ID   I17RD_CHICK             Reviewed;         741 AA.
AC   Q7T2L7; Q8AV76;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Interleukin-17 receptor D;
DE            Short=IL-17 receptor D;
DE            Short=IL-17RD;
DE   AltName: Full=Sef homolog;
DE            Short=cSEF;
DE   Flags: Precursor;
GN   Name=IL17RD; Synonyms=SEF;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12766772; DOI=10.1038/ncb989;
RA   Kawakami Y., Rodriguez-Leon J., Koth C.M., Buescher D., Itoh T., Raya A.,
RA   Ng J.K., Rodriguez Esteban C., Takahashi S., Henrique D., Schwarz M.-F.,
RA   Asahara H., Izpisua Belmonte J.C.;
RT   "MKP3 mediates the cellular response to FGF8 signalling in the vertebrate
RT   limb.";
RL   Nat. Cell Biol. 5:513-519(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 45-741.
RC   TISSUE=Mesenchymal cell;
RA   Neubueser A.;
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Feedback inhibitor of fibroblast growth factor mediated Ras-
CC       MAPK signaling and ERK activation. May inhibit FGF-induced FGFR1
CC       tyrosine phosphorylation (By similarity). Inhibits TGFB-induced
CC       epithelial-to-mesenchymal transition in lens epithelial cells (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8JZL1}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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DR   EMBL; AY278204; AAP70001.1; -; mRNA.
DR   EMBL; AJ508679; CAD48485.1; -; mRNA.
DR   RefSeq; NP_989846.1; NM_204515.1.
DR   AlphaFoldDB; Q7T2L7; -.
DR   SMR; Q7T2L7; -.
DR   STRING; 9031.ENSGALP00000008813; -.
DR   PaxDb; Q7T2L7; -.
DR   GeneID; 395186; -.
DR   KEGG; gga:395186; -.
DR   CTD; 54756; -.
DR   VEuPathDB; HostDB:geneid_395186; -.
DR   eggNOG; ENOG502QV61; Eukaryota.
DR   InParanoid; Q7T2L7; -.
DR   OrthoDB; 184720at2759; -.
DR   PhylomeDB; Q7T2L7; -.
DR   PRO; PR:Q7T2L7; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030368; F:interleukin-17 receptor activity; IBA:GO_Central.
DR   InterPro; IPR039465; IL-17_rcpt-like.
DR   InterPro; IPR031951; IL17R_D_N.
DR   InterPro; IPR013568; SEFIR_dom.
DR   InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR   PANTHER; PTHR15583; PTHR15583; 1.
DR   Pfam; PF16742; IL17R_D_N; 1.
DR   Pfam; PF08357; SEFIR; 1.
DR   SUPFAM; SSF52200; SSF52200; 1.
DR   PROSITE; PS51534; SEFIR; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..741
FT                   /note="Interleukin-17 receptor D"
FT                   /id="PRO_0000041873"
FT   TOPO_DOM        27..301
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        323..741
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          357..510
FT                   /note="SEFIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00867"
FT   REGION          688..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..707
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   741 AA;  83554 MW;  64B8E88241AC60CF CRC64;
     MAPGRELGAF LLALLAFCGG RRLAEAAGGP GGRRGAAADA CGGRGLSSVT KSNGLLNITF
     KYDNCTPYLN SVGKHVIGDV QNITISQYAC YEQVAVTILW TANAIGIEYL RGFRVILEEL
     KSEGRQCQQM VLRDPKQLSP SFKRTGMESN PFANLKFETD YFVKIVPFPS IKNESNYHPF
     FFRTRPCELL LQPENLICKP YWKPRNLNVT QQGFNMQVSF DHAPHNFGFR YYFLHYKLKH
     EGPFKQKTCK QDQNTDTTSC ILQNVTPGDY IIELVDDTNT TRKTMHYALK PVHSPWAGPI
     RAIAITVPLV VISAFATLFT VMCRKKQQEN IYSHLDEESS ESSAYGAGLP VERLRPRPKV
     FICYSSKDCQ KHINVIQCFA YFLQDFCGCE VALDLWEDLK ICKESQKEWL IKKINESQFI
     IIVCSKGMKY FVEKKNWKHR GVTKDTGKGE LFLFAVFTVA EKLRQAKQNS NDLCKFIAVY
     FDYSCEGDIP GILDLSTKYK LMDNLPQLYS HLHSRDLSVQ DSEVFPVNVS KRNYFRSKSG
     RSLYVAICNM HQFIDQEPDW FEKQFIPFLP HPLHYSEPVM EKFDSGLVLN DLVNKQAADD
     DFYLKTDVNI ISAGSSDSHC IIQHLNLGED VETQDIQRGG SSVLRPLLHA VKASNLKDMP
     RDSGIYDSSV PSSELSLPLM EGLLTDQTET SSITGSVSSS SGLGEEEPPV ITSTKFLLPG
     ICKAELHCHI HTDELQAIAP L