EGG1_CAEBR
ID EGG1_CAEBR Reviewed; 636 AA.
AC A8X765;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=LDL receptor repeat-containing protein egg-1 {ECO:0000303|PubMed:16360684};
GN Name=egg-1 {ECO:0000312|WormBase:CBG08534};
GN ORFNames=CBG08534 {ECO:0000312|WormBase:CBG08534};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000312|Proteomes:UP000008549};
RN [1] {ECO:0000312|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|Proteomes:UP000008549};
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).
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 and egg-5 (By
CC similarity). {ECO:0000250|UniProtKB:Q09967,
CC 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; HE601197; CAP28476.2; -; Genomic_DNA.
DR AlphaFoldDB; A8X765; -.
DR STRING; 6238.CBG08534; -.
DR WormBase; CBG08534; CBP08034; WBGene00030306; Cbr-egg-1.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_021811_0_0_1; -.
DR InParanoid; A8X765; -.
DR OMA; CTPVKEC; -.
DR OrthoDB; 556051at2759; -.
DR Proteomes; UP000008549; Chromosome V.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0007338; P:single fertilization; IMP:UniProtKB.
DR CDD; cd00112; LDLa; 6.
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; 6.
DR PROSITE; PS50068; LDLRA_2; 7.
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..636
FT /note="LDL receptor repeat-containing protein egg-1"
FT /id="PRO_0000442793"
FT TOPO_DOM 1..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q09967"
FT TRANSMEM 131..151
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..636
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q09967"
FT DOMAIN 205..243
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 244..296
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 298..335
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 336..375
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 378..415
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 457..499
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 503..541
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 542..579
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 213..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 227..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 245..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 251..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 280..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 299..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 306..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 319..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 337..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 359..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 379..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 387..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 399..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 458..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 466..489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 483..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 504..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 514..531
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 525..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 543..556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 550..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 563..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 636 AA; 69365 MW; 28AD6B18A0FBC660 CRC64;
MSSIAQKNRN YFLYIFYGRI FNSSDKTFFI IKKQLVIAPN FFSVDQKLIC SSELFCGTAC
SRSLVVLYEN YKKIVILNSP QFFAGLDSGR ENQSPDGSVQ GNGLKWMLFL CQKSKRTIFS
NHSNLFQCPS VAIVLVLALV ILGVLAAIPL TLMLTSSAQK MSTDSTDLTD YSIRHPKFWP
KTDKIHFDDL GGIPMSSMFP PNVSTCSGFG FACTGAVHMV IPSSKRCDGF KDCQDGSDEE
NCKECQSVFS CRSHIEEDSK KKRKTKVQPT LICLTAERLC NGVQDCLDGS DEAMCKSTCS
KDQFKCNGSN ACLPLSAKCD GVKDCSDGSD ENNCNKCQKG AHVSLVSRNI KHLFASHVCD
GVAQCADRSD EQQCDCKTCS GSDKALCDDG TCIKRSQVCD GKKDCSDGMD EENCPGTCSI
EAFATKVKRV TCSDGKDYTE SEACSGVEES CGGSCSKCHP KLTFTCPAAG NAQKKCIKRS
KVCDGIFDCD DGADEKNCTP VKECGIDNAS QFTCDRKCVD ASRRCDGVWD CEDKSDEQNC
SQCASGSIKC SADKKCLPAY TRCNGVAECS DGSDELKCSC EECLGAHSNT YMCSESNRCL
KRDEVCSPYS MCPNATYTDK AYCAALVLKN SGRFPY
