LET23_CAEEL
ID LET23_CAEEL Reviewed; 1323 AA.
AC P24348;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Receptor tyrosine-protein kinase let-23;
DE EC=2.7.10.1;
DE AltName: Full=Lethal protein 23;
DE Flags: Precursor;
GN Name=let-23 {ECO:0000312|WormBase:ZK1067.1a};
GN Synonyms=kin-7 {ECO:0000312|WormBase:ZK1067.1a};
GN ORFNames=ZK1067.1 {ECO:0000312|WormBase:ZK1067.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1979659; DOI=10.1038/348693a0;
RA Aroian R.V., Koga M., Mendel J.E., Ohshima Y., Sternberg P.W.;
RT "The let-23 gene necessary for Caenorhabditis elegans vulval induction
RT encodes a tyrosine kinase of the EGF receptor subfamily.";
RL Nature 348:693-699(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=8604137; DOI=10.1006/jmbi.1996.0107;
RA Sakai T., Koga M., Ohshima Y.;
RT "Genomic structure and 5' regulatory regions of the let-23 gene in the
RT nematode C. elegans.";
RL J. Mol. Biol. 256:548-555(1996).
RN [3]
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-368.
RX PubMed=2071015; DOI=10.1093/genetics/128.2.251;
RA Aroian R.V., Sternberg P.W.;
RT "Multiple functions of let-23, a Caenorhabditis elegans receptor tyrosine
RT kinase gene required for vulval induction.";
RL Genetics 128:251-267(1991).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF CYS-368; GLY-469; CYS-700; CYS-753; THR-1065
RP AND GLY-1074.
RX PubMed=8313880; DOI=10.1002/j.1460-2075.1994.tb06269.x;
RA Aroian R.V., Les G.M., Sternberg P.W.;
RT "Mutations in the Caenorhabditis elegans let-23 EGFR-like gene define
RT elements important for cell-type specificity and function.";
RL EMBO J. 13:360-366(1994).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF THR-1065.
RX PubMed=9491893; DOI=10.1016/s0092-8674(00)80945-9;
RA Clandinin T.R., DeModena J.A., Sternberg P.W.;
RT "Inositol trisphosphate mediates a RAS-independent response to LET-23
RT receptor tyrosine kinase activation in C. elegans.";
RL Cell 92:523-533(1998).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=10359617; DOI=10.1091/mbc.10.6.2087;
RA Whitfield C.W., Benard C., Barnes T., Hekimi S., Kim S.K.;
RT "Basolateral localization of the Caenorhabditis elegans epidermal growth
RT factor receptor in epithelial cells by the PDZ protein lin-10.";
RL Mol. Biol. Cell 10:2087-2100(1999).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-368.
RX PubMed=15194811; DOI=10.1091/mbc.e04-03-0198;
RA Yin X., Gower N.J., Baylis H.A., Strange K.;
RT "Inositol 1,4,5-trisphosphate signaling regulates rhythmic contractile
RT activity of myoepithelial sheath cells in Caenorhabditis elegans.";
RL Mol. Biol. Cell 15:3938-3949(2004).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-376, AND IDENTIFICATION BY MASS
RP 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 [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17891142; DOI=10.1038/nn1981;
RA Van Buskirk C., Sternberg P.W.;
RT "Epidermal growth factor signaling induces behavioral quiescence in
RT Caenorhabditis elegans.";
RL Nat. Neurosci. 10:1300-1307(2007).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF CYS-364.
RX PubMed=20230814; DOI=10.1016/j.ydbio.2010.03.004;
RA Simms C.L., Baillie D.L.;
RT "A strawberry notch homolog, let-765/nsh-1, positively regulates lin-3/egf
RT expression to promote RAS-dependent vulval induction in C. elegans.";
RL Dev. Biol. 341:472-485(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 1318-GLN--LEU-1323.
