CED1_CAEEL
ID CED1_CAEEL Reviewed; 1111 AA.
AC Q9XWD6; Q0E7J9; Q8T3A6; Q8T3A7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cell death abnormality protein 1 {ECO:0000303|PubMed:11163239};
DE Flags: Precursor;
GN Name=ced-1 {ECO:0000303|PubMed:11163239, ECO:0000312|WormBase:Y47H9C.4a};
GN ORFNames=Y47H9C.4 {ECO:0000312|WormBase:Y47H9C.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG60061.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, IDENTIFICATION OF NPXY AND YXXL MOTIFS, PHOSPHORYLATION
RP AT TYR-1019, AND MUTAGENESIS OF PRO-124; CYS-136; CYS-330; CYS-448;
RP CYS-501; CYS-803; ASN-962; TYR-965 AND TYR-1019.
RC TISSUE=Embryo {ECO:0000269|PubMed:11163239};
RX PubMed=11163239; DOI=10.1016/s0092-8674(01)00190-8;
RA Zhou Z., Hartwieg E., Horvitz H.R.;
RT "CED-1 is a transmembrane receptor that mediates cell corpse engulfment in
RT C. elegans.";
RL Cell 104:43-56(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA21739.1}
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] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=6857247; DOI=10.1126/science.6857247;
RA Hedgecock E.M., Sulston J.E., Thomson J.N.;
RT "Mutations affecting programmed cell deaths in the nematode Caenorhabditis
RT elegans.";
RL Science 220:1277-1279(1983).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1936965; DOI=10.1093/genetics/129.1.79;
RA Ellis R.E., Jacobson D.M., Horvitz H.R.;
RT "Genes required for the engulfment of cell corpses during programmed cell
RT death in Caenorhabditis elegans.";
RL Genetics 129:79-94(1991).
RN [5] {ECO:0000305}
RP INTERACTION WITH CED-6.
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 [6]
RP FUNCTION, AND MUTAGENESIS OF 375-GLN--THR-1111.
RX PubMed=12944970; DOI=10.1038/nature01920;
RA Bloss T.A., Witze E.S., Rothman J.H.;
RT "Suppression of CED-3-independent apoptosis by mitochondrial betaNAC in
RT Caenorhabditis elegans.";
RL Nature 424:1066-1071(2003).
RN [7] {ECO:0000305}
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-333, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [8] {ECO:0000305}
RP FUNCTION.
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 [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16740477; DOI=10.1016/j.devcel.2006.04.007;
RA Yu X., Odera S., Chuang C.H., Lu N., Zhou Z.;
RT "C. elegans Dynamin mediates the signaling of phagocytic receptor CED-1 for
RT the engulfment and degradation of apoptotic cells.";
RL Dev. Cell 10:743-757(2006).
RN [10] {ECO:0000305}
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-66 AND ASN-333, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [11] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18606143; DOI=10.1016/j.devcel.2008.05.006;
RA Haskins K.A., Russell J.F., Gaddis N., Dressman H.K., Aballay A.;
RT "Unfolded protein response genes regulated by CED-1 are required for
RT Caenorhabditis elegans innate immunity.";
RL Dev. Cell 15:87-97(2008).
RN [12] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18351800; DOI=10.1371/journal.pbio.0060061;
RA Yu X., Lu N., Zhou Z.;
RT "Phagocytic receptor CED-1 initiates a signaling pathway for degrading
RT engulfed apoptotic cells.";
RL PLoS Biol. 6:E61-E61(2008).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26598553; DOI=10.1242/jcs.174201;
RA Min H., Shim Y.H., Kawasaki I.;
RT "Loss of PGL-1 and PGL-3, members of a family of constitutive germ-granule
RT components, promotes germline apoptosis in C. elegans.";
RL J. Cell Sci. 129:341-353(2016).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27650246; DOI=10.1038/srep33884;
RA Al-Amin M., Min H., Shim Y.H., Kawasaki I.;
RT "Somatically expressed germ-granule components, PGL-1 and PGL-3, repress
RT programmed cell death in C. elegans.";
RL Sci. Rep. 6:33884-33884(2016).
