ILCR1_CAEEL
ID ILCR1_CAEEL Reviewed; 846 AA.
AC Q9NA64;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Interleukin cytokine receptor-related protein 1 {ECO:0000312|WormBase:Y64G10A.6};
DE AltName: Full=Interleukin-17 receptor-like protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=ilcr-1 {ECO:0000303|PubMed:28099418, ECO:0000312|WormBase:Y64G10A.6};
GN ORFNames=Y64G10A.6 {ECO:0000312|WormBase:Y64G10A.6};
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, IDENTIFICATION IN RECEPTOR COMPLEX WITH ILCR-2, INTERACTION WITH
RP ILCR-2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 159-GLN--HIS-846; 264-GLN--HIS-846; PRO-292; SER-487 AND 548-ARG--HIS-846.
RX PubMed=28099418; DOI=10.1038/nature20818;
RA Chen C., Itakura E., Nelson G.M., Sheng M., Laurent P., Fenk L.A.,
RA Butcher R.A., Hegde R.S., de Bono M.;
RT "IL-17 is a neuromodulator of Caenorhabditis elegans sensory responses.";
RL Nature 542:43-48(2017).
CC -!- FUNCTION: Forms a receptor complex together with receptor ilcr-2, which
CC upon activation acts as a modulator of neuronal activity. Binding of
CC the ligand ilc-17.1 to the ilcr-1/2 receptor complex triggers a
CC signaling cascade that activates the downsteam signaling components
CC actl-1, pik-1 and nfki-1, and results in increased neuronal activity in
CC RMG interneurons in response to input from oxygen-sensing neurons. This
CC leads to increased animal movement and promotes aggregation behavior.
CC {ECO:0000269|PubMed:28099418}.
CC -!- SUBUNIT: Component of a heterodimeric receptor complex composed of
CC ilcr-1 and ilcr-2. The receptor complex interacts with actl-1 and ilc-
CC 17.1 with the interaction being mediated by ilcr-2.
CC {ECO:0000269|PubMed:28099418}.
CC -!- INTERACTION:
CC Q9NA64; Q18008: actl-1; NbExp=2; IntAct=EBI-16877763, EBI-324674;
CC Q9NA64; Q10128: ilcr-2; NbExp=3; IntAct=EBI-16877763, EBI-327172;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28099418};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in most neurons.
CC {ECO:0000269|PubMed:28099418}.
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DR EMBL; BX284604; CAB54470.1; -; Genomic_DNA.
DR PIR; T27282; T27282.
DR RefSeq; NP_502736.1; NM_070335.4.
DR AlphaFoldDB; Q9NA64; -.
DR SMR; Q9NA64; -.
DR ComplexPortal; CPX-3401; Interleukin-17-like receptor complex.
DR IntAct; Q9NA64; 2.
DR STRING; 6239.Y64G10A.6; -.
DR PaxDb; Q9NA64; -.
DR EnsemblMetazoa; Y64G10A.6.1; Y64G10A.6.1; WBGene00013415.
DR GeneID; 178376; -.
DR KEGG; cel:CELE_Y64G10A.6; -.
DR UCSC; Y64G10A.6; c. elegans.
DR CTD; 178376; -.
DR WormBase; Y64G10A.6; CE22716; WBGene00013415; ilcr-1.
DR eggNOG; ENOG502RCG0; Eukaryota.
DR GeneTree; ENSGT00940000165644; -.
DR HOGENOM; CLU_015782_0_0_1; -.
DR InParanoid; Q9NA64; -.
DR OMA; CFEEYEV; -.
DR OrthoDB; 348230at2759; -.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR PRO; PR:Q9NA64; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00013415; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098797; C:plasma membrane protein complex; IDA:ComplexPortal.
DR GO; GO:0043235; C:receptor complex; IMP:UniProtKB.
DR GO; GO:0030368; F:interleukin-17 receptor activity; IBA:GO_Central.
DR GO; GO:0097400; P:interleukin-17-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0070482; P:response to oxygen levels; IMP:UniProtKB.
DR GO; GO:0050893; P:sensory processing; IC:ComplexPortal.
DR Gene3D; 2.60.40.2160; -; 1.
DR InterPro; IPR039465; IL-17_rcpt-like.
DR InterPro; IPR038683; IL17RA/B_FnIII-like_1_sf.
DR InterPro; IPR013568; SEFIR_dom.
DR PANTHER; PTHR15583; PTHR15583; 1.
DR Pfam; PF08357; SEFIR; 1.
DR PROSITE; PS51534; SEFIR; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..846
FT /note="Interleukin cytokine receptor-related protein 1"
FT /evidence="ECO:0000305"
FT /id="PRO_5004330844"
FT TOPO_DOM 26..418
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..846
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 476..618
FT /note="SEFIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00867"
FT REGION 388..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..771
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 159..846
FT /note="Missing: In db719; defective aggregation behavior."
FT /evidence="ECO:0000269|PubMed:28099418"
FT MUTAGEN 264..846
FT /note="Missing: Defective aggregation behavior."
FT /evidence="ECO:0000269|PubMed:28099418"
FT MUTAGEN 292
FT /note="P->L: Defective aggregation behavior."
FT /evidence="ECO:0000269|PubMed:28099418"
FT MUTAGEN 487
FT /note="S->F: Defective aggregation behavior."
FT /evidence="ECO:0000269|PubMed:28099418"
FT MUTAGEN 548..846
FT /note="Missing: Defective aggregation behavior."
FT /evidence="ECO:0000269|PubMed:28099418"
SQ SEQUENCE 846 AA; 94852 MW; 613AEF55EBB89EA4 CRC64;
MFLHSPALLI WLFLFCLAGP QAVRTEPYNS TSSSSSPTAN DVTSSDLLLL ASEETPTRAP
KPVTKQGKKN VVKVKKGGNG TVDDSPWVTD CSEPLNKDIS CSVNIIGCSD NVFKYVDAGQ
EPPRAHDVRI APTTKVMGAN RIDKRKHRLH VDVSWQIPQL EASTHLKAFK LIVNGPDGKN
TCFVFNVTQT HVDDEGISPR YRFSSNTLFD FGHNYTVTIV SLPMSRKRAP KVSATSLMPD
DPDAAPVKIV KTNEQMCEGK SNPQASKWAA SFRKIFLFSA IRLIQIEFLA APPQYCFEEY
EVRLLDSSGI VMLQSAIITK DELRTEIING RPVQFGEFNF TDIELDTDLI PSVIPIESAH
DGRCLCVTEN GCSCLAADWK PVKLTRIEKP PATSNQTEES DGKAEKDKKE DTTWTWHTYA
ITGGAIIAIL FILSVCAGLK CYKKFNNKKK ASNIHLLNEN PAFSHSGSIP LILKQSISVL
IVYSHDSAQH EAAVLAFAEL LRDVFNLNVH LDVWDEDDIE ENRAEYINSS IVRANKVIII
NSIGAYFRTV FRHQREPAIE RITTGRNDVI FDMQCELALQ HPCVISCHFS YTNPKYVFFP
INRLLQYSIP NSLMTMTTAL TEQPARPEQL AGFNQVFARL QAAISRKLNY IESDPQWFEN
THHRVATRRV SELEAHNIVP LPPSLEVKVE DEDAFGQMET LPIDELKEKF AAKRDLEVEV
LDSEDVKLLE DVKCAPGPIH VEPTEPEVLE PAEEPMEEAE EDEEDEDDVD SVEGQTARIE
ELQRLIVHKD MNHDSGNLDS AYVSGSDFSA DIHNEILDKP RLNAEMDLRK ANREDSAFHD
EVIGIH