RX PubMed=32053105; DOI=10.7554/elife.50986;
RA Haag A., Walser M., Henggeler A., Hajnal A.;
RT "The CHORD protein CHP-1 regulates EGF receptor trafficking and signaling
RT in C. elegans and in human cells.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Tyrosine-protein kinase receptor which, upon binding ligand
CC lin-3, activates 2 signaling cascades: the let-60/Ras and MAP kinase
CC signaling pathway and the let-60-independent phospholipase C-mediated
CC Ca(2+) signaling pathway. Each pathway regulates distinct functions. By
CC activating let-60/Ras, regulates larval development, induction of vulva
CC cell precursors during vulva development, male spicule formation and
CC posterior development of the epidermis (PubMed:2071015, PubMed:8313880,
CC PubMed:9491893, PubMed:20230814, PubMed:32053105). Probably by
CC activating phospholipase plc-3 and inositol 1,4,5-trisphosphate
CC receptor itr-1 signaling cascade downstream of ligand lin-3, plays a
CC role in ovulation by promoting ovulatory gonadal sheath cell
CC contractions (PubMed:9491893, PubMed:15194811). Probably by regulating
CC neuronal transmission in ALA neurons, mediates, independently of let-
CC 60/Ras, the decrease in pharyngeal pumping and locomotion during the
CC quiescent state that precedes each larval molt, downstream of lin-3 and
CC upstream of plc-3 (PubMed:17891142). {ECO:0000269|PubMed:15194811,
CC ECO:0000269|PubMed:17891142, ECO:0000269|PubMed:20230814,
CC ECO:0000269|PubMed:2071015, ECO:0000269|PubMed:32053105,
CC ECO:0000269|PubMed:8313880, ECO:0000269|PubMed:9491893}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:10359617, ECO:0000269|PubMed:32053105}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:10359617}. Basolateral cell
CC membrane {ECO:0000269|PubMed:10359617, ECO:0000269|PubMed:32053105};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:10359617}.
CC Note=Basolateral and apical membrane of cell junctions in epithelial
CC vulval precursor cells. {ECO:0000269|PubMed:10359617}.
CC -!- TISSUE SPECIFICITY: Expressed in vulval precursor cells (at protein
CC level) (PubMed:10359617). Expressed in ALA neurons, 2 ventral head
CC neurons, a single neuron in the tail, pharyngeal-intestinal valve and
CC posterior arcade epithelial cells (PubMed:17891142).
CC {ECO:0000269|PubMed:10359617, ECO:0000269|PubMed:17891142}.
CC -!- DEVELOPMENTAL STAGE: Expressed during L2 and L3 larval stages
CC (PubMed:10359617). Highly expressed in vulval precursor cells P6.p in
CC late L2 and early L3 stage larvae (PubMed:32053105).
CC {ECO:0000269|PubMed:10359617, ECO:0000269|PubMed:32053105}.
CC -!- DISRUPTION PHENOTYPE: Larval lethality, lack of vulva formation,
CC infertility and lack of male spicule formation (PubMed:2071015). RNAi-
CC mediated knockdown causes sterility, a small decrease in the peak rate
CC of sheath cell contractions and a delay in the onset of ovulatory
CC contractions (PubMed:15194811). Restores normal pharyngeal pumping rate
CC in 30 percent of animals overexpressing lin-3 (PubMed:17891142).
CC {ECO:0000269|PubMed:15194811, ECO:0000269|PubMed:17891142,
CC ECO:0000269|PubMed:2071015}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09729.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X57767; CAA40919.1; -; mRNA.
DR EMBL; D63426; BAA09729.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX284602; CAA93882.3; -; Genomic_DNA.
DR PIR; E88257; E88257.
DR PIR; S70712; S70712.
DR RefSeq; NP_495962.2; NM_063561.4.
DR PDB; 5WNO; X-ray; 2.39 A; A=866-1191.
DR PDBsum; 5WNO; -.
DR AlphaFoldDB; P24348; -.
DR SMR; P24348; -.
DR BioGRID; 39787; 108.
DR DIP; DIP-1014N; -.
DR IntAct; P24348; 2.
DR MINT; P24348; -.
