ID I17RD_DANRE Reviewed; 745 AA. AC Q8QHJ9; Q4VBV6; Q8QHJ6; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 2. DT 27-MAR-2024, entry version 104. DE RecName: Full=Interleukin-17 receptor D; DE Short=IL-17 receptor D; DE Short=IL-17RD; DE AltName: Full=Similar expression to FGF genes protein; DE Short=Sef; DE Flags: Precursor; GN Name=il17rd; Synonyms=cb208, sef; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH FGFR1 AND FGFR2. RX PubMed=11802164; DOI=10.1038/ncb749; RA Tsang M., Friesel R., Kudoh T., Dawid I.; RT "Identification of Sef, a novel modulator of FGF signalling."; RL Nat. Cell Biol. 4:165-169(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=11802165; DOI=10.1038/ncb750; RA Fuerthauer M., Lin W., Ang S.-L., Thisse B., Thisse C.; RT "Sef is a feedback-induced antagonist of Ras/MAPK-mediated FGF RT signalling."; RL Nat. Cell Biol. 4:170-174(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-441. RC TISSUE=Larva; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (MAY-2005) 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. {ECO:0000269|PubMed:11802164, CC ECO:0000269|PubMed:11802165}. CC -!- SUBUNIT: Interacts with fgfr1 and fgfr2. {ECO:0000269|PubMed:11802164}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- SEQUENCE CAUTION: CC Sequence=AAH94998.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF364103; AAL76112.1; -; mRNA. DR EMBL; AF401232; AAL78817.1; -; mRNA. DR EMBL; BC094998; AAH94998.1; ALT_SEQ; mRNA. DR AlphaFoldDB; Q8QHJ9; -. DR SMR; Q8QHJ9; -. DR STRING; 7955.ENSDARP00000140479; -. DR GlyCosmos; Q8QHJ9; 6 sites, No reported glycans. DR PaxDb; 7955-ENSDARP00000107809; -. DR AGR; ZFIN:ZDB-GENE-020320-5; -. DR ZFIN; ZDB-GENE-020320-5; il17rd. DR eggNOG; ENOG502QV61; Eukaryota. DR InParanoid; Q8QHJ9; -. DR PhylomeDB; Q8QHJ9; -. DR Reactome; R-DRE-5674135; MAP2K and MAPK activation. DR PRO; PR:Q8QHJ9; -. DR Proteomes; UP000000437; Genome assembly. DR GO; GO:0016020; C:membrane; ISS:ZFIN. DR GO; GO:0030368; F:interleukin-17 receptor activity; IBA:GO_Central. DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN. DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IMP:ZFIN. DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:ZFIN. DR Gene3D; 3.40.50.11530; -; 1. DR InterPro; IPR039465; IL-17_rcpt-like. DR InterPro; IPR031951; IL17R_D_N. DR InterPro; IPR013568; SEFIR_dom. DR PANTHER; PTHR15583; INTERLEUKIN-17 RECEPTOR; 1. DR PANTHER; PTHR15583:SF19; INTERLEUKIN-17 RECEPTOR D; 1. DR Pfam; PF16742; IL17R_D_N; 1. DR Pfam; PF08357; SEFIR; 1. DR PROSITE; PS51534; SEFIR; 1. PE 1: Evidence at protein level; KW Glycoprotein; Membrane; Receptor; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..745 FT /note="Interleukin-17 receptor D" FT /id="PRO_0000041874" FT TOPO_DOM 27..298 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 299..319 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 320..745 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 354..518 FT /note="SEFIR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00867" FT REGION 432..454 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 631..713 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 631..646 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 691..708 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 61 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 79 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 136 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 170 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 205 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 276 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 67 FT /note="S -> N (in Ref. 1; AAL76112)" FT /evidence="ECO:0000305" FT CONFLICT 81 FT /note="S -> T (in Ref. 1; AAL76112)" FT /evidence="ECO:0000305" FT CONFLICT 167 FT /note="T -> N (in Ref. 2; AAL78817)" FT /evidence="ECO:0000305" FT CONFLICT 739 FT /note="L -> F (in Ref. 2; AAL78817)" FT /evidence="ECO:0000305" SQ SEQUENCE 745 AA; 83391 MW; 6F8998D63D9DA24F CRC64; MAGSRRLAHF FMASCLFLCY TASVNGGKRG NSDKCSYKQG TQTSSMDEGA RKLGVTFRYD NCSVNWSPLG KHAIHEVNNI SFSHLSCDSQ AAVVVHWMAS PLGIEHVKGF RVYLEDKNPE RKQCQHLILK DPRQLNFSYK TIRMSSQPFS SLAFETDYMV RIVPFPTFLN DSFFPPSFLR TNSCEVLLGP DNLVCKPFWK PKMLNVSQLG SNLHVVFDHA PSTFGFSIYY LYYKLRQEGP FRLKRCKPEQ NGPKTTCVLQ DVTPGTYAIE LRDDSNNTRR QTQYHVSQVH SPWAGPIRAM AITVPLVIMS AFATLFTVMC RKKQQENIYS HLDEESSESS SQTTALSADR PWPRPKIFIC YSSRDGAKHL AVIQSFAFFL QDFCGCEVSL DLWEHLEICK EGQMSWLSRR IDEAHFIITV CSKGLKHFVE KRHRKGKATS KEKNREPSAS DSSSSSRDLF IVASAIISEK LKEVHQKSSD LSRFMSVYFD YSHETDVPTS LSLAPKFKLM DQLPQLFARL HSRQLSLTDR EPQPPNVSKR NYFCSKSGRS LYVAIYNMHQ HVTQEPDWLE KELMPPPLPN KRTIPEKVDS GLVLNEVKLK HGSESECPPV RSNVLILPQT PQVGVSLSLS REDLGEGSSS QDAGSCRPVL HTDGSASPPE MPRDSGIYDS SVPSSELSIP LMDGLSPDHA DNSSLADSVS SSSGLGDEEP PAVSSLHCTA HTICKADLHH QHLHPSEGLI AAAST //