P24348 · LET23_CAEEL
- ProteinReceptor tyrosine-protein kinase let-23
- Genelet-23
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1323 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tyrosine-protein kinase receptor which, upon binding ligand lin-3, activates 2 signaling cascades: the let-60/Ras and MAP kinase signaling pathway and the let-60-independent phospholipase C-mediated Ca2+ signaling pathway. Each pathway regulates distinct functions. By activating let-60/Ras, regulates larval development, induction of vulva cell precursors during vulva development, male spicule formation and posterior development of the epidermis (PubMed:20230814, PubMed:2071015, PubMed:32053105, PubMed:8313880, PubMed:9491893).
Probably by activating phospholipase plc-3 and inositol 1,4,5-trisphosphate receptor itr-1 signaling cascade downstream of ligand lin-3, plays a role in ovulation by promoting ovulatory gonadal sheath cell contractions (PubMed:15194811, PubMed:9491893).
Probably by regulating neuronal transmission in ALA neurons, mediates, independently of let-60/Ras, the decrease in pharyngeal pumping and locomotion during the quiescent state that precedes each larval molt, downstream of lin-3 and upstream of plc-3 (PubMed:17891142).
Probably by activating phospholipase plc-3 and inositol 1,4,5-trisphosphate receptor itr-1 signaling cascade downstream of ligand lin-3, plays a role in ovulation by promoting ovulatory gonadal sheath cell contractions (PubMed:15194811, PubMed:9491893).
Probably by regulating neuronal transmission in ALA neurons, mediates, independently of let-60/Ras, the decrease in pharyngeal pumping and locomotion during the quiescent state that precedes each larval molt, downstream of lin-3 and upstream of plc-3 (PubMed:17891142).
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReceptor tyrosine-protein kinase let-23
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionP24348
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Apical cell membrane ; Single-pass type I membrane protein
Basolateral cell membrane ; Single-pass type I membrane protein
Note: Basolateral and apical membrane of cell junctions in epithelial vulval precursor cells.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 21-818 | Extracellular | ||||
Sequence: FGNSNAQLWKRCVSPQDCLCSGTTNGISRYGTGNILEDLETMYRGCRRVYGNLEITWIEANEIKKWRESTNSTVDPKNEDSPLKSINFFDNLEEIRGSLIIYRANIQKISFPRLRVIYGDEVFHDNALYIHKNDKVHEVVMRELRVIRNGSVTIQDNPKMCYIGDKIDWKELLYDPDVQKVETTNSHQHCYQNGKSMAKCHESCNDKCWGSGDNDCQRVYRSVCPKSCSQCFYSNSTSSYECCDSACLGGCTGHGPKNCIACSKYELDGICIETCPSRKIFNHKTGRLVFNPDGRYQNGNHCVKECPPELLIENDVCVRHCSDGHHYDATKDVRECEKCRSSSCPKICTVDGHLTNETLKNLEGCEQIDGHLIIEHAFTYEQLKVLETVKIVSEYITIVQQNFYDLKFLKNLQIIEGRKLHNVRWALAIYQCDDLEELSLNSLKLIKTGAVLIMKNHRLCYVSKIDWSSIITSKGKDNKPSLAIAENRDSKLCETEQRVCDKNCNKRGCWGKEPEDCLECKTWKSVGTCVEKCDTKGFLRNQTSMKCERCSPECETCNGLGELDCLTCRHKTLYNSDFGNRMECVHDCPVSHFPTQKNVCEKCHPTCYDNGCTGPDSNLGYGGCKQCKYAVKYENDTIFCLQSSGMNNVCVENDLPNYYISTYDTEGVIETHCEKCSISCKTCSSAGRNVVQNKCVCKHVEYQPNPSERICMDQCPVNSFMVPDTNNTVCKKCHHECDQNYHCANGQSTGCQKCKNFTVFKGDIAQCVSECPKNLPFSNPANGECLDYDIASRQRKTR | ||||||
Transmembrane | 819-839 | Helical | ||||
Sequence: MVIIGSVLFGFAVMFLFILLV | ||||||
Topological domain | 840-1323 | Cytoplasmic | ||||
Sequence: YWRCQRIGKKLKIAEMVDMPELTPIDASVRPNMSRICLIPSSELQTKLDKKLGAGAFGTVFAGIYYPKRAKNVKIPVAIKVFQTDQSQTDEMLEEATNMFRLRHDNLLKIIGFCMHDDGLKIVTIYRPLGNLQNFLKLHKENLGAREQVLYCYQIASGMQYLEKQRVVHRDLATRNVLVKKFNHVEITDFGLSKILKHDADSITIKSGKVAIKWLAIEIFSKHCYTHASDVWAFGVTCWEIITFGQSPYQGMSTDSIHNFLKDGNRLSQPPNCSQDLYQELLRCWMADPKSRPGFEILYERFKEFCKVPQLFLENSNKISESDLSAEERFQTERIREMFDGNIDPQMYFDQGSLPSMPSSPTSMATFTIPHGDLMNRMQSVNSSRYKTEPFDYGSTAQEDNSYLIPKTKEVQQSAVLYTAVTNEDGQTELSPSNGDYYNQPNTPSSSSGYYNEPHLKTKKPETSEEAEAVQYENEEVSQKETCL |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Larval lethality, lack of vulva formation, infertility and lack of male spicule formation (PubMed:2071015).
