ID CED1_CAEBR Reviewed; 1134 AA.
AC A8XMW6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Cell death abnormality protein 1 {ECO:0000250|UniProtKB:Q9XWD6};
DE Flags: Precursor;
GN Name=ced-1 {ECO:0000312|EMBL:CAP33991.2}; ORFNames=CBG15845;
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:CAP33991.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP33991.2};
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: Involved in programmed cell death/apoptosis. Acts by
CC recruiting ced-6 to phagosomes which enables actin-dependent
CC cytoskeletal reorganization and subsequent engulfment of the apoptotic
CC cell corpse. Has a role in the association of ppk-3 and rab-7 with the
CC phagosomal surface which is necessary for the incorporation of
CC lysosomes to phagosomes during phagosome maturation. Activates the
CC expression of unfolded protein response genes, which are involved in
CC the immune response to live bacteria (By similarity).
CC {ECO:0000250|UniProtKB:Q9XWD6}.
CC -!- SUBUNIT: Interacts (via C-terminus) with ced-6 (via PTB domain).
CC {ECO:0000250|UniProtKB:Q9XWD6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9XWD6,
CC ECO:0000255}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9XWD6, ECO:0000255}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000250|UniProtKB:Q9XWD6, ECO:0000255}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:Q9XWD6,
CC ECO:0000255}. Note=Colocalizes with ced-6 and actin halos around early
CC apoptotic cells. Temporally colocalizes with dyn-1 during engulfment of
CC cell corpses (By similarity). {ECO:0000250|UniProtKB:Q9XWD6,
CC ECO:0000255}.
CC -!- PTM: Phosphorylation of Tyr-1021, within the YXXL motif, is thought to
CC initiate phagosomal formation. {ECO:0000250|UniProtKB:Q9XWD6}.
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DR EMBL; HE600911; CAP33991.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XMW6; -.
DR SMR; A8XMW6; -.
DR STRING; 6238.A8XMW6; -.
DR GlyCosmos; A8XMW6; 3 sites, No reported glycans.
DR WormBase; CBG15845a; CBP40325; WBGene00035967; Cbr-ced-1.
DR eggNOG; KOG1218; Eukaryota.
DR HOGENOM; CLU_008281_2_0_1; -.
DR InParanoid; A8XMW6; -.
DR OMA; CGKEAHF; -.
DR OrthoDB; 2540323at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0034620; P:cellular response to unfolded protein; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0043652; P:engulfment of apoptotic cell; ISS:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; ISS:UniProtKB.
DR GO; GO:0001845; P:phagolysosome assembly; ISS:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; ISS:UniProtKB.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 6.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR042635; MEGF10/SREC1/2-like.
DR PANTHER; PTHR24043:SF8; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24043; SCAVENGER RECEPTOR CLASS F; 1.
DR Pfam; PF00053; Laminin_EGF; 4.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 13.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS51041; EMI; 1.
PE 3: Inferred from homology;
KW Apoptosis; Cell membrane; Cytoplasmic vesicle; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1134
FT /note="Cell death abnormality protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000379931"
FT TOPO_DOM 21..912
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 913..933
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 934..1134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..123
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 113..148
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 156..191
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 199..233
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 246..276
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 553..587
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 629..682
FT /note="FU"
FT /evidence="ECO:0000255"
FT REGION 941..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 964..967
FT /note="NPXY"
FT /evidence="ECO:0000255"
FT MOTIF 1021..1024
FT /note="YXXL"
FT /evidence="ECO:0000255"
FT COMPBIAS 1033..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1021
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9XWD6"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..106
FT /evidence="ECO:0000255"
FT DISULFID 71..80
FT /evidence="ECO:0000255"
FT DISULFID 105..117
FT /evidence="ECO:0000255"
FT DISULFID 121..130
FT /evidence="ECO:0000255"
FT DISULFID 125..136
FT /evidence="ECO:0000255"
FT DISULFID 138..147
FT /evidence="ECO:0000255"
FT DISULFID 160..172
FT /evidence="ECO:0000255"
FT DISULFID 166..179
FT /evidence="ECO:0000255"
FT DISULFID 181..190
FT /evidence="ECO:0000255"
FT DISULFID 203..215
FT /evidence="ECO:0000255"
FT DISULFID 209..221
FT /evidence="ECO:0000255"
FT DISULFID 223..232
FT /evidence="ECO:0000255"
FT DISULFID 249..257
FT /evidence="ECO:0000255"
FT DISULFID 251..264
FT /evidence="ECO:0000255"
FT DISULFID 266..275
FT /evidence="ECO:0000255"
FT DISULFID 557..568
FT /evidence="ECO:0000255"
FT DISULFID 561..575
FT /evidence="ECO:0000255"
FT DISULFID 577..586
FT /evidence="ECO:0000255"
SQ SEQUENCE 1134 AA; 121087 MW; 8DC6C35B9D06DFEF CRC64;
MRLLLLVGVL LAATWQVGYT RAPTFPDKSK SAADAINEPK GEHVCTVKTI VDDYELRKVI
HQVVYNDTEQ CLNPLTGFQC VVEKRGQKAS YQRQLVQKEK YIKQCCEGYY QTKDNQCQPD
CNPPCKKGKC VEPGKCECDP GFGGKICSSS CSIGTWGLGC SKKCDCENGA NCDPELGDCI
CPSGFQGKRC EEECPIDKWG PNCVKSCPCQ NGGKCNHEGK CVCTDGWGGE YCLNKCEEGK
FGADCKFECT CQNGATCDNT NGKCLCKSGF HGALCEKPCS EGFFGAGCTQ KCQCLNNQDC
DSETGECKCI GWTGKQCDIG CARGRFGLQC KQKCTCPGLE FQDSNASCDA KTGECQCESG
YKGANCDERK CSADTYGADC SKQCSCVMSN TVMCAPNTGF CRCKPGFYGD NCELACSKDS
YGPNCEKQAM CDWTHASEAD PANGKCVCKS GRSGANCSQP CPIDFYGPNC ALQCECNGRG
IGCHGFDGKC NCAPGYTGHR CEHHCPALTF GANCEKRCQC PAGVGCNPIT GECECPAGRQ
GLKCDISCPE GSYGPECKLH CKCVNGKCDP ETGECSCEPG FGGADCSTSC PKGKYGDACE
LSCDCSDSYC SRQTGKCICP LGKKGTLCDQ PCEANTYGPQ CQLTTTPSQC ASTDPRNGVC
LTCPPGSSGH QCEQNCPQGT YGTDCASKCA CADGGHGCDP TTGECICEPG YHGATCSEKC
PDGKFGYACA QNCPKCAAGS SCDHISGQCV CPAGLEGATC TRPCGVGFWG NGCRQVCRCT
SEFKQCNAQT GECSCPAGFQ GDRCDKPCED GYYGPDCIKK CKCQGTATAS CNRVTGVCIC
HPGFTGEFCH ALCPESTFGL RCSKECPKDG CGDGYECDAA IGCCHVDQMS CGKAKQEFEA
LNGGRAKSSG ATWLLILFII GLCGVLGLAA LFYRNKYQKE KDPDMPTVSF HKSPNAEDNR
EFQNPLYNRQ SVFPDSGAFS GSSEGGVGAA PDGLLTLEEE DLEDKKIHGG GASRNMRNHD
YASLDEVAGG EGGPATSSSS GVQNRRGQNS GDVRRPLLNS EDVDDDDEDE DFEEIPHENR
NSTQKLSLER NSKFSEKNFK KKFLSENPYA HIPSPDPNIQ NSTNSRRAQE NLYT
//
