I17RD_MOUSE
ID I17RD_MOUSE Reviewed; 738 AA.
AC Q8JZL1; B2RRY7; Q8K447; Q8R5J8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Interleukin-17 receptor D;
DE Short=IL-17 receptor D;
DE Short=IL-17RD;
DE AltName: Full=Interleukin-17 receptor-like protein;
DE AltName: Full=Sef homolog;
DE Short=mSef;
DE Flags: Precursor;
GN Name=Il17rd; Synonyms=Il17rlm, Sef;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RX PubMed=11960706; DOI=10.1016/s0925-4773(02)00018-7;
RA Lin W., Fuerthauer M., Thisse B., Thisse C., Jing N., Ang S.-L.;
RT "Cloning of the mouse Sef gene and comparative analysis of its expression
RT with Fgf8 and Spry2 during embryogenesis.";
RL Mech. Dev. 113:163-168(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ;
RX PubMed=12958313; DOI=10.1074/jbc.m306936200;
RA Xiong S.Q., Zhao Q.H., Rong Z., Huang G.R., Huang Y., Chen P.L., Zhang S.,
RA Liu L., Chang Z.J.;
RT "hSef inhibits PC-12 cell differentiation by interfering with Ras-mitogen-
RT activated protein kinase MAPK signaling.";
RL J. Biol. Chem. 278:50273-50282(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH FGFR1.
RX PubMed=12604616; DOI=10.1074/jbc.c200606200;
RA Kovalenko D., Yang X., Nadeau R.J., Harkins L.K., Friesel R.;
RT "Sef inhibits fibroblast growth factor signaling by inhibiting FGFR1
RT tyrosine phosphorylation and subsequent ERK activation.";
RL J. Biol. Chem. 278:14087-14091(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH MAP3K7.
RX PubMed=15277532; DOI=10.1074/jbc.c400318200;
RA Yang X., Kovalenko D., Nadeau R.J., Harkins L.K., Mitchell J., Zubanova O.,
RA Chen P.-Y., Friesel R.;
RT "Sef interacts with TAK1 and mediates JNK activation and apoptosis.";
RL J. Biol. Chem. 279:38099-38102(2004).
RN [6]
RP POSSIBLE FUNCTION IN GNRH NEURON FATE SPECIFICATION.
RX PubMed=23643382; DOI=10.1016/j.ajhg.2013.04.008;
RA Miraoui H., Dwyer A.A., Sykiotis G.P., Plummer L., Chung W., Feng B.,
RA Beenken A., Clarke J., Pers T.H., Dworzynski P., Keefe K., Niedziela M.,
RA Raivio T., Crowley W.F. Jr., Seminara S.B., Quinton R., Hughes V.A.,
RA Kumanov P., Young J., Yialamas M.A., Hall J.E., Van Vliet G.,
RA Chanoine J.P., Rubenstein J., Mohammadi M., Tsai P.S., Sidis Y., Lage K.,
RA Pitteloud N.;
RT "Mutations in FGF17, IL17RD, DUSP6, SPRY4, and FLRT3 are identified in
RT individuals with congenital hypogonadotropic hypogonadism.";
RL Am. J. Hum. Genet. 92:725-743(2013).
RN [7]
RP FUNCTION.
RX PubMed=25576668; DOI=10.1016/j.exer.2015.01.001;
RA Zhao G., Wojciechowski M.C., Jee S., Boros J., McAvoy J.W., Lovicu F.J.;
RT "Negative regulation of TGFbeta-induced lens epithelial to mesenchymal
RT transition (EMT) by RTK antagonists.";
RL Exp. Eye Res. 132:9-16(2015).