RNAi-mediated knockdown causes sterility, a small decrease in the peak rate of sheath cell contractions and a delay in the onset of ovulatory contractions (PubMed:15194811).
Restores normal pharyngeal pumping rate in 30 percent of animals overexpressing lin-3 (PubMed:17891142).
RNAi-mediated knockdown causes sterility, a small decrease in the peak rate of sheath cell contractions and a delay in the onset of ovulatory contractions (PubMed:15194811).
Restores normal pharyngeal pumping rate in 30 percent of animals overexpressing lin-3 (PubMed:17891142).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 364 | In sa62; multivulva phenotype. RNAi-mediated knockdown of let-765 suppresses the multivulva phenotype. Multivulva phenotype enhanced in a swsn-4 (sy598) mutant background. | ||||
Sequence: C → Y | ||||||
Mutagenesis | 368 | In sy10; severe larval lethality, lack of vulva induction, infertile and lack of male spicule formation. Impaired ovulation characterized by a delay in the initiation of ovulatory sheath cell contractions and prolonged ovulatory contractions. | ||||
Sequence: C → Y | ||||||
Mutagenesis | 469 | In mn216; larval lethality. | ||||
Sequence: G → R | ||||||
Mutagenesis | 700 | In mn23; larval lethality. | ||||
Sequence: C → W | ||||||
Mutagenesis | 753 | In SY11. | ||||
Sequence: C → Y | ||||||
Mutagenesis | 1065 | In sy16; larval lethality and lack of vulva induction. Viability, vulva induction but not fertility are restored in a let-60 (n1046gf) mutant background. Viability is not restored in a lfe-1 (sy290) or lfe-2 (sy326) mutant background. Fertility is restored in a let-60 (n1046gf) and lfe-1 (sy290) mutant background. | ||||
Sequence: T → I | ||||||
Mutagenesis | 1074 | In SY7. | ||||
Sequence: G → E | ||||||
Mutagenesis | 1318-1323 | In sy1; reduces vulval induction. The vulval induction incidence is further reduced in a chp-1 tm2277 mutant background and in swsn-4 (os13) and swsn-1 (os22) mutant backgrounds. | ||||
Sequence: Missing |
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MRYPPSIGSILLIIPIFLTF | ||||||
Chain | PRO_0000016677 | 21-1323 | Receptor tyrosine-protein kinase let-23 | |||
Sequence: FGNSNAQLWKRCVSPQDCLCSGTTNGISRYGTGNILEDLETMYRGCRRVYGNLEITWIEANEIKKWRESTNSTVDPKNEDSPLKSINFFDNLEEIRGSLIIYRANIQKISFPRLRVIYGDEVFHDNALYIHKNDKVHEVVMRELRVIRNGSVTIQDNPKMCYIGDKIDWKELLYDPDVQKVETTNSHQHCYQNGKSMAKCHESCNDKCWGSGDNDCQRVYRSVCPKSCSQCFYSNSTSSYECCDSACLGGCTGHGPKNCIACSKYELDGICIETCPSRKIFNHKTGRLVFNPDGRYQNGNHCVKECPPELLIENDVCVRHCSDGHHYDATKDVRECEKCRSSSCPKICTVDGHLTNETLKNLEGCEQIDGHLIIEHAFTYEQLKVLETVKIVSEYITIVQQNFYDLKFLKNLQIIEGRKLHNVRWALAIYQCDDLEELSLNSLKLIKTGAVLIMKNHRLCYVSKIDWSSIITSKGKDNKPSLAIAENRDSKLCETEQRVCDKNCNKRGCWGKEPEDCLECKTWKSVGTCVEKCDTKGFLRNQTSMKCERCSPECETCNGLGELDCLTCRHKTLYNSDFGNRMECVHDCPVSHFPTQKNVCEKCHPTCYDNGCTGPDSNLGYGGCKQCKYAVKYENDTIFCLQSSGMNNVCVENDLPNYYISTYDTEGVIETHCEKCSISCKTCSSAGRNVVQNKCVCKHVEYQPNPSERICMDQCPVNSFMVPDTNNTVCKKCHHECDQNYHCANGQSTGCQKCKNFTVFKGDIAQCVSECPKNLPFSNPANGECLDYDIASRQRKTRMVIIGSVLFGFAVMFLFILLVYWRCQRIGKKLKIAEMVDMPELTPIDASVRPNMSRICLIPSSELQTKLDKKLGAGAFGTVFAGIYYPKRAKNVKIPVAIKVFQTDQSQTDEMLEEATNMFRLRHDNLLKIIGFCMHDDGLKIVTIYRPLGNLQNFLKLHKENLGAREQVLYCYQIASGMQYLEKQRVVHRDLATRNVLVKKFNHVEITDFGLSKILKHDADSITIKSGKVAIKWLAIEIFSKHCYTHASDVWAFGVTCWEIITFGQSPYQGMSTDSIHNFLKDGNRLSQPPNCSQDLYQELLRCWMADPKSRPGFEILYERFKEFCKVPQLFLENSNKISESDLSAEERFQTERIREMFDGNIDPQMYFDQGSLPSMPSSPTSMATFTIPHGDLMNRMQSVNSSRYKTEPFDYGSTAQEDNSYLIPKTKEVQQSAVLYTAVTNEDGQTELSPSNGDYYNQPNTPSSSSGYYNEPHLKTKKPETSEEAEAVQYENEEVSQKETCL | ||||||
Glycosylation | 91 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 169 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 220↔228 | |||||
Sequence: CHESCNDKC | ||||||
Disulfide bond | 224↔236 | |||||
Sequence: CNDKCWGSGDNDC | ||||||
Disulfide bond | 244↔251 | |||||
Sequence: CPKSCSQC | ||||||
Disulfide bond | 248↔262 | |||||
Sequence: CSQCFYSNSTSSYEC | ||||||
Glycosylation | 255 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 263↔271 | |||||
Sequence: CDSACLGGC | ||||||
Disulfide bond | 267↔279 | |||||
Sequence: CLGGCTGHGPKNC | ||||||
Disulfide bond | 282↔291 | |||||
Sequence: CSKYELDGIC | ||||||
Disulfide bond | 295↔322 | |||||
Sequence: CPSRKIFNHKTGRLVFNPDGRYQNGNHC | ||||||
Disulfide bond | 326↔337 | |||||
Sequence: CPPELLIENDVC | ||||||
Disulfide bond | 341↔356 | |||||
Sequence: CSDGHHYDATKDVREC | ||||||
Disulfide bond | 359↔364 | |||||
Sequence: CRSSSC | ||||||
Glycosylation | 376 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 520↔529 | |||||
Sequence: CDKNCNKRGC | ||||||
Disulfide bond | 524↔537 | |||||
Sequence: CNKRGCWGKEPEDC | ||||||
Disulfide bond | 540↔549 | |||||
Sequence: CKTWKSVGTC | ||||||
Disulfide bond | 553↔567 | |||||
Sequence: CDTKGFLRNQTSMKC | ||||||
Glycosylation | 561 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 570↔577 | |||||
Sequence: CSPECETC | ||||||
Disulfide bond | 574↔585 | |||||
Sequence: CETCNGLGELDC | ||||||
Disulfide bond | 588↔604 | |||||
Sequence: CRHKTLYNSDFGNRMEC | ||||||
Disulfide bond | 608↔620 | |||||
Sequence: CPVSHFPTQKNVC | ||||||
Disulfide bond | 623↔632 | |||||
Sequence: CHPTCYDNGC | ||||||
Disulfide bond | 627↔644 | |||||
Sequence: CYDNGCTGPDSNLGYGGC | ||||||
Disulfide bond | 647↔660 | |||||
Sequence: CKYAVKYENDTIFC | ||||||
Glycosylation | 655 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 670↔693 | |||||
Sequence: CVENDLPNYYISTYDTEGVIETHC | ||||||
Disulfide bond | 696↔703 | |||||
Sequence: CSISCKTC | ||||||
