EGG1_CAEEL
ID EGG1_CAEEL Reviewed; 551 AA.
AC Q09967;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=LDL receptor repeat-containing protein egg-1 {ECO:0000303|PubMed:16360684};
DE AltName: Full=Egg sterile protein 1 {ECO:0000312|WormBase:B0244.8};
GN Name=egg-1 {ECO:0000312|WormBase:B0244.8};
GN ORFNames=B0244.8 {ECO:0000312|WormBase:B0244.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, TOPOLOGY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16360684; DOI=10.1016/j.cub.2005.10.043;
RA Kadandale P., Stewart-Michaelis A., Gordon S., Rubin J., Klancer R.,
RA Schweinsberg P., Grant B.D., Singson A.;
RT "The egg surface LDL receptor repeat-containing proteins EGG-1 and EGG-2
RT are required for fertilization in Caenorhabditis elegans.";
RL Curr. Biol. 15:2222-2229(2005).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20971008; DOI=10.1016/j.cub.2010.09.059;
RA Johnston W.L., Krizus A., Dennis J.W.;
RT "Eggshell chitin and chitin-interacting proteins prevent polyspermy in C.
RT elegans.";
RL Curr. Biol. 20:1932-1937(2010).
CC -!- FUNCTION: Probable receptor which is required for the oocyte-to-zygote
CC transition although its exact function is controversial
CC (PubMed:16360684, PubMed:20971008). Redundantly with egg-2, seems to be
CC required for fertilization probably by promoting the interaction or
CC fusion between sperm and oocyte (PubMed:16360684). Conversely, shown to
CC be dispensable for fertilization but required together with egg-2 for
CC the formation of a continuous and cohesive eggshell chitin layer by
CC maintaining a homogenous distribution of chitin synthase chs-1 at the
CC unfertilized oocyte cell membrane (PubMed:20971008). Appears to recruit
CC or maintain together to the unfertilized oocyte cortex several proteins
CC including chs-1, kinase mbk-2 and pseudophosphatases egg-3, and
CC possibly egg-4 and egg-5 (PubMed:20971008).
CC {ECO:0000269|PubMed:16360684, ECO:0000269|PubMed:20971008}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16360684,
CC ECO:0000269|PubMed:20971008}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:16360684}. Endosome membrane
CC {ECO:0000269|PubMed:20971008}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:16360684}. Note=Localizes to the cell membrane of
CC developing oocytes (PubMed:16360684, PubMed:20971008). Plasma membrane
CC localization requires extracellular matrix protein cbd-1
CC (PubMed:20971008). After fertilization, localizes to endosomes in
CC zygotes (PubMed:20971008). {ECO:0000269|PubMed:16360684,
CC ECO:0000269|PubMed:20971008}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in developing oocytes of
CC adult germ line. {ECO:0000269|PubMed:16360684}.
CC -!- DISRUPTION PHENOTYPE: Temperature sensitive phenotype with severe
CC sterility at the restrictive temperature of 25 degrees Celsius
CC (PubMed:16360684, PubMed:20971008). Zygotes exit the spermatheca with a
CC pinched morphology and leave a trailing section behind and are
CC polyspermic (PubMed:20971008). The eggshell chitin layer is fragmented
CC and often accumulates at one end of the embryo (PubMed:20971008).
CC Ovulation is severely reduced resulting in oocyte accumulation in the
CC gonad and a disappearance of sperm in the spermatheca
CC (PubMed:16360684). Conversely, although sperm and oocyte appear to make
CC contact in the spermatheca no visible fertilization occurs and
CC endomitotic oocytes accumulate with age (PubMed:16360684). Male
CC fertility is not affected (PubMed:16360684). Simultaneous RNAi-mediated
CC knockdown with egg-2 results in complete sterility (PubMed:16360684).
CC In unfertilized oocytes, disrupts the homogenous distribution of
CC cortical chitin synthase chs-1, pseudophosphatase egg-3 and kinase mbk-
CC 2 (PubMed:20971008). {ECO:0000269|PubMed:16360684,
CC ECO:0000269|PubMed:20971008}.
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DR EMBL; BX284603; CCD61503.1; -; Genomic_DNA.
DR PIR; B88465; B88465.
DR RefSeq; NP_498237.2; NM_065836.7.
DR AlphaFoldDB; Q09967; -.
DR DIP; DIP-24694N; -.
DR STRING; 6239.B0244.8; -.
DR EPD; Q09967; -.
DR PaxDb; Q09967; -.
DR PeptideAtlas; Q09967; -.
DR EnsemblMetazoa; B0244.8.1; B0244.8.1; WBGene00015083.
DR GeneID; 175804; -.
DR KEGG; cel:CELE_B0244.8; -.
DR UCSC; B0244.8; c. elegans.
DR CTD; 175804; -.
DR WormBase; B0244.8; CE32094; WBGene00015083; egg-1.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000162544; -.
DR HOGENOM; CLU_021811_0_0_1; -.
DR InParanoid; Q09967; -.
DR OMA; SNTYMCN; -.
DR OrthoDB; 556051at2759; -.
DR PhylomeDB; Q09967; -.
DR PRO; PR:Q09967; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015083; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISS:WormBase.
DR GO; GO:0030703; P:eggshell formation; IGI:UniProtKB.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; IGI:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IGI:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IMP:WormBase.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 4.10.400.10; -; 8.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00192; LDLa; 8.
DR SUPFAM; SSF57424; SSF57424; 7.
DR PROSITE; PS01209; LDLRA_1; 7.
DR PROSITE; PS50068; LDLRA_2; 8.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond; Endosome;
KW Fertilization; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Repeat; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..551
FT /note="LDL receptor repeat-containing protein egg-1"
FT /id="PRO_0000442792"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16360684"
FT TRANSMEM 49..69
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..551
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16360684"
FT DOMAIN 122..160
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 161..213
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 215..252
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 253..288
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 291..328
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 372..414
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 418..456
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 457..494
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 130..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 144..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 162..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 168..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 197..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 216..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 223..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 236..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 254..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 261..278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 272..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 292..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 300..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 312..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 373..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 381..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 398..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 419..433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 429..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 440..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 458..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 465..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 478..493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 551 AA; 59694 MW; E199259A2371FA37 CRC64;
MSQQPGSARR VNFPEEPMTL GEKFSHRMDQ LKEIIADGGC SRAAKCVSIT VCLVLLVLIF
GGAIVYLVMS LTSSAQKMSA DSMDISPQAI RHPKFWPPTD KIRFDDLNGI PMTSLFPQNV
STCSGFGFAC TGAVHMVIPS SKRCDGRRDC EDGSDEENCK ECQSVFSCKL RPEEESKKKG
RSTVQPTLIC LTAQHLCDNV ENCPDGSDEA VCKSSCSKDQ FKCPGSNACL PLSAKCDGIN
DCADASDEKN CSKCQNNAHK CGKQCIKASH VCDGVAQCAD GSDEQQCDCQ RCSGTDKALC
DDGTCIMRTQ VCDGKKDCTD GMDEEDCPGS CTIESFSPKL KMVTCSDGKQ YTEAEACSGS
FESCDHDCPN SKCHPKLAFT CPASKEARKM CISRRKVCDG TPDCDDGADE INCTPIKECG
IAKNTQFKCD HKCLDSSRRC DGVWDCEDKS DEKGCDKCPS GTIKCAADKK CLPAFTRCNG
VADCSDGSDE LKCSCQECLG VHSNTYMCNE SNRCLKRDEV CSPYSMCPNA TYTDKAFCAA
LFLKKSGTSP F
