ID FGFR1_MOUSE Reviewed; 822 AA. AC P16092; E9Q2P4; Q01736; Q60830; Q61562; Q80T10; Q8CFK8; Q9QZM7; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 2. DT 02-SEP-2026, entry version 243. DE RecName: Full=Fibroblast growth factor receptor 1; DE Short=FGFR-1; DE Short=bFGF-R-1; DE EC=2.7.10.1 {ECO:0000250|UniProtKB:P11362}; DE AltName: Full=Basic fibroblast growth factor receptor 1; DE AltName: Full=MFR; DE AltName: Full=Proto-oncogene c-Fgr; DE AltName: CD_antigen=CD331; DE Flags: Precursor; GN Name=Fgfr1; Synonyms=Flg; 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). RC TISSUE=Brain; RX PubMed=1689490; DOI=10.1073/pnas.87.4.1596; RA Reid H.H., Wilks A.F., Bernard O.; RT "Two forms of the basic fibroblast growth factor receptor-like mRNA are RT expressed in the developing mouse brain."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1596-1600(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6). RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=2161096; RA Safran A., Avivi A., Orr-Urtereger A., Neufeld G., Lonai P., Givol D., RA Yarden Y.; RT "The murine flg gene encodes a receptor for fibroblast growth factor."; RL Oncogene 5:635-643(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING. RX PubMed=1708247; DOI=10.1016/0006-291x(91)90885-b; RA Kouhara H., Kasayama S., Saito H., Matsumoto K., Sato B.; RT "Expression cDNA cloning of fibroblast growth factor (FGF) receptor in RT mouse breast cancer cells: a variant form in FGF-responsive transformed RT cells."; RL Biochem. Biophys. Res. Commun. 176:31-37(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=2161540; DOI=10.1073/pnas.87.11.4378; RA Mansukhani A., Moscatelli D., Talarico D., Levytska V., Basilico C.; RT "A murine fibroblast growth factor (FGF) receptor expressed in CHO cells is RT activated by basic FGF and Kaposi FGF."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4378-4382(1990). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING. RC STRAIN=Swiss Webster; TISSUE=Embryonic heart; RX PubMed=7897669; DOI=10.1006/jmcc.1994.1164; RA Jin Y., Pasumarthi K.B., Bock M.E., Lytras A., Kardami E., Cattini P.A.; RT "Cloning and expression of fibroblast growth factor receptor-1 isoforms in RT the mouse heart: evidence for isoform switching during heart development."; RL J. Mol. Cell. Cardiol. 26:1449-1459(1994). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION, FUNCTION AS RP FGF7 RECEPTOR AND IN ACTIVATION OF SIGNALING PATHWAYS, INTERACTION WITH RP FGF1; FGF2; FGF7 AND FGF10, GLYCOSYLATION, TISSUE SPECIFICITY, AND RP ALTERNATIVE SPLICING. RC STRAIN=BALB/cJ; RX PubMed=10821861; DOI=10.1074/jbc.275.21.16091; RA Beer H.-D., Vindevoghel L., Gait M.J., Revest J.-M., Duan D.R., Mason I., RA Dickson C., Werner S.; RT "Fibroblast growth factor (FGF) receptor 1-IIIb is a naturally occurring RT functional receptor for FGFs that is preferentially expressed in the skin RT and the brain."; RL J. Biol. Chem. 275:16091-16097(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC STRAIN=FVB/N; TISSUE=Mammary tumor; 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 [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-15, AND ALTERNATIVE SPLICING. RX PubMed=7802632; DOI=10.1006/bbrc.1994.2773; RA Harada T., Saito H., Kouhara H., Kurebayashi S., Kasayama S., Terakawa N., RA Kishimoto T., Sato B.; RT "Murine fibroblast growth factor receptor 1 gene generates multiple RT messenger RNAs containing two open reading frames via alternative RT splicing."; RL Biochem. Biophys. Res. Commun. 