ID   FGRL1_CHICK             Reviewed;         487 AA.
AC   Q7T2H2;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Fibroblast growth factor receptor-like 1;
DE   Flags: Precursor;
GN   Name=FGFRL1;
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], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP   WITH HEPARIN AND FGF2.
RC   TISSUE=Cartilage;
RX   PubMed=12813049; DOI=10.1074/jbc.m300281200;
RA   Trueb B., Zhuang L., Taeschler S., Wiedemann M.;
RT   "Characterization of FGFRL1, a novel fibroblast growth factor (FGF)
RT   receptor preferentially expressed in skeletal tissues.";
RL   J. Biol. Chem. 278:33857-33865(2003).
CC   -!- FUNCTION: Has a negative effect on cell proliferation.
CC       {ECO:0000269|PubMed:12813049}.
CC   -!- SUBUNIT: Interacts with heparin and FGF2.
CC       {ECO:0000269|PubMed:12813049}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in cartilaginous structures.
CC       {ECO:0000269|PubMed:12813049}.
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DR   EMBL; AJ535114; CAD59380.1; -; mRNA.
DR   RefSeq; NP_989787.1; NM_204456.1.
DR   AlphaFoldDB; Q7T2H2; -.
DR   SMR; Q7T2H2; -.
DR   STRING; 9031.ENSGALP00000025315; -.
DR   PaxDb; Q7T2H2; -.
DR   Ensembl; ENSGALT00000047764; ENSGALP00000057609; ENSGALG00000037525.
DR   GeneID; 395107; -.
DR   KEGG; gga:395107; -.
DR   CTD; 53834; -.
DR   VEuPathDB; HostDB:geneid_395107; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   GeneTree; ENSGT00940000156736; -.
DR   HOGENOM; CLU_038830_1_0_1; -.
DR   InParanoid; Q7T2H2; -.
DR   OMA; WAQPRFT; -.
DR   OrthoDB; 612548at2759; -.
DR   PhylomeDB; Q7T2H2; -.
DR   Reactome; R-GGA-5658623; FGFRL1 modulation of FGFR1 signaling.
DR   PRO; PR:Q7T2H2; -.
DR   Proteomes; UP000000539; Chromosome 4.
DR   Bgee; ENSGALG00000037525; Expressed in liver and 11 other tissues.
DR   ExpressionAtlas; Q7T2H2; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0017134; F:fibroblast growth factor binding; IBA:GO_Central.
DR   GO; GO:0005007; F:fibroblast growth factor receptor activity; IBA:GO_Central.
DR   GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF07679; I-set; 3.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Heparin-binding;
KW   Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..487
FT                   /note="Fibroblast growth factor receptor-like 1"
FT                   /id="PRO_0000021249"
FT   TOPO_DOM        19..371
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        393..487
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          23..109
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          141..231
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          240..348
FT                   /note="Ig-like C2-type 3"
FT   REGION          115..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        45..93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        166..215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        262..332
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   487 AA;  54099 MW;  FFD0132AD917FF94 CRC64;
     MGLQLALLLA GIVALSDSAR GPPRIADKVI HRQSVRLGRT IKLLCPVEGD PPPLTMWMKD
     GRTIHSGWTR FRILQQGLKI KEVESEDAGT YICKATNGFG STNVNYTLIV IDDTSSGKNS
     QTPEGSNGEY EDHSGKQWAQ PRFTQPAKMR RRVIARPVGS SIRLKCVASG NPRPDITWLK
     DNKPLMPHEI GENKKKKWTL NLKNLKPEDS GKYTCRVFNK VGEINATYKV EVIQRTRSKP
     ILTGTHPVNT TVDYGGTTSF QCKVRSDVKP VIQWLKRVEY GTESKYNSTI DVGGQKFVVL
     PTGEVWSRPD GSYLNKLMIT RAKEEDAGMY ICLGANTMGY SFRSAFLTVL PDPKPPSAPV
     PPSSVSSLPW PVIIGIPAGA VFIFGTILLW LCQTKKKPCS PPAAAPVHRP QPRDRICVSQ
     VPDKDCISSI NYEEYVAQQQ HLLSQGPALA PAMASKMYPK IYTDIHTHTH SHVEGKVHQH
     QHIQYQC