I17RD_DANRE
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 03-AUG-2022, entry version 98.
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};
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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.ENSDARP00000107809; -.
DR PaxDb; Q8QHJ9; -.
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 Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of 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 InterPro; IPR039465; IL-17_rcpt-like.
DR InterPro; IPR031951; IL17R_D_N.
DR InterPro; IPR013568; SEFIR_dom.
DR PANTHER; PTHR15583; PTHR15583; 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