205:1057-1063(1994). RN [11] RP INTERACTION WITH FGF1; FGF2; FGF4; FGF5; FGF6, AND FUNCTION IN CELL RP PROLIFERATION. RX PubMed=1309590; DOI=10.1128/mcb.12.1.240-247.1992; RA Ornitz D.M., Yayon A., Flanagan J.G., Svahn C.M., Levi E., Leder P.; RT "Heparin is required for cell-free binding of basic fibroblast growth RT factor to a soluble receptor and for mitogenesis in whole cells."; RL Mol. Cell. Biol. 12:240-247(1992). RN [12] RP DISRUPTION PHENOTYPE, AND FUNCTION DURING EMBRYONIC DEVELOPMENT. RX PubMed=8001822; DOI=10.1101/gad.8.24.3032; RA Yamaguchi T.P., Harpal K., Henkemeyer M., Rossant J.; RT "fgfr-1 is required for embryonic growth and mesodermal patterning during RT mouse gastrulation."; RL Genes Dev. 8:3032-3044(1994). RN [13] RP DISRUPTION PHENOTYPE, AND FUNCTION DURING EMBRYONIC DEVELOPMENT. RX PubMed=8001823; DOI=10.1101/gad.8.24.3045; RA Deng C.X., Wynshaw-Boris A., Shen M.M., Daugherty C., Ornitz D.M., RA Leder P.; RT "Murine FGFR-1 is required for early postimplantation growth and axial RT organization."; RL Genes Dev. 8:3045-3057(1994). RN [14] RP SUBUNIT, AND LIGAND SPECIFICITY. RX PubMed=8663044; DOI=10.1074/jbc.271.25.15292; RA Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A., Coulier F., RA Gao G., Goldfarb M.; RT "Receptor specificity of the fibroblast growth factor family."; RL J. Biol. Chem. 271:15292-15297(1996). RN [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10896947; DOI=10.1074/jbc.m910132199; RA Chikazu D., Hakeda Y., Ogata N., Nemoto K., Itabashi A., Takato T., RA Kumegawa M., Nakamura K., Kawaguchi H.; RT "Fibroblast growth factor (FGF)-2 directly stimulates mature osteoclast RT function through activation of FGF receptor 1 and p42/p44 MAP kinase."; RL J. Biol. Chem. 275:31444-31450(2000). RN [16] RP INTERACTION WITH SHB. RX PubMed=12181353; DOI=10.1091/mbc.e02-02-0103; RA Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M., RA Claesson-Welsh L.; RT "The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and regulates RT the Ras/MEK/MAPK pathway via FRS2 phosphorylation in endothelial cells."; RL Mol. Biol. Cell 13:2881-2893(2002). RN [17] RP SUBCELLULAR LOCATION. RX PubMed=15383174; DOI=10.1089/dna.2004.23.538; RA Reilly J.F., Mizukoshi E., Maher P.A.; RT "Ligand dependent and independent internalization and nuclear translocation RT of fibroblast growth factor (FGF) receptor 1."; RL DNA Cell Biol. 23:538-548(2004). RN [18] RP INTERACTION WITH FLRT1; FLRT2 AND FLRT3. RX PubMed=16872596; DOI=10.1016/j.ydbio.2006.04.004; RA Haines B.P., Wheldon L.M., Summerbell D., Heath J.K., Rigby P.W.J.; RT "Regulated expression of FLRT genes implies a functional role in the RT regulation of FGF signalling during mouse development."; RL Dev. Biol. 297:14-25(2006). RN [19] RP FUNCTION, AND INTERACTION WITH KL AND FGF23. RX PubMed=17086194; DOI=10.1038/nature05315; RA Urakawa I., Yamazaki Y., Shimada T., Iijima K., Hasegawa H., Okawa K., RA Fujita T., Fukumoto S., Yamashita T.; RT "Klotho converts canonical FGF receptor into a specific receptor for RT FGF23."; RL Nature 444:770-774(2006). RN [20] RP INTERACTION WITH SOX2 AND SOX3. RX PubMed=17728342; DOI=10.1242/dev.007906; RA Rizzoti K., Lovell-Badge R.; RT "SOX3 activity during pharyngeal segmentation is required for craniofacial RT morphogenesis."; RL Development 134:3437-3448(2007). RN [21] RP INTERACTION WITH KLB. RX PubMed=17452648; DOI=10.1073/pnas.0701600104; RA Ogawa Y., Kurosu H., Yamamoto M., Nandi A., Rosenblatt K.P., Goetz R., RA Eliseenkova A.V., Mohammadi M., Kuro-o M.; RT "BetaKlotho is required for metabolic activity of fibroblast growth factor RT 21."; RL Proc. Natl. Acad. Sci. U.S.A. 104:7432-7437(2007). RN [22] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [24] RP STRUCTURE BY NMR OF 25-119. RX PubMed=16731982; DOI=10.1110/ps.062207906; RA Kiselyov V.V., Bock E., Berezin V., Poulsen F.M.; RT "NMR structure of the first Ig module of mouse FGFR1."; RL Protein Sci. 15:1512-1515(2006). CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor CC for fibroblast growth factors and plays an essential role in the CC regulation of embryonic development, cell proliferation, CC differentiation and migration. Required for normal mesoderm