EGG2_CAEEL
ID EGG2_CAEEL Reviewed; 548 AA.
AC Q21629;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=LDL receptor repeat-containing protein egg-2 {ECO:0000303|PubMed:16360684};
DE AltName: Full=Egg sterile protein 2 {ECO:0000312|WormBase:R01H2.3};
GN Name=egg-2 {ECO:0000312|WormBase:R01H2.3};
GN ORFNames=R01H2.3 {ECO:0000312|WormBase:R01H2.3};
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, 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).
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-1, 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-1 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 pseudophosphatase egg-3, and possibly
CC egg-4 and egg-5 (PubMed:20971008). {ECO:0000269|PubMed:16360684,
CC ECO:0000269|PubMed:20971008}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20971008};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q09967}.
CC Endosome membrane {ECO:0000250|UniProtKB:Q09967}; Single-pass type II
CC membrane protein {ECO:0000250|UniProtKB:Q09967}. Note=Localizes to the
CC cell membrane of developing oocytes (PubMed:20971008). Plasma membrane
CC localization requires extracellular matrix protein cbd-1
CC (PubMed:20971008). After fertilization, localizes to endosomes in
CC zygotes (By similarity). {ECO:0000250|UniProtKB:Q09967,
CC ECO:0000269|PubMed:20971008}.
CC -!- DISRUPTION PHENOTYPE: Severe sterility at the restrictive temperature
CC of 25 degrees Celsius (PubMed:16360684). Accumulation of unfertilized
CC oocytes in the uterus, although this is controversial
CC (PubMed:16360684). Simultaneous RNAi-mediated knockdown with egg-1
CC results in a fragmented eggshell chitin layer which often accumulates
CC at one end of the embryo (PubMed:20971008). In unfertilized oocytes,
CC disrupts the homogenous distribution of cortical chitin synthase chs-1,
CC pseudophosphatase egg-3 and kinase mbk-2 (PubMed:20971008). In a egg-1
CC (tm1071) mutant background, causes polyspermy (PubMed:20971008).
CC {ECO:0000269|PubMed:16360684, ECO:0000269|PubMed:20971008}.
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DR EMBL; BX284603; CCD69284.1; -; Genomic_DNA.
DR PIR; T16642; T16642.
DR RefSeq; NP_498537.1; NM_066136.5.
DR AlphaFoldDB; Q21629; -.
DR STRING; 6239.R01H2.3; -.
DR EPD; Q21629; -.
DR PaxDb; Q21629; -.
DR PeptideAtlas; Q21629; -.
DR EnsemblMetazoa; R01H2.3.1; R01H2.3.1; WBGene00019811.
DR GeneID; 187510; -.
DR KEGG; cel:CELE_R01H2.3; -.
DR UCSC; R01H2.3; c. elegans.
DR CTD; 187510; -.
DR WormBase; R01H2.3; CE00802; WBGene00019811; egg-2.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000162544; -.
DR HOGENOM; CLU_021811_0_0_1; -.
DR InParanoid; Q21629; -.
DR OMA; CTPVKEC; -.
DR OrthoDB; 1276798at2759; -.
DR PhylomeDB; Q21629; -.
DR PRO; PR:Q21629; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00019811; Expressed in germ line (C elegans) and 3 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; 6.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00192; LDLa; 8.
DR SUPFAM; SSF57424; SSF57424; 8.
DR PROSITE; PS01209; LDLRA_1; 7.
DR PROSITE; PS50068; LDLRA_2; 8.
PE 3: Inferred from homology;
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..548
FT /note="LDL receptor repeat-containing protein egg-2"
FT /id="PRO_0000442795"
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..548
FT /note="Extracellular"
FT /evidence="ECO:0000305"
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 370..412
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 416..454
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 455..492
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 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 527
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 371..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 379..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 396..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 417..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 427..444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 438..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 456..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 463..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 476..491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 548 AA; 59288 MW; B3130BD3FD27C885 CRC64;
MSQQAGNAQR GRFDEEPMSL GEKISHRMDQ LKEIVSSSCP CAGKFPPVAI VLIVALIILG
VIIAVPLVIF LSPSAQAMSS GTRDLSSHSI RHPKVWPKTE KVQDDDLSAI QMTSLLPPNV
STCSGFGFAC TGSIDMIIPS SKRCDGLKDC SDGSDEENCK ECQSIYSCRA HIEEESEKKD
KTSVLPTLIC LTAEKLCNGV ENCPDGSDEA SCRSKCSKDQ FKCSGSDACL PISVKCDGVS
DCENESDESN CNKCQKGAHK CGKNCIKASK VCDGIPDCDD GSDEHQCDCK TCSGSEKALC
EDGTCIMRSQ VCDGKHDCLD GIDEENCPGS CSNERFSSKL KLLTCDDGNQ YSEVEACSGL
VEACELNCPK CDPKHTFTCP AVGGIHNKCI KRSKVCDGIF DCEDGADEKK CTPVKECVVE
SSIQFTCDNK CLESSRRCDG VWDCEDKSDE KGCDKCPSRS FKCSADKKCL PFHTRCNGVA
ECSDGSDEHK CSCQECLGTH HDTYMCSESN RCLKRGEVCS PYSMCPNATY IDKAYCASLA
LKNSGLRP
