EGG1_CAERE
ID EGG1_CAERE Reviewed; 551 AA.
AC E3LYX0;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=LDL receptor repeat-containing protein egg-1 {ECO:0000303|PubMed:16360684};
GN Name=egg-1 {ECO:0000303|PubMed:16360684};
GN ORFNames=CRE_04724 {ECO:0000312|EMBL:EFO86538.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641;
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, AND 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).
CC -!- FUNCTION: Probable receptor which is required for the oocyte-to-zygote
CC transition although its exact function is controversial (By
CC similarity). Seems to be required for fertilization probably by
CC promoting the interaction or fusion between sperm and oocyte
CC (PubMed:16360684). Conversely, shown to be dispensable for
CC fertilization but required for the formation of a continuous and
CC cohesive eggshell chitin layer by maintaining a homogenous distribution
CC of chitin synthase chs-1 at the unfertilized oocyte cell membrane (By
CC similarity). Appears to recruit or maintain together to the
CC unfertilized oocyte cortex several proteins including chs-1, kinase
CC mbk-2 and pseudophosphatases egg-3, and possibly egg-4 (By similarity).
CC {ECO:0000250|UniProtKB:Q09967, ECO:0000269|PubMed:16360684}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q09967};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q09967}.
CC Note=Localizes to the cell membrane of developing oocytes. Plasma
CC membrane localization requires extracellular matrix protein cbd-1.
CC After fertilization, localizes to endosomes in zygotes.
CC {ECO:0000250|UniProtKB:Q09967}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in sterility due
CC to the loss of oocyte fertilization. {ECO:0000269|PubMed:16360684}.
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DR EMBL; DS268419; EFO86538.1; -; Genomic_DNA.
DR RefSeq; XP_003110706.1; XM_003110658.1.
DR AlphaFoldDB; E3LYX0; -.
DR SMR; E3LYX0; -.
DR STRING; 31234.CRE04724; -.
DR EnsemblMetazoa; CRE04724.1; CRE04724.1; WBGene00055605.
DR GeneID; 9800717; -.
DR CTD; 9800717; -.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_021811_0_0_1; -.
DR InParanoid; E3LYX0; -.
DR OMA; SNTYMCN; -.
DR OrthoDB; 556051at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007338; P:single fertilization; IMP:UniProtKB.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 4.10.400.10; -; 7.
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 3: Inferred from homology;
KW Cell membrane; Developmental protein; Disulfide bond; Fertilization;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Repeat;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..551
FT /note="LDL receptor repeat-containing protein egg-1"
FT /id="PRO_0000442794"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 50..70
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..551
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 124..162
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 163..215
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 217..254
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 255..290
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 293..330
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 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 423
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 132..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 146..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 164..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 170..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 199..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 218..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 225..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 238..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 256..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 263..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 274..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 294..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 302..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 314..329
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; 59866 MW; 574C6A7943B388C8 CRC64;
MSQQPGSDRR VNFAQEEPMT LGEKISHRMD QFKEMVSSGC CSCASRCPSV AIVLILALVI
LGILAAIPLT LMLTSSAQRM STDSTDLSPY SIRHPKFWPK TDKIHFNDLD GIPMSSLFPP
NVSTCSGFGF ACTGAVHMII PSSKRCDGIK DCQDGSDEEN CKECQSVFSC RSHVEEDSKT
KRKTKVLPTL ICLTAEKLCN DVQDCPDGSD ESVCKSTCSK DQFKCTGNNA CLPTSAKCDG
VNDCTDGSDE KNCNECQKGA HKCGKQCIKA SHVCDGVAQC ADRSDEKECD CKSCSGSDKA
LCEDGTCIKR TQVCDGKKDC TDGMDEENCP GSCSIEAFST KTKQLTCSDE KRYTESEACS
GVVEACEQSC PKCHPKLTFT CPAVGGSQKR CIRRSKVCDG INDCDDGADE KNCTPIKECG
IENASQFTCD RKCLDASRRC DGVWDCEDKS DEQNCQQCSS GSIRCAADKK CLPAYTRCNG
VAECSDGSDE QKCSCEECLG AHSNTYMCNE SNRCLKRDEV CSPYSMCPNA TYTDKAYCAA
LVLKNSGRFP Y
