FGFR1_MOUSE
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 03-AUG-2022, entry version 225.
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 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=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, 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};
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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_001079908.2. [P16092-6]
DR RefSeq; NP_001073378.1; NM_001079909.2. [P16092-2]
DR RefSeq; NP_034336.2; NM_010206.3. [P16092-1]
DR RefSeq; XP_006509073.1; XM_006509010.2.
DR RefSeq; XP_006509075.1; XM_006509012.1.
DR RefSeq; XP_011240423.1; XM_011242121.1.
DR PDB; 2CKN; NMR; -; A=25-119.
DR PDBsum; 2CKN; -.
DR AlphaFoldDB; P16092; -.
DR BMRB; P16092; -.
DR SMR; P16092; -.
DR BioGRID; 199656; 42.
DR DIP; DIP-6033N; -.
DR IntAct; P16092; 11.
DR MINT; P16092; -.
DR STRING; 10090.ENSMUSP00000081041; -.
DR BindingDB; P16092; -.
DR ChEMBL; CHEMBL3960; -.
DR GlyConnect; 2314; 5 N-Linked glycans (2 sites).
DR GlyGen; P16092; 8 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; P16092; -.
DR PhosphoSitePlus; P16092; -.
DR CPTAC; non-CPTAC-4034; -.
DR jPOST; P16092; -.
DR MaxQB; P16092; -.
DR PaxDb; P16092; -.
DR PeptideAtlas; P16092; -.
DR PRIDE; 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 Antibodypedia; 11015; 2522 antibodies from 48 providers.
DR DNASU; 14182; -.
DR Ensembl; ENSMUST00000084027; ENSMUSP00000081041; ENSMUSG00000031565. [P16092-1]
DR Ensembl; ENSMUST00000117179; ENSMUSP00000113909; ENSMUSG00000031565. [P16092-6]
DR Ensembl; ENSMUST00000119398; ENSMUSP00000113855; ENSMUSG00000031565. [P16092-2]
DR Ensembl; ENSMUST00000167764; ENSMUSP00000131343; ENSMUSG00000031565. [P16092-5]
DR Ensembl; ENSMUST00000178276; ENSMUSP00000137515; ENSMUSG00000031565. [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 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 PhylomeDB; P16092; -.
DR TreeFam; TF316307; -.
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 74 CRISPR screens.
DR ChiTaRS; Fgfr1; mouse.
DR EvolutionaryTrace; P16092; -.
DR PRO; PR:P16092; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P16092; protein.
DR Bgee; ENSMUSG00000031565; Expressed in molar tooth and 335 other tissues.
DR ExpressionAtlas; P16092; baseline and differential.
DR Genevisible; P16092; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IPI:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
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:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0090722; F:receptor-receptor interaction; ISO:MGI.
DR GO; GO:0042169; F:SH2 domain binding; IPI:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA: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:0060038; P:cardiac muscle cell proliferation; IGI:MGI.
DR GO; GO:0048469; P:cell maturation; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0071529; P:cementum mineralization; IDA:MGI.
DR GO; GO:0021954; P:central nervous system neuron development; ISO:MGI.
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:MGI.
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:0010463; P:mesenchymal cell proliferation; IMP:MGI.
DR GO; GO:0030901; P:midbrain development; IMP:MGI.
DR GO; GO:0042474; P:middle ear morphogenesis; IMP:MGI.
DR GO; GO:0021837; P:motogenic signaling involved in postnatal olfactory bulb interneuron migration; ISO: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:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IGI:MGI.
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; ISS:UniProtKB.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
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:2000546; P:positive regulation of endothelial cell chemotaxis to fibroblast growth factor; ISO:MGI.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:MGI.
DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
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:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0050678; P:regulation of epithelial cell 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:0051930; P:regulation of sensory perception of pain; ISO:MGI.
DR GO; GO:0072091; P:regulation of stem cell proliferation; ISO:MGI.
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:0048863; P:stem cell differentiation; IGI:MGI.
DR GO; GO:0019827; P:stem cell population maintenance; ISO:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA: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; cd05098; PTKc_FGFR1; 1.
DR Gene3D; 2.60.40.10; -; 3.
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.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
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; SSF48726; 3.
DR SUPFAM; SSF56112; SSF56112; 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.
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 123..137
FT /note="Acidic 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