CC -!- FUNCTION: Involved in programmed cell death, also called apoptosis, in
CC both somatic and germ cells (PubMed:11163239, PubMed:6857247,
CC PubMed:1936965, PubMed:15744306, PubMed:16740477, PubMed:18351800,
CC PubMed:26598553, PubMed:27650246, PubMed:12944970). Acts by recruiting
CC ced-6 to phagosomes which enables actin-dependent cytoskeletal
CC reorganization and subsequent engulfment of the apoptotic cell corpse
CC (PubMed:15744306). Has a role in the association of ppk-3 and rab-7
CC with the phagosomal surface which is necessary for the incorporation of
CC lysosomes to phagosomes during phagosome maturation (PubMed:16740477,
CC PubMed:18351800). Activates the expression of unfolded protein response
CC genes, which are involved in the immune response to live bacteria
CC (PubMed:18606143). {ECO:0000269|PubMed:11163239,
CC ECO:0000269|PubMed:12944970, ECO:0000269|PubMed:15744306,
CC ECO:0000269|PubMed:16740477, ECO:0000269|PubMed:18351800,
CC ECO:0000269|PubMed:18606143, ECO:0000269|PubMed:1936965,
CC ECO:0000269|PubMed:26598553, ECO:0000269|PubMed:27650246,
CC ECO:0000269|PubMed:6857247}.
CC -!- SUBUNIT: Interacts (via C-terminus) with ced-6 (via PTB domain).
CC {ECO:0000269|PubMed:11729193}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11163239};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:11163239}.
CC Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:11163239};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:11163239}.
CC Note=Colocalizes with ced-6 and actin halos around early apoptotic
CC cells. Temporally colocalizes with dyn-1 during engulfment of cell
CC corpses. {ECO:0000255, ECO:0000269|PubMed:11163239}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a {ECO:0000312|WormBase:Y47H9C.4a};
CC IsoId=Q9XWD6-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y47H9C.4b};
CC IsoId=Q9XWD6-2; Sequence=VSP_053136;
CC Name=c {ECO:0000312|WormBase:Y47H9C.4c};
CC IsoId=Q9XWD6-3; Sequence=VSP_053135, VSP_053137;
CC Name=d {ECO:0000312|WormBase:Y47H9C.4d};
CC IsoId=Q9XWD6-4; Sequence=VSP_053133, VSP_053134;
CC -!- TISSUE SPECIFICITY: Expressed in engulfing cells and syncytium
CC hypodermal cells. Ced-7 is necessary for clustering around cell corpses
CC prior to engulfment. {ECO:0000269|PubMed:11163239}.
CC -!- DOMAIN: NPXY motif thought to be involved in signal transduction that
CC activates the cell corpse internalization process.
CC {ECO:0000269|PubMed:11163239}.
CC -!- PTM: Phosphorylation of Tyr-1019, within the YXXL motif, is thought to
CC initiate phagosomal formation. {ECO:0000269|PubMed:11163239}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of cell corpses (PubMed:26598553).
CC Appears immunocompromised resulting in susceptibility to bacterial
CC infection (PubMed:6857247, PubMed:1936965, PubMed:18606143). Reduced or
CC lack of association of ppk-3 and rab-7 with the phagosomal surface
CC (PubMed:18351800). Defective in the recruitment of lysosomes to
CC phagosomes (PubMed:16740477). Double knockout with the P-granule
CC component pgl-1 results in an increased number of cell corpses in the
CC gonad as compared to the ced-1 single mutant (PubMed:26598553).
CC Conversely, double knockout with pgl-1 or pgl-3 results in reduced
CC somatic cell apoptosis (PubMed:27650246). Double knockout with the
CC synthetic multivulva class B protein hpl-2 results in reduced somatic
CC cell apoptosis at 25 degrees Celsius (PubMed:27650246). Triple knockout
CC with hpl-2 and pgl-1 partially recovers the reduced somatic cell
CC apoptotic cell defect in the ced-1 and hpl-2 double knockout
CC (PubMed:27650246). Triple knockout with hpl-2 and pgl-1 and knockdown
CC with either ced-3 or ced-4 reduces the somatic cell apoptosis defect in
CC the ced-1, hpl-2 and pgl-1 triple knockout (PubMed:27650246). Double
CC knockout with hpl-2 and knockdown with either pgl-1, pgl-3, glh-1 or
CC glh-4 RNAi rescues the reduced somatic cell apoptotic cell defect in
CC the ced-1 and hpl-2 double knockout (PubMed:27650246). Knockout with
CC RNAi-mediated knockdown of synthetic multivulva class B proteins lin-9,
CC lin-35, lin-37 or lin-54 results in reduced somatic cell apoptosis
CC (PubMed:27650246). {ECO:0000269|PubMed:16740477,
CC ECO:0000269|PubMed:18351800, ECO:0000269|PubMed:18606143,
CC ECO:0000269|PubMed:1936965, ECO:0000269|PubMed:26598553,
CC ECO:0000269|PubMed:27650246, ECO:0000269|PubMed:6857247}.
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DR EMBL; AF332568; AAG60061.1; -; mRNA.
DR EMBL; BX284601; CAA21739.1; -; Genomic_DNA.
DR EMBL; BX284601; CAD27614.1; -; Genomic_DNA.
