRID; 41002; 10.
DR ELM; O76337; -.
DR IntAct; O76337; 4.
DR MINT; O76337; -.
DR STRING; 6239.F56D2.7; -.
DR iPTMnet; O76337; -.
DR EPD; O76337; -.
DR PaxDb; O76337; -.
DR PeptideAtlas; O76337; -.
DR PRIDE; O76337; -.
DR EnsemblMetazoa; F56D2.7.1; F56D2.7.1; WBGene00000420.
DR GeneID; 175773; -.
DR KEGG; cel:CELE_F56D2.7; -.
DR UCSC; F56D2.7; c. elegans.
DR CTD; 35971; -.
DR WormBase; F56D2.7; CE33657; WBGene00000420; ced-6.
DR eggNOG; KOG3536; Eukaryota.
DR GeneTree; ENSGT00940000156186; -.
DR HOGENOM; CLU_539941_0_0_1; -.
DR InParanoid; O76337; -.
DR OMA; CYAFTSE; -.
DR OrthoDB; 920757at2759; -.
DR SignaLink; O76337; -.
DR PRO; PR:O76337; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000420; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:WormBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:WormBase.
DR GO; GO:0035615; F:clathrin adaptor activity; IPI:WormBase.
DR GO; GO:0005124; F:scavenger receptor binding; IPI:WormBase.
DR GO; GO:1902742; P:apoptotic process involved in development; IMP:UniProtKB.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IMP:WormBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
DR GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IMP:UniProtKB.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IGI:UniProtKB.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; IMP:WormBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Developmental protein; Phagocytosis;
KW Reference proteome.
FT CHAIN 1..492
FT /note="Cell death protein 6"
FT /id="PRO_0000296683"
FT DOMAIN 55..215
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 19..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..271
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 208
FT /note="L->P: Loss of dimerization; when associated with P-
FT 215."
FT /evidence="ECO:0000269|PubMed:10734103"
FT MUTAGEN 215
FT /note="L->P: Loss of dimerization; when associated with P-
FT 208."
FT /evidence="ECO:0000269|PubMed:10734103"
SQ SEQUENCE 492 AA; 52808 MW; 578C318D8268EF96 CRC64;
MAKDIYKTFK RSVSGIVGGN NINGEGSSSP STSAPQVKYR GGTGRTWIHP PDYLINGHVE
YVARFLGCVE TPKANGSDVA REAIHAIRFQ RDLKRSEQTR ETAKLQKVEI RISIDNVIIA
DIKTKAPMYT FPLGRISFCA DDKDDKRMFS FIARAEGASG KPSCYAFTSE KLAEDITLTI
GEAFDLAYKR FLDKNRTSLE NQKQIYILKK KIVELETENQ VLIERLAEAL RANSKADYEN
TGPPIYPGLG PPALPLSPMP QGPPPNIPPS SIYSMPRAND LPPTEMAPTL PQISTSSNGA
SPSVSPASTS PSGPAPSIPP PRPPALAPPP PVAPRRNPVV SPKNSTAGLL DGLELGSAEP
AKKAPSNIFD DSFDPRAGEK KSTAAEYNPF GADFLSGIQN GKEAPPSASA ELLASEAIAR
LPKPESSSVP PKKTAAEYDA MINEVEKKLA AMSSGSFEFG QLQTGDLGGI EGESDYGTPS
DRLNPKMMNL KQ