CC -!- FUNCTION: Feedback inhibitor of fibroblast growth factor mediated Ras-
CC MAPK signaling and ERK activation (PubMed:12604616). Regulates the
CC nuclear ERK signaling pathway by spatially blocking nuclear
CC translocation of activated ERK (By similarity). Mediates JNK activation
CC and may be involved in apoptosis (PubMed:15277532). May inhibit FGF-
CC induced FGFR1 tyrosine phosphorylation (PubMed:12604616). Might have a
CC role in the early stages of fate specification of GnRH-secreting
CC neurons (PubMed:23643382). Inhibits TGFB-induced epithelial-to-
CC mesenchymal transition in lens epithelial cells (PubMed:25576668).
CC {ECO:0000250|UniProtKB:Q8NFM7, ECO:0000269|PubMed:12604616,
CC ECO:0000269|PubMed:15277532, ECO:0000269|PubMed:23643382,
CC ECO:0000269|PubMed:25576668}.
CC -!- SUBUNIT: Self-associates. Interacts with FGFR2 and phosphorylated
CC MAP2K1 or MAP2K2. Associates with a MAP2K1/2-MAPK1/3 complex (By
CC similarity). Interacts with FGFR1 and MAP3K7. {ECO:0000250,
CC ECO:0000269|PubMed:12604616, ECO:0000269|PubMed:15277532}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type I membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Note=Associated with the Golgi apparatus and is partially translocated
CC to the plasma membrane upon stimulation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=IL17RLM-L, Long;
CC IsoId=Q8JZL1-1; Sequence=Displayed;
CC Name=2; Synonyms=IL17RLM-S, Short;
CC IsoId=Q8JZL1-2; Sequence=VSP_015585;
CC -!- DEVELOPMENTAL STAGE: During early embryogenesis, predominantly
CC expressed at 6.5 dpc and 9.5 dpc in the forebrain, mid-hindbrain
CC boundary, branchial arches, somites, limb bud and tailbud. At 12.5 dpc
CC additionally expressed in the diencephalon, optic stalk, pituitary,
CC olfactory and oral epithelium, tooth primordia, somites, developing
CC metanephric kidney and stomach. Expressed in the neopallial cortex,
CC rhombic lip and dorsal regions of the myelencephalon and in the frontal
CC nasal process. Expressed in the commissural plate and septal area of
CC the forebrain and in the hippocampus, lens and optic cup. In the oral
CC region, expressed in the tongue and in the mesenchyme of the first
CC branchial arch. Also expressed in the developing inner ear. Expression
CC patterns remain essentially unchanged at 15.5 dpc, with the addition of
CC a strong expression in the submandibular gland.
CC {ECO:0000269|PubMed:11960706}.
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; AF459444; AAM28441.1; -; mRNA.
DR EMBL; AF424804; AAL79530.1; -; mRNA.
DR EMBL; AF494209; AAM74078.1; -; mRNA.
DR EMBL; AF494210; AAM74079.1; -; mRNA.
DR EMBL; BC138629; AAI38630.1; -; mRNA.
DR CCDS; CCDS26885.1; -. [Q8JZL1-1]
DR RefSeq; NP_602319.1; NM_134437.3. [Q8JZL1-1]
DR RefSeq; XP_006518731.1; XM_006518668.2. [Q8JZL1-2]
DR AlphaFoldDB; Q8JZL1; -.
DR SMR; Q8JZL1; -.
DR BioGRID; 228596; 3.
DR STRING; 10090.ENSMUSP00000036076; -.
DR GlyGen; Q8JZL1; 8 sites.
DR PhosphoSitePlus; Q8JZL1; -.
DR MaxQB; Q8JZL1; -.
DR PaxDb; Q8JZL1; -.
DR PeptideAtlas; Q8JZL1; -.
DR PRIDE; Q8JZL1; -.
DR ProteomicsDB; 267076; -. [Q8JZL1-1]
DR ProteomicsDB; 267077; -. [Q8JZL1-2]
DR Antibodypedia; 31518; 317 antibodies from 31 providers.
DR DNASU; 171463; -.