DR EMBL; BX284601; CAD27615.1; -; Genomic_DNA.
DR EMBL; BX284601; CAL44979.1; -; Genomic_DNA.
DR PIR; T26972; T26972.
DR RefSeq; NP_001021772.1; NM_001026601.3. [Q9XWD6-2]
DR RefSeq; NP_001021773.1; NM_001026602.3.
DR RefSeq; NP_001076621.1; NM_001083152.2. [Q9XWD6-4]
DR RefSeq; NP_740922.1; NM_170927.4. [Q9XWD6-1]
DR AlphaFoldDB; Q9XWD6; -.
DR SMR; Q9XWD6; -.
DR BioGRID; 38467; 6.
DR ELM; Q9XWD6; -.
DR IntAct; Q9XWD6; 1.
DR MINT; Q9XWD6; -.
DR STRING; 6239.Y47H9C.4a; -.
DR iPTMnet; Q9XWD6; -.
DR EPD; Q9XWD6; -.
DR PaxDb; Q9XWD6; -.
DR PeptideAtlas; Q9XWD6; -.
DR EnsemblMetazoa; Y47H9C.4a.1; Y47H9C.4a.1; WBGene00000415. [Q9XWD6-1]
DR EnsemblMetazoa; Y47H9C.4b.1; Y47H9C.4b.1; WBGene00000415. [Q9XWD6-2]
DR EnsemblMetazoa; Y47H9C.4c.1; Y47H9C.4c.1; WBGene00000415. [Q9XWD6-3]
DR EnsemblMetazoa; Y47H9C.4d.1; Y47H9C.4d.1; WBGene00000415. [Q9XWD6-4]
DR GeneID; 173064; -.
DR KEGG; cel:CELE_Y47H9C.4; -.
DR UCSC; Y47H9C.4a; c. elegans.
DR CTD; 173064; -.
DR WormBase; Y47H9C.4a; CE20264; WBGene00000415; ced-1. [Q9XWD6-1]
DR WormBase; Y47H9C.4b; CE30361; WBGene00000415; ced-1. [Q9XWD6-2]
DR WormBase; Y47H9C.4c; CE30362; WBGene00000415; ced-1. [Q9XWD6-3]
DR WormBase; Y47H9C.4d; CE40433; WBGene00000415; ced-1. [Q9XWD6-4]
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00940000167451; -.
DR InParanoid; Q9XWD6; -.
DR OMA; CSKPCPQ; -.
DR OrthoDB; 561378at2759; -.
DR PhylomeDB; Q9XWD6; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-CEL-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR Reactome; R-CEL-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q9XWD6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000415; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001891; C:phagocytic cup; IDA:WormBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0031260; C:pseudopodium membrane; IDA:WormBase.
DR GO; GO:0005044; F:scavenger receptor activity; IPI:WormBase.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
DR GO; GO:1902742; P:apoptotic process involved in development; IMP:UniProtKB.
DR GO; GO:0034620; P:cellular response to unfolded protein; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IDA:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; IDA:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
DR GO; GO:0001845; P:phagolysosome assembly; IMP: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; IMP:UniProtKB.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; IMP:UniProtKB.
DR GO; GO:0043654; P:recognition of apoptotic cell; IDA:WormBase.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 5.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 16.
DR SMART; SM00261; FU; 5.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cell membrane; Cytoplasmic vesicle;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1111
FT /note="Cell death abnormality protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000379932"
FT TOPO_DOM 19..910
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 932..1111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..113
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 118..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 241..276
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 421..458
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 629..680
FT /note="FU"
FT /evidence="ECO:0000255"
FT DOMAIN 681..716
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 940..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 962..965
FT /note="NPXY"
FT /evidence="ECO:0000255"
FT MOTIF 1019..1022
FT /note="YXXL"
FT /evidence="ECO:0000255"
FT COMPBIAS 959..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1019
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11163239"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
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 245..257
FT /evidence="ECO:0000255"
FT DISULFID 251..264
FT /evidence="ECO:0000255"
FT DISULFID 266..275
FT /evidence="ECO:0000255"
FT DISULFID 425..439
FT /evidence="ECO:0000255"
FT DISULFID 431..446
FT /evidence="ECO:0000255"
FT DISULFID 448..457
FT /evidence="ECO:0000255"
FT DISULFID 685..697
FT /evidence="ECO:0000255"
FT DISULFID 691..704
FT /evidence="ECO:0000255"
FT DISULFID 706..715
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..49
FT /note="MRLILLVLLATWQVVVDTRAPTFPDKLTQQLQQQGTTEPQGDHVCTVKT ->
FT MCVPRDIGSRVKTHTPTSHHRTPSPRTLRTKNVLRTICTPKFEFSYIFF (in
FT isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_053133"
FT VAR_SEQ 50..1111
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_053134"
FT VAR_SEQ 1017..1082
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_053135"
FT VAR_SEQ 1042..1082
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053136"
FT VAR_SEQ 1083
FT /note="E -> K (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_053137"
FT MUTAGEN 124
FT /note="P->L: In n1995; increase in corpses in L1 head."