patterning CC and correct axial organization during embryonic development, normal CC skeletogenesis and normal development of the gonadotropin-releasing CC hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and CC SHB. Ligand binding leads to the activation of several signaling CC cascades. Activation of PLCG1 leads to the production of the cellular CC signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. CC Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and CC SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the CC MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. CC Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the CC nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the CC regulation of transcription. FGFR1 signaling is down-regulated by CC IL17RD/SEF, and by FGFR1 ubiquitination, internalization and CC degradation (By similarity). {ECO:0000250|UniProtKB:P11362, CC ECO:0000269|PubMed:10821861, ECO:0000269|PubMed:10896947, CC ECO:0000269|PubMed:1309590, ECO:0000269|PubMed:17086194, CC ECO:0000269|PubMed:8001822, ECO:0000269|PubMed:8001823}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; CC -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence CC of bound ligand. Ligand binding leads to dimerization and activation by CC sequential autophosphorylation on tyrosine residues (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Monomer. Homodimer after ligand binding. Interacts CC predominantly with FGF1 and FGF2, but can also interact with FGF3, CC FGF4, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in vitro) CC (PubMed:10821861, PubMed:1309590, PubMed:17086194). Ligand specificity CC is determined by tissue-specific expression of isoforms, and CC differences in the third Ig-like domain are crucial for ligand CC specificity. Affinity for fibroblast growth factors (FGFs) is increased CC by heparan sulfate glycosaminoglycans that function as coreceptors. CC Likewise, KLB increases the affinity for FGF19, FGF21 and FGF23. CC Interacts (phosphorylated on Tyr-766) with PLCG1 (via SH2 domains). CC Interacts with FRS2. Interacts with RPS6KA1. Interacts (via C-terminus) CC with NEDD4 (via WW3 domain). Interacts with KL (PubMed:17086194). CC Interacts with SHB (via SH2 domain) (PubMed:12181353). Interacts with CC GRB10 (By similarity). Interacts with ANOS1; this interaction does not CC interfere with FGF2-binding to FGFR1, but prevents binding of heparin- CC bound FGF2 (By similarity). Interacts with SOX2 and SOX3 CC (PubMed:17728342). Interacts with FLRT1, FLRT2 and FLRT3 CC (PubMed:16872596). Found in a ternary complex with FGF1 and ITGAV:ITGB3 CC (By similarity). {ECO:0000250|UniProtKB:P11362, CC ECO:0000269|PubMed:10821861, ECO:0000269|PubMed:12181353, CC ECO:0000269|PubMed:1309590, ECO:0000269|PubMed:16872596, CC ECO:0000269|PubMed:17086194, ECO:0000269|PubMed:17452648, CC ECO:0000269|PubMed:17728342, ECO:0000269|PubMed:8663044}. CC -!- INTERACTION: CC P16092; O35082: Kl; NbExp=2; IntAct=EBI-7953898, EBI-1570828; CC P16092; Q99N32: Klb; NbExp=3; IntAct=EBI-7953898, EBI-15633521; CC P16092; P13596: Ncam1; Xeno; NbExp=2; IntAct=EBI-7953898, EBI-916499; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle. Note=After CC ligand binding, both receptor and ligand are rapidly internalized. Can CC translocate to the nucleus after internalization, or by translocation CC from the endoplasmic reticulum or Golgi apparatus to the cytosol, and CC from there to the nucleus. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I CC membrane protein. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane; Single-pass type I CC membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=FGFR1-IIIc, Long; CC IsoId=P16092-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=P16092-2; Sequence=VSP_002962; CC Name=3; Synonyms=Variant; CC IsoId=P16092-3; Sequence=VSP_002961, VSP_002963; CC Name=4; CC IsoId=P16092-4; Sequence=VSP_002962, VSP_002963; CC Name=5; Synonyms=FGFR1-IIIb; CC IsoId=P16092-5; Sequence=VSP_002962, VSP_002963, VSP_041919, CC VSP_041920, VSP_041921, VSP_041922; CC Name=6; CC IsoId=P16092-6; Sequence=VSP_002963; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10821861}. CC -!