DR Ensembl; ENSMUST00000035336; ENSMUSP00000036076; ENSMUSG00000040717. [Q8JZL1-1]
DR Ensembl; ENSMUST00000225146; ENSMUSP00000153543; ENSMUSG00000040717. [Q8JZL1-2]
DR GeneID; 171463; -.
DR KEGG; mmu:171463; -.
DR UCSC; uc007stl.1; mouse. [Q8JZL1-1]
DR CTD; 54756; -.
DR MGI; MGI:2159727; Il17rd.
DR VEuPathDB; HostDB:ENSMUSG00000040717; -.
DR eggNOG; ENOG502QV61; Eukaryota.
DR GeneTree; ENSGT00940000156669; -.
DR HOGENOM; CLU_024846_0_0_1; -.
DR InParanoid; Q8JZL1; -.
DR OMA; DFCLKAE; -.
DR OrthoDB; 184720at2759; -.
DR PhylomeDB; Q8JZL1; -.
DR TreeFam; TF329644; -.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR BioGRID-ORCS; 171463; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Il17rd; mouse.
DR PRO; PR:Q8JZL1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8JZL1; protein.
DR Bgee; ENSMUSG00000040717; Expressed in vestibular epithelium and 206 other tissues.
DR ExpressionAtlas; Q8JZL1; baseline and differential.
DR Genevisible; Q8JZL1; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030368; F:interleukin-17 receptor activity; IBA:GO_Central.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR InterPro; IPR039465; IL-17_rcpt-like.
DR InterPro; IPR031951; IL17R_D_N.
DR InterPro; IPR013568; SEFIR_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
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 Alternative splicing; Cell membrane; Glycoprotein; Golgi apparatus;
KW Membrane; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..738
FT /note="Interleukin-17 receptor D"
FT /id="PRO_0000041872"
FT TOPO_DOM 17..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 355..509
FT /note="SEFIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00867"
FT REGION 653..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12958313"
FT /id="VSP_015585"
FT CONFLICT 715
FT /note="L -> F (in Ref. 2; AAM74078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 738 AA; 82348 MW; D8CE66230E3E8226 CRC64;
MAPWLQLCSF FFTVNACLNG SQLAVAAGGS GRARGADTCG WRGVGPASRN SGLHNITFRY
DNCTTYLNPG GKHAIADAQN ITISQYACHD QVAVTILWSP GALGIEFLKG FRVILEELKS
EGRQCQQLIL KDPKQLNSSF RRTGMESQPF LNMKFETDYF VKIVPFPSIK NESNYHPFFF
RTRACDLLLQ PDNLACKPFW KPRNLNISQH GSDMHVSFDH APQNFGFRGF HVLYKLKHEG
PFRRRTCRQD QNTETTSCLL QNVSPGDYII ELVDDSNTTR KAAQYVVKSV QSPWAGPIRA
VAITVPLVVI SAFATLFTVM CRKKQQENIY SHLDEESPES STYAAALPRD RLRPQPKVFL
CYSNKDGQNH MNVVQCFAYF LQDFCGCEVA LDLWEDFSLC REGQREWAIQ KIHESQFIIV
VCSKGMKYFV DKKNFRHKGG SRGEAQGEFF LVAVAAIAEK LRQAKQSSSA ALRKFIAVYF
DYSCEGDVPC SLDLSTKYKL MDHLPELCAH LHSGEQEVLG QHPGHSSRRN YFRSKSGRSL
YVAICNMHQF IDEEPDWFEK QFIPFQHPPV RYQEPVLEKF DSGLVLNDVI SKPGPESDFC
RKVEACVLGA AGPADSYSYL ESQHVGLDQD TEAQPSCDSA PALQPLLHAV KAGSPSEMPR
DSGIYDSSVP SSELSLPLME GLSPDQIETS SLTESVSSSS GLGEEDPPTL PSKLLASGVS
REHGCHSHTD ELQALAPL