DR STRING; 6239.ZK1067.1c; -.
DR iPTMnet; P24348; -.
DR PaxDb; P24348; -.
DR EnsemblMetazoa; ZK1067.1a.1; ZK1067.1a.1; WBGene00002299.
DR GeneID; 174462; -.
DR UCSC; ZK1067.1; c. elegans.
DR CTD; 174462; -.
DR WormBase; ZK1067.1a; CE03840; WBGene00002299; let-23.
DR eggNOG; KOG1025; Eukaryota.
DR GeneTree; ENSGT00940000168382; -.
DR InParanoid; P24348; -.
DR PhylomeDB; P24348; -.
DR BRENDA; 2.7.10.1; 1045.
DR Reactome; R-CEL-1227986; Signaling by ERBB2.
DR Reactome; R-CEL-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-CEL-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-CEL-1253288; Downregulation of ERBB4 signaling.
DR Reactome; R-CEL-1257604; PIP3 activates AKT signaling.
DR Reactome; R-CEL-177929; Signaling by EGFR.
DR Reactome; R-CEL-179812; GRB2 events in EGFR signaling.
DR Reactome; R-CEL-180292; GAB1 signalosome.
DR Reactome; R-CEL-180336; SHC1 events in EGFR signaling.
DR Reactome; R-CEL-182971; EGFR downregulation.
DR Reactome; R-CEL-1963642; PI3K events in ERBB2 signaling.
DR Reactome; R-CEL-212718; EGFR interacts with phospholipase C-gamma.
DR Reactome; R-CEL-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-CEL-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-CEL-445144; Signal transduction by L1.
DR Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
DR Reactome; R-CEL-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-CEL-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-CEL-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-CEL-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-CEL-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR SignaLink; P24348; -.
DR PRO; PR:P24348; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002299; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; P24348; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:WormBase.
DR GO; GO:0005911; C:cell-cell junction; IDA:WormBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:WormBase.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005006; F:epidermal growth factor receptor activity; IDA:WormBase.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:WormBase.
DR GO; GO:0030539; P:male genitalia development; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0030728; P:ovulation; IMP:WormBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0040026; P:positive regulation of vulval development; IMP:WormBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0030431; P:sleep; IMP:WormBase.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0072327; P:vulval cell fate specification; IMP:UniProtKB.
DR CDD; cd00064; FU; 5.
DR Gene3D; 3.80.20.20; -; 2.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR032778; GF_recep_IV.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 7.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Developmental protein;
KW Disulfide bond; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1323
FT /note="Receptor tyrosine-protein kinase let-23"
FT /id="PRO_0000016677"
FT TOPO_DOM 21..818
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 819..839
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 840..1323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 885..1152
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1265..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1010
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 891..899
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 919
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 220..228
FT /evidence="ECO:0000250"
FT DISULFID 224..236
FT /evidence="ECO:0000250"
FT DISULFID 244..251
FT /evidence="ECO:0000250"
FT DISULFID 248..262
FT /evidence="ECO:0000250"
FT DISULFID 263..271
FT /evidence="ECO:0000250"
FT DISULFID 267..279
FT /evidence="ECO:0000250"
FT DISULFID 282..291
FT /evidence="ECO:0000250"
FT DISULFID 295..322
FT /evidence="ECO:0000250"
FT DISULFID 326..337
FT /evidence="ECO:0000250"
FT DISULFID 341..356
FT /evidence="ECO:0000250"
FT DISULFID 359..364
FT /evidence="ECO:0000250"
FT DISULFID 520..529
FT /evidence="ECO:0000250"
FT DISULFID 524..537
FT /evidence="ECO:0000250"
FT DISULFID 540..549
FT /evidence="ECO:0000250"
FT DISULFID 553..567
FT /evidence="ECO:0000250"
FT DISULFID 570..577
FT /evidence="ECO:0000250"
FT DISULFID 574..585
FT /evidence="ECO:0000250"
FT DISULFID 588..604
FT /evidence="ECO:0000250"
FT DISULFID 608..620
FT /evidence="ECO:0000250"
FT DISULFID 623..632
FT /evidence="ECO:0000250"
FT DISULFID 627..644
FT /evidence="ECO:0000250"
FT DISULFID 647..660
FT /evidence="ECO:0000255"
FT DISULFID 670..693
FT /evidence="ECO:0000255"
FT DISULFID 696..703
FT /evidence="ECO:0000255"
FT DISULFID 700..715
FT /evidence="ECO:0000255"
FT DISULFID 717..731
FT /evidence="ECO:0000255"
FT DISULFID 735..750
FT /evidence="ECO:0000255"
FT DISULFID 753..763
FT /evidence="ECO:0000255"
FT DISULFID 757..771
FT /evidence="ECO:0000255"
FT DISULFID 774..787
FT /evidence="ECO:0000255"
FT DISULFID 791..805
FT /evidence="ECO:0000255"
FT MUTAGEN 364
FT /note="C->Y: In sa62; multivulva phenotype. RNAi-mediated
FT knockdown of let-765 suppresses the multivulva phenotype."