- DOMAIN: The second and third Ig-like domains directly interact with CC fibroblast growth factors (FGF) and heparan sulfate proteoglycans. CC Isoforms lacking the first Ig-like domain have higher affinity for CC fibroblast growth factors (FGF) and heparan sulfate proteoglycans than CC isoforms with all three Ig-like domains (By similarity). {ECO:0000250}. CC -!- PTM: Autophosphorylated. Binding of FGF family members together with CC heparan sulfate proteoglycan or heparin promotes receptor dimerization CC and autophosphorylation on tyrosine residues. Autophosphorylation CC occurs in trans between the two FGFR molecules present in the dimer and CC proceeds in a highly ordered manner. Initial autophosphorylation at CC Tyr-653 increases the kinase activity by a factor of 50 to 100. After CC this, Tyr-583 becomes phosphorylated, followed by phosphorylation of CC Tyr-463, Tyr-766, Tyr-583 and Tyr-585. In a third stage, Tyr-654 is CC autophosphorylated, resulting in a further tenfold increase of kinase CC activity. Phosphotyrosine residues provide docking sites for CC interacting proteins and so are crucial for FGFR1 function and its CC regulation (By similarity). {ECO:0000250|UniProtKB:P11362}. CC -!- PTM: Ubiquitinated. FGFR1 is rapidly ubiquitinated by NEDD4 after CC autophosphorylation, leading to internalization and lysosomal CC degradation. CBL is recruited to activated FGFR1 via FRS2 and GRB2, and CC mediates ubiquitination and subsequent degradation of FGFR1 (By CC similarity). {ECO:0000250|UniProtKB:P11362}. CC -!- PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan chains CC undergo further maturation to an Endo H-resistant form in the Golgi CC apparatus. {ECO:0000269|PubMed:10821861, ECO:0000269|PubMed:19349973}. CC -!- DISRUPTION PHENOTYPE: Embryonic lethality around gastrulation, due to CC growth defects during early embryonic development and aberrant mesoderm CC patterning. {ECO:0000269|PubMed:8001822, ECO:0000269|PubMed:8001823}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Fibroblast growth factor receptor subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB32845.1; Type=Miscellaneous discrepancy; Note=Proposes two coding sequences for the same mRNA.; 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; M28998; AAA37290.1; -; mRNA. DR EMBL; X51893; CAA36175.1; -; mRNA. DR EMBL; M65053; AAA37620.1; -; mRNA. DR EMBL; M33760; AAA37622.1; -; mRNA. DR EMBL; U23445; AAC52183.1; -; mRNA. DR EMBL; AF176552; AAF05312.1; -; mRNA. DR EMBL; AK028354; BAC25899.1; -; mRNA. DR EMBL; S74765; AAB32845.1; ALT_SEQ; mRNA. DR EMBL; AC160526; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC033447; AAH33447.1; -; mRNA. DR CCDS; CCDS40304.1; -. [P16092-2] DR CCDS; CCDS52526.1; -. [P16092-1] DR CCDS; CCDS57614.1; -. [P16092-6] DR PIR; A34849; TVMSFG. DR PIR; B42057; B42057. DR PIR; I49293; I49293. DR PIR; JH0393; JH0393. DR RefSeq; NP_001073377.1; NM_001079908.3. [P16092-6] DR RefSeq; NP_001073378.1; NM_001079909.3. [P16092-2] DR RefSeq; NP_034336.2; NM_010206.4. [P16092-1] DR PDB; 2CKN; NMR; -; A=25-119. DR AlphaFoldDB; P16092; -. DR BMRB; P16092; -. DR SMR; P16092; -. DR BioGRID; 199656; 44. DR CORUM; P16092; -. DR DIP; DIP-6033N; -. DR FunCoup; P16092; 2060. DR IntAct; P16092; 11. DR MINT; P16092; -. DR STRING; 10090.ENSMUSP00000081041; -. DR BindingDB; P16092; -. DR ChEMBL; CHEMBL3960; -. DR GlyConnect; P16092; 5 N-Linked glycans (2 sites). DR GlyCosmos; P16092; 8 sites, 5 glycans. DR GlyGen; P16092; 10 sites, 8 N-linked glycans (5 sites), 1 O-linked glycan (1 site). DR