FT /evidence="ECO:0000269|PubMed:11163239"
FT MUTAGEN 136
FT /note="C->Y: In n2091; increase in corpses in L1 head."
FT /evidence="ECO:0000269|PubMed:11163239"
FT MUTAGEN 330
FT /note="C->Y: In n2089; increase in corpses in L1 head."
FT /evidence="ECO:0000269|PubMed:11163239"
FT MUTAGEN 375..1111
FT /note="Missing: In e1735; defective clearance of apoptotic
FT cell corpses in embryos."
FT /evidence="ECO:0000269|PubMed:12944970"
FT MUTAGEN 448
FT /note="C->Y: In e1797, n2000, and n2092; increase in
FT corpses in L1 head."
FT /evidence="ECO:0000269|PubMed:11163239"
FT MUTAGEN 501
FT /note="C->Y: In n1951; increase in corpses in L1 head."
FT /evidence="ECO:0000269|PubMed:11163239"
FT MUTAGEN 803
FT /note="C->Y: In e1801; increase in corpses in L1 head."
FT /evidence="ECO:0000269|PubMed:11163239"
FT MUTAGEN 962
FT /note="N->A: 85% loss of activity."
FT /evidence="ECO:0000269|PubMed:11163239"
FT MUTAGEN 965
FT /note="Y->A: 71% loss of activity."
FT /evidence="ECO:0000269|PubMed:11163239"
FT MUTAGEN 1019
FT /note="Y->A: 54% loss of activity."
FT /evidence="ECO:0000269|PubMed:11163239"
SQ SEQUENCE 1111 AA; 118804 MW; A39F374C008F9874 CRC64;
MRLILLVLLA TWQVVVDTRA PTFPDKLTQQ LQQQGTTEPQ GDHVCTVKTI VDDYELKKVI
HTVVYNDTEQ CLNPLTGFQC TVEKRGQKAS YQRQLVKKEK YVKQCCDGYY QTKDHFCLPD
CNPPCKKGKC IEPGKCECDP GYGGKYCASS CSVGTWGLGC SKSCDCENGA NCDPELGTCI
CTSGFQGERC EKPCPDNKWG PNCVKSCPCQ NGGKCNKEGK CVCSDGWGGE FCLNKCEEGK
FGAECKFECN CQNGATCDNT NGKCICKSGY HGALCENECS VGFFGSGCTQ KCDCLNNQNC
DSSSGECKCI GWTGKHCDIG CSRGRFGLQC KQNCTCPGLE FSDSNASCDA KTGQCQCESG
YKGPKCDERK CDAEQYGADC SKTCTCVREN TLMCAPNTGF CRCKPGFYGD NCELACSKDS
YGPNCEKQAM CDWNHASECN PETGSCVCKP GRTGKNCSEP CPLDFYGPNC AHQCQCNQRG
VGCDGADGKC QCDRGWTGHR CEHHCPADTF GANCEKRCKC PKGIGCDPIT GECTCPAGLQ
GANCDIGCPE GSYGPGCKLH CKCVNGKCDK ETGECTCQPG FFGSDCSTTC SKGKYGESCE
LSCPCSDASC SKQTGKCLCP LGTKGVSCDQ KCDPNTFGFL CQETVTPSPC ASTDPKNGVC
LSCPPGSSGI HCEHNCPAGS YGDGCQQVCS CADGHGCDPT TGECICEPGY HGKTCSEKCP
DGKYGYGCAL DCPKCASGST CDHINGLCIC PAGLEGALCT RPCSAGFWGN GCRQVCRCTS
EYKQCNAQTG ECSCPAGFQG DRCDKPCEDG YYGPDCIKKC KCQGTATSSC NRVSGACHCH
PGFTGEFCHA LCPESTFGLK CSKECPKDGC GDGYECDAAI GCCHVDQMSC GKAKQEFEAL
NGAGRSTGLT WFFVLLIVAL CGGLGLIALF YRNKYQKEKD PDMPTVSFHK APNNDEGREF
QNPLYSRQSV FPDSDAFSSE NNGNHQGGPP NGLLTLEEEE LENKKIHGRS AAGRGNNDYA
SLDEVAGEGS SSSASASASR RGLNSSEQSR RPLLEEHDEE EFDEPHENSI SPAHAVTTSN
HNENPYADIS SPDPVTQNSA NKKRAQDNLY T