FT /evidence="ECO:0000269|PubMed:20230814"
FT MUTAGEN 368
FT /note="C->Y: In sy10; severe larval lethality, lack of
FT vulva induction, infertile and lack of male spicule
FT formation. Impaired ovulation characterized by a delay in
FT the initiation of ovulatory sheath cell contractions and
FT prolonged ovulatory contractions."
FT /evidence="ECO:0000269|PubMed:15194811,
FT ECO:0000269|PubMed:2071015, ECO:0000269|PubMed:8313880"
FT MUTAGEN 469
FT /note="G->R: In mn216; larval lethality."
FT /evidence="ECO:0000269|PubMed:8313880"
FT MUTAGEN 700
FT /note="C->W: In mn23; larval lethality."
FT /evidence="ECO:0000269|PubMed:8313880"
FT MUTAGEN 753
FT /note="C->Y: In SY11."
FT /evidence="ECO:0000269|PubMed:8313880"
FT MUTAGEN 1065
FT /note="T->I: In sy16; larval lethality and lack of vulva
FT induction. Viability, vulva induction but not fertility are
FT restored in a let-60 (n1046gf) mutant background. Viability
FT is not restored in a lfe-1 (sy290) or lfe-2 (sy326) mutant
FT background. Fertility is restored in a let-60 (n1046gf) and
FT lfe-1 (sy290) mutant background."
FT /evidence="ECO:0000269|PubMed:8313880,
FT ECO:0000269|PubMed:9491893"
FT MUTAGEN 1074
FT /note="G->E: In SY7."
FT /evidence="ECO:0000269|PubMed:8313880"
FT MUTAGEN 1318..1323
FT /note="Missing: In sy1; reduces vulval induction. The
FT vulval induction incidence is further reduced in a chp-1
FT tm2277 mutant background."