iPTMnet; P16092; -. DR PhosphoSitePlus; P16092; -. DR CPTAC; non-CPTAC-4034; -. DR jPOST; P16092; -. DR PaxDb; 10090-ENSMUSP00000081041; -. DR PeptideAtlas; P16092; -. DR ProteomicsDB; 271577; -. [P16092-1] DR ProteomicsDB; 271578; -. [P16092-2] DR ProteomicsDB; 271579; -. [P16092-3] DR ProteomicsDB; 271580; -. [P16092-4] DR ProteomicsDB; 271581; -. [P16092-5] DR ProteomicsDB; 271582; -. [P16092-6] DR Pumba; P16092; -. DR Antibodypedia; 11015; 2592 antibodies from 50 providers. DR DNASU; 14182; -. DR Ensembl; ENSMUST00000084027.13; ENSMUSP00000081041.6; ENSMUSG00000031565.20. [P16092-1] DR Ensembl; ENSMUST00000117179.9; ENSMUSP00000113909.3; ENSMUSG00000031565.20. [P16092-6] DR Ensembl; ENSMUST00000119398.10; ENSMUSP00000113855.3; ENSMUSG00000031565.20. [P16092-2] DR Ensembl; ENSMUST00000167764.2; ENSMUSP00000131343.2; ENSMUSG00000031565.20. [P16092-5] DR GeneID; 14182; -. DR KEGG; mmu:14182; -. DR UCSC; uc009lfy.2; mouse. [P16092-1] DR UCSC; uc009lga.2; mouse. [P16092-2] DR UCSC; uc033jet.1; mouse. [P16092-4] DR AGR; MGI:95522; -. DR CTD; 2260; -. DR MGI; MGI:95522; Fgfr1. DR VEuPathDB; HostDB:ENSMUSG00000031565; -. DR eggNOG; KOG0200; Eukaryota. DR GeneTree; ENSGT00940000155860; -. DR HOGENOM; CLU_000288_74_1_1; -. DR InParanoid; P16092; -. DR OrthoDB; 18071at9989; -. DR PhylomeDB; P16092; -. DR BRENDA; 2.7.10.1; 3474. DR Reactome; R-MMU-109704; PI3K Cascade. DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling. DR Reactome; R-MMU-190370; FGFR1b ligand binding and activation. DR Reactome; R-MMU-190373; FGFR1c ligand binding and activation. DR Reactome; R-MMU-190374; FGFR1c and Klotho ligand binding and activation. DR Reactome; R-MMU-445144; Signal transduction by L1. DR Reactome; R-MMU-5654219; Phospholipase C-mediated cascade: FGFR1. DR Reactome; R-MMU-5654687; Downstream signaling of activated FGFR1. DR Reactome; R-MMU-5654688; SHC-mediated cascade:FGFR1. DR Reactome; R-MMU-5654689; PI-3K cascade:FGFR1. DR Reactome; R-MMU-5654693; FRS-mediated FGFR1 signaling. DR Reactome; R-MMU-5654726; Negative regulation of FGFR1 signaling. DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade. DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR BioGRID-ORCS; 14182; 6 hits in 79 CRISPR screens. DR EvolutionaryTrace; P16092; -. DR PRO; PR:P16092; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; P16092; protein. DR Bgee; ENSMUSG00000031565; Expressed in molar tooth and 338 other cell types or tissues. DR ExpressionAtlas; P16092; baseline and differential. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005634; C:nucleus; ISO:GO_Central. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:GO_Central. DR GO; GO:0005886; C:plasma membrane; IPI:MGI. DR GO; GO:0098794; C:postsynapse; IDA:SynGO. DR GO; GO:0043235; C:signaling receptor complex; ISO:MGI. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:GO_Central. DR GO; GO:0017134; F:fibroblast growth factor binding; IDA:MGI. DR GO; GO:0005007; F:fibroblast growth factor receptor activity; IDA:MGI. DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; ISO:GO_Central. DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:GO_Central. DR GO; GO:0044877; F:protein-containing complex binding; ISO:GO_Central. DR GO; GO:0090722; F:receptor-receptor interaction; ISO:GO_Central. DR GO; GO:0042169; F:SH2 domain binding; IPI:MGI. DR GO; GO:0005102; F:signaling receptor binding; ISO:GO_Central. DR GO; GO:0001525; P:angiogenesis; IGI:MGI. DR GO; GO:0060117; P:auditory receptor cell development; IMP:MGI. DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI. DR GO; GO:0007420; P:brain development; IMP:MGI. DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI. DR GO; GO:0055074; P:calcium ion homeostasis; IGI:MGI. DR GO; GO:0048469; P:cell maturation; IMP:MGI. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISO:GO_Central. DR GO; GO:0071529; P:cementum mineralization; IDA:MGI. DR GO; GO:0021954; P:central nervous system neuron development; ISO:GO_Central. DR GO; GO:0002062; P:chondrocyte differentiation; IGI:MGI. DR GO; GO:0071344; P:diphosphate metabolic process; IDA:MGI. DR GO; GO:0043583; P:ear development; IMP:MGI. DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI. DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:GO_Central. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI. DR GO; GO:0035607; P:fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development; IMP:UniProtKB. DR GO; GO:0010467; P:gene expression; IDA:MGI. DR GO; GO:0048699; P:generation of neurons; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI. DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0060484; P:lung-associated mesenchyme development; IGI:MGI. DR GO; GO:0048762; P:mesenchymal cell differentiation; IGI:MGI. DR GO; GO:0030901; P:midbrain development; IMP:MGI. DR GO; GO:0042474; P:middle ear morphogenesis; IMP:MGI. DR GO; GO:0090272; P:negative regulation of fibroblast growth factor production; IGI:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0031175; P:neuron projection development; ISO:GO_Central. DR GO; GO:0021769; P:orbitofrontal cortex development; IMP:UniProtKB. DR GO; GO:0001759; P:organ induction; IMP:MGI. DR GO; GO:0042473; P:outer ear morphogenesis; IMP:MGI. DR GO; GO:0048339; P:paraxial mesoderm development; IGI:MGI. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:GO_Central. DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:GO_Central. DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IGI:MGI. DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB. DR GO; GO:0045597; P:positive regulation of cell differentiation; IBA:GO_Central. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI. DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISO:GO_Central. DR GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:GO_Central. DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; ISO:GO_Central. DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:GO_Central. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:GO_Central. DR GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; IGI:MGI. DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI. DR GO; GO:1903465; P:positive regulation of mitotic cell cycle DNA replication; IDA:MGI. DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; IGI:MGI. DR GO; GO:2000830; P:positive regulation of parathyroid hormone secretion; IGI:MGI. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:GO_Central. DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:GO_Central. DR GO; GO:0021827; P:postnatal olfactory bulb interneuron migration; ISO:GO_Central. DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB. DR GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; IDA:MGI. DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI. DR GO; GO:2001239; P:regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:0048378; P:regulation of lateral mesodermal cell fate specification; IGI:MGI. DR GO; GO:0010966; P:regulation of phosphate transport; IGI:MGI. DR GO; GO:0051174; P:regulation of phosphorus metabolic process; IGI:MGI. DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO. DR GO; GO:0072091; P:regulation of stem cell proliferation; ISO:GO_Central. DR GO; GO:1904383; P:response to sodium phosphate; IDA:MGI. DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:MGI. DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI. DR GO; GO:0019827; P:stem cell population maintenance; ISO:GO_Central. DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; ISO:GO_Central. DR GO; GO:0001657; P:ureteric bud development; IGI:MGI. DR GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; TAS:DFLAT. DR GO; GO:0021847; P:ventricular zone neuroblast division; IMP:UniProtKB. DR