Disulfide bond | 700↔715 | |||||
Sequence: CKTCSSAGRNVVQNKC | ||||||
Disulfide bond | 717↔731 | |||||
Sequence: CKHVEYQPNPSERIC | ||||||
Disulfide bond | 735↔750 | |||||
Sequence: CPVNSFMVPDTNNTVC | ||||||
Glycosylation | 746 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 753↔763 | |||||
Sequence: CHHECDQNYHC | ||||||
Disulfide bond | 757↔771 | |||||
Sequence: CDQNYHCANGQSTGC | ||||||
Disulfide bond | 774↔787 | |||||
Sequence: CKNFTVFKGDIAQC | ||||||
Glycosylation | 776 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 791↔805 | |||||
Sequence: CPKNLPFSNPANGEC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in vulval precursor cells (at protein level) (PubMed:10359617).
Expressed in ALA neurons, 2 ventral head neurons, a single neuron in the tail, pharyngeal-intestinal valve and posterior arcade epithelial cells (PubMed:17891142).
Expressed in ALA neurons, 2 ventral head neurons, a single neuron in the tail, pharyngeal-intestinal valve and posterior arcade epithelial cells (PubMed:17891142).
Developmental stage
Expressed during L2 and L3 larval stages (PubMed:10359617).
Highly expressed in vulval precursor cells P6.p in late L2 and early L3 stage larvae (PubMed:32053105).
Highly expressed in vulval precursor cells P6.p in late L2 and early L3 stage larvae (PubMed:32053105).
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 885-1152 | Protein kinase | ||||
Sequence: TKLDKKLGAGAFGTVFAGIYYPKRAKNVKIPVAIKVFQTDQSQTDEMLEEATNMFRLRHDNLLKIIGFCMHDDGLKIVTIYRPLGNLQNFLKLHKENLGAREQVLYCYQIASGMQYLEKQRVVHRDLATRNVLVKKFNHVEITDFGLSKILKHDADSITIKSGKVAIKWLAIEIFSKHCYTHASDVWAFGVTCWEIITFGQSPYQGMSTDSIHNFLKDGNRLSQPPNCSQDLYQELLRCWMADPKSRPGFEILYERFKEFCKVPQLFL | ||||||
Compositional bias | 1265-1292 | Polar residues | ||||
Sequence: GQTELSPSNGDYYNQPNTPSSSSGYYNE | ||||||
Region | 1265-1323 | Disordered | ||||
Sequence: GQTELSPSNGDYYNQPNTPSSSSGYYNEPHLKTKKPETSEEAEAVQYENEEVSQKETCL |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,323
- Mass (Da)150,511
- Last updated2006-07-25 v3
- Checksum6B0307EE53EEFA99
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0K3AX35 | A0A0K3AX35_CAEEL | let-23 | 1335 | ||
B5BM27 | B5BM27_CAEEL | let-23 | 1328 | ||
B5BM28 | B5BM28_CAEEL | let-23 | 1262 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1179 | in Ref. 1; CAA40919 | ||||
Sequence: D → H | ||||||
Compositional bias | 1265-1292 | Polar residues | ||||
Sequence: GQTELSPSNGDYYNQPNTPSSSSGYYNE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X57767 EMBL· GenBank· DDBJ | CAA40919.1 EMBL· GenBank· DDBJ | mRNA | ||
D63426 EMBL· GenBank· DDBJ | BAA09729.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BX284602 EMBL· GenBank· DDBJ | CAA93882.3 EMBL· GenBank· DDBJ | Genomic DNA |