ILCR2_CAEEL
ID ILCR2_CAEEL Reviewed; 718 AA.
AC Q10128;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Interleukin cytokine receptor-related protein 2 {ECO:0000312|WormBase:F56D1.2};
DE AltName: Full=Interleukin-17 receptor-like protein 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=ilcr-2 {ECO:0000312|WormBase:F56D1.2};
GN ORFNames=F56D1.2 {ECO:0000312|WormBase:F56D1.2};
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 [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 [2]
RP FUNCTION, IDENTIFICATION IN RECEPTOR COMPLEX WITH ILCR-1, INTERACTION WITH
RP ACTL-1; ILC-17.1 AND ILCR-1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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-1, 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 Q10128; Q18008: actl-1; NbExp=2; IntAct=EBI-327172, EBI-324674;
CC Q10128; Q9NA64: ilcr-1; NbExp=3; IntAct=EBI-327172, EBI-16877763;
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, and in pharyngeal
CC muscle. {ECO:0000269|PubMed:28099418}.
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DR EMBL; BX284602; CCD68955.1; -; Genomic_DNA.
DR PIR; T30113; T30113.
DR RefSeq; NP_001022206.1; NM_001027035.3.
DR AlphaFoldDB; Q10128; -.
DR SMR; Q10128; -.
DR BioGRID; 39276; 4.
DR ComplexPortal; CPX-3401; Interleukin-17-like receptor complex.
DR DIP; DIP-25999N; -.
DR IntAct; Q10128; 2.
DR STRING; 6239.F56D1.2; -.
DR iPTMnet; Q10128; -.
DR EPD; Q10128; -.
DR PaxDb; Q10128; -.
DR PeptideAtlas; Q10128; -.
DR EnsemblMetazoa; F56D1.2.1; F56D1.2.1; WBGene00018960.
DR GeneID; 173932; -.
DR KEGG; cel:CELE_F56D1.2; -.
DR UCSC; F56D1.2; c. elegans.
DR CTD; 173932; -.
DR WormBase; F56D1.2; CE01970; WBGene00018960; ilcr-2.
DR eggNOG; ENOG502S3GM; Eukaryota.
DR HOGENOM; CLU_023540_0_0_1; -.
DR InParanoid; Q10128; -.
DR OMA; MIWPCRS; -.
DR OrthoDB; 578590at2759; -.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR SignaLink; Q10128; -.
DR PRO; PR:Q10128; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00018960; Expressed in embryo and 4 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:0050893; P:sensory processing; IC:ComplexPortal.
DR InterPro; IPR039465; IL-17_rcpt-like.
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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..718
FT /note="Interleukin cytokine receptor-related protein 2"
FT /id="PRO_0000014286"
FT TOPO_DOM 36..372
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..718
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 414..564
FT /note="SEFIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00867"
FT REGION 654..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..705
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 718 AA; 81622 MW; 42B9E056288417AA CRC64;
MVRLCTTNFL AYRATGSPLL LLYFYLCSLS SVKSSAAASY TNASDYVLRN VFEHSDQCYK
DSFVYVRADD KKSDPFITYS TTKECSERLK KNDLPEKLPT CPPGLIDLEL KPVYVPKSQI
SYPYANLNIS VTAHSSVDTI AFRLECLSAS DGSDVYCSNS KAMYINGVKE WPCRGIHLSS
RVQYPTRFSY SCFRLTSFSV YAINATILPQ KCRVSTIMTA PYFDDMFPEI LVDPTTNQSI
ITKTDPFWAP MLSADFSDKN AIWVRLGKAE RAECETMVVN VYKEHDDDSQ KVTFLEILTV
KCPETAVKWE NQKAGRYLLT AYVPIRGCKF YCEKKERGCR QCLRTHLNLV IYKNRASLSW
LALQKFKDYG FEIFIAVVVL LILIIVLAVT GFGYVLWRDK VRSREVRNIA LTEFVKVMIV
YADDNDLHTD CVKKLVENLR NCASCDPVFD LEKLITAEQI VPSRWLVDQI SSLKKFIIVV
SDCAEKILDT EASETHQLVQ ARPFADLFGP AMEMIIRDAT HNFPEARKKY AVVRFNYSPH
VPPNLAILNL PTFILPEQFA QLTAFLHNVE HTERANVTQN ISEAQIHEWN LCASRMMSFF
VRNPNWLETR WKPKDELAAL HLKRQSPVIV PIQTEEDRIA ASIKYNLVPP QALVDSDDED
DVDLQPHASH QNQPLILLPP EQCGPDSDSD SESDSSSESE SESDNEGEDP KTIVVKKS