GO; GO:0070640; P:vitamin D3 metabolic process; IGI:MGI. DR CDD; cd04973; IgI_1_FGFR; 1. DR CDD; cd05857; IgI_2_FGFR; 1. DR CDD; cd05098; PTKc_FGFR1; 1. DR FunFam; 1.10.510.10:FF:000007; Fibroblast growth factor receptor; 1. DR FunFam; 2.60.40.10:FF:000016; Fibroblast growth factor receptor; 1. DR FunFam; 2.60.40.10:FF:000020; Fibroblast growth factor receptor; 1. DR FunFam; 2.60.40.10:FF:000408; Fibroblast growth factor receptor; 1. DR FunFam; 3.30.200.20:FF:000011; Fibroblast growth factor receptor; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR028174; FGF_rcpt_1. DR InterPro; IPR016248; FGF_rcpt_fam. 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 InterPro; IPR013151; Immunoglobulin_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR050122; RTK. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR PANTHER; PTHR24416:SF131; FIBROBLAST GROWTH FACTOR RECEPTOR 1; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF07679; I-set; 2. DR Pfam; PF00047; ig; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PIRSF; PIRSF000628; FGFR; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 3. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PDBsum; 2CKN; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Heparin-binding; KW Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; Nucleus; KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase; KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase; KW Ubl conjugation. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..822 FT /note="Fibroblast growth factor receptor 1" FT /id="PRO_0000016781" FT TOPO_DOM 22..376 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 377..397 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 398..822 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 25..119 FT /note="Ig-like C2-type 1" FT DOMAIN 158..246 FT /note="Ig-like C2-type 2" FT DOMAIN 255..357 FT /note="Ig-like C2-type 3" FT DOMAIN 478..767 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 120..162 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 160..177 FT /note="Heparin-binding" FT REGION 782..822 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 125..135 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 136..145 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 782..792 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 623 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 484..490 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 514 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 562..564 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 568 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 627 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 641 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT SITE 766 FT /note="Mediates interaction with PLCG1 and SHB" FT /evidence="ECO:0000250" FT MOD_RES 463 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P11362" FT MOD_RES 583 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P11362" FT MOD_RES 585 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P11362" FT MOD_RES 653 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P11362" FT MOD_RES 654 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P11362" FT MOD_RES 730 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P11362" FT MOD_RES 766 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P11362" FT CARBOHYD 77 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 117 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 227 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 240 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 264 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 296 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 317 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 330 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 