FT /evidence="ECO:0000269|PubMed:32053105"
FT CONFLICT 1179
FT /note="D -> H (in Ref. 1; CAA40919)"
FT /evidence="ECO:0000305"
FT HELIX 880..882
FT /evidence="ECO:0007829|PDB:5WNO"
FT STRAND 883..892
FT /evidence="ECO:0007829|PDB:5WNO"
FT STRAND 898..904
FT /evidence="ECO:0007829|PDB:5WNO"
FT STRAND 914..921
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 929..939
FT /evidence="ECO:0007829|PDB:5WNO"
FT STRAND 949..954
FT /evidence="ECO:0007829|PDB:5WNO"
FT STRAND 959..964
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 971..977
FT /evidence="ECO:0007829|PDB:5WNO"
FT TURN 978..981
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 984..1003
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 1013..1015
FT /evidence="ECO:0007829|PDB:5WNO"
FT STRAND 1016..1020
FT /evidence="ECO:0007829|PDB:5WNO"
FT STRAND 1023..1026
FT /evidence="ECO:0007829|PDB:5WNO"
FT TURN 1032..1034
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 1049..1053
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 1056..1060
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 1066..1081
FT /evidence="ECO:0007829|PDB:5WNO"
FT TURN 1087..1090
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 1095..1101
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 1114..1122
FT /evidence="ECO:0007829|PDB:5WNO"
FT TURN 1128..1130
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 1134..1144
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 1148..1150
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 1160..1177
FT /evidence="ECO:0007829|PDB:5WNO"
FT TURN 1178..1180
FT /evidence="ECO:0007829|PDB:5WNO"
FT HELIX 1184..1189
FT /evidence="ECO:0007829|PDB:5WNO"
SQ SEQUENCE 1323 AA; 150511 MW; 6B0307EE53EEFA99 CRC64;
MRYPPSIGSI LLIIPIFLTF FGNSNAQLWK RCVSPQDCLC SGTTNGISRY GTGNILEDLE
TMYRGCRRVY GNLEITWIEA NEIKKWREST NSTVDPKNED SPLKSINFFD NLEEIRGSLI
IYRANIQKIS FPRLRVIYGD EVFHDNALYI HKNDKVHEVV MRELRVIRNG SVTIQDNPKM
CYIGDKIDWK ELLYDPDVQK VETTNSHQHC YQNGKSMAKC HESCNDKCWG SGDNDCQRVY
RSVCPKSCSQ CFYSNSTSSY ECCDSACLGG CTGHGPKNCI ACSKYELDGI CIETCPSRKI
FNHKTGRLVF NPDGRYQNGN HCVKECPPEL LIENDVCVRH CSDGHHYDAT KDVRECEKCR
SSSCPKICTV DGHLTNETLK NLEGCEQIDG HLIIEHAFTY EQLKVLETVK IVSEYITIVQ
QNFYDLKFLK NLQIIEGRKL HNVRWALAIY QCDDLEELSL NSLKLIKTGA VLIMKNHRLC
YVSKIDWSSI ITSKGKDNKP SLAIAENRDS KLCETEQRVC DKNCNKRGCW GKEPEDCLEC
KTWKSVGTCV EKCDTKGFLR NQTSMKCERC SPECETCNGL GELDCLTCRH KTLYNSDFGN
RMECVHDCPV SHFPTQKNVC EKCHPTCYDN GCTGPDSNLG YGGCKQCKYA VKYENDTIFC
LQSSGMNNVC VENDLPNYYI STYDTEGVIE THCEKCSISC KTCSSAGRNV VQNKCVCKHV
EYQPNPSERI CMDQCPVNSF MVPDTNNTVC KKCHHECDQN YHCANGQSTG CQKCKNFTVF
KGDIAQCVSE CPKNLPFSNP ANGECLDYDI ASRQRKTRMV IIGSVLFGFA VMFLFILLVY
WRCQRIGKKL KIAEMVDMPE LTPIDASVRP NMSRICLIPS SELQTKLDKK LGAGAFGTVF
AGIYYPKRAK NVKIPVAIKV FQTDQSQTDE MLEEATNMFR LRHDNLLKII GFCMHDDGLK
IVTIYRPLGN LQNFLKLHKE NLGAREQVLY CYQIASGMQY LEKQRVVHRD LATRNVLVKK
FNHVEITDFG LSKILKHDAD SITIKSGKVA IKWLAIEIFS KHCYTHASDV WAFGVTCWEI
ITFGQSPYQG MSTDSIHNFL KDGNRLSQPP NCSQDLYQEL LRCWMADPKS RPGFEILYER
FKEFCKVPQL FLENSNKISE SDLSAEERFQ TERIREMFDG NIDPQMYFDQ GSLPSMPSSP
TSMATFTIPH GDLMNRMQSV NSSRYKTEPF DYGSTAQEDN SYLIPKTKEV QQSAVLYTAV
TNEDGQTELS PSNGDYYNQP NTPSSSSGYY NEPHLKTKKP ETSEEAEAVQ YENEEVSQKE
TCL