55..101 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 178..230 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 277..341 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 30 FT /note="Q -> QGSSSWPLWVAAA (in isoform 3)" FT /evidence="ECO:0000303|PubMed:1708247" FT /id="VSP_002961" FT VAR_SEQ 31..119 FT /note="Missing (in isoform 2, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:10821861, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:2161540, ECO:0000303|PubMed:7897669" FT /id="VSP_002962" FT VAR_SEQ 148..149 FT /note="Missing (in isoform 3, isoform 4, isoform 5 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:10821861, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1708247, FT ECO:0000303|PubMed:2161096" FT /id="VSP_002963" FT VAR_SEQ 313..323 FT /note="TAGVNTTDKEM -> HSGINSSDA (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10821861" FT /id="VSP_041919" FT VAR_SEQ 327..336 FT /note="HLRNVSFEDA -> TLFNVTEAQS (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10821861" FT /id="VSP_041920" FT VAR_SEQ 340..352 FT /note="TCLAGNSIGLSHH -> VCKVSNYIGEANQ (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10821861" FT /id="VSP_041921" FT VAR_SEQ 359..360 FT /note="LE -> TRPVAK (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10821861" FT /id="VSP_041922" FT CONFLICT 229 FT /note="T -> S (in Ref. 4; AAA37622)" FT /evidence="ECO:0000305" FT CONFLICT 256..258 FT /note="ILQ -> HPS (in Ref. 1; AAA37290 and 3; AAA37620)" FT /evidence="ECO:0000305" FT CONFLICT 265 FT /note="K -> E (in Ref. 5; AAC52183)" FT /evidence="ECO:0000305" FT CONFLICT 270 FT /note="G -> A (in Ref. 4; AAA37622)" FT /evidence="ECO:0000305" FT CONFLICT 387 FT /note="I -> M (in Ref. 3; AAA37620)" FT /evidence="ECO:0000305" FT CONFLICT 440 FT /note="G -> A (in Ref. 2; CAA36175)" FT /evidence="ECO:0000305" FT CONFLICT 457 FT /note="L -> P (in Ref. 5; AAC52183)" FT /evidence="ECO:0000305" FT CONFLICT 508 FT /note="V -> L (in Ref. 3; AAA37620)" FT /evidence="ECO:0000305" FT CONFLICT 544 FT /note="I -> M (in Ref. 4; AAA37622)" FT /evidence="ECO:0000305" FT CONFLICT 549 FT /note="G -> E (in Ref. 6; AAF05312)" FT /evidence="ECO:0000305" FT CONFLICT 753 FT /note="D -> V (in Ref. 6; AAF05312)" FT /evidence="ECO:0000305" FT CONFLICT 756 FT /note="R -> H (in Ref. 1; AAA37290)" FT /evidence="ECO:0000305" FT CONFLICT 763 FT /note="N -> S (in Ref. 5; AAC52183)" FT /evidence="ECO:0000305" FT CONFLICT 765 FT /note="E -> D (in Ref. 4; AAA37622)" FT /evidence="ECO:0000305" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:2CKN" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:2CKN" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:2CKN" FT STRAND 63..68 FT /evidence="ECO:0007829|PDB:2CKN" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:2CKN" FT STRAND 83..90 FT /evidence="ECO:0007829|PDB:2CKN" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:2CKN" FT STRAND 96..105 FT /evidence="ECO:0007829|PDB:2CKN" FT STRAND 108..118 FT /evidence="ECO:0007829|PDB:2CKN" SQ SEQUENCE 822 AA; 91981 MW; D5A4695FA680926B CRC64; MWGWKCLLFW AVLVTATLCT ARPAPTLPEQ AQPWGVPVEV ESLLVHPGDL LQLRCRLRDD VQSINWLRDG VQLVESNRTR ITGEEVEVRD SIPADSGLYA CVTSSPSGSD TTYFSVNVSD ALPSSEDDDD DDDSSSEEKE TDNTKPNRRP VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS HHSAWLTVLE ALEERPAVMT SPLYLEIIIY CTGAFLISCM LGSVIIYKMK SGTKKSDFHS QMAVHKLAKS IPLRRQVTVS ADSSASMNSG VLLVRPSRLS SSGTPMLAGV SEYELPEDPR WELPRDRLVL GKPLGEGCFG QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS EMEMMKMIGK HKNIINLLGA CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN PEEQLSSKDL VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH IDYYKKTTNG RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP YPGVPVEELF KLLKEGHRMD KPSNCTNELY MMMRDCWHAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS IPLDQYSPSF PDTRSSTCSS GEDSVFSHEP LPEEPCLPRH PTQLANSGLK RR //