FGFR1_RAT
ID FGFR1_RAT Reviewed; 822 AA.
AC Q04589;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 184.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8382532; DOI=10.1016/0167-4781(93)90266-g;
RA Yazaki N., Hiroko F., Mitsuhiro O., Toshisuke K., Nobuyuki I.;
RT "The structure and expression of the FGF receptor-1 mRNA isoforms in rat
RT tissues.";
RL Biochim. Biophys. Acta 1172:37-42(1993).
RN [2]
RP INTERACTION WITH RPS6KA1, AND SUBCELLULAR LOCATION.
RX PubMed=15117958; DOI=10.1074/jbc.m311144200;
RA Hu Y., Fang X., Dunham S.M., Prada C., Stachowiak E.K., Stachowiak M.K.;
RT "90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast
RT growth factor receptor 1 (FGFR1): role in FGFR1 signaling.";
RL J. Biol. Chem. 279:29325-29335(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=17992255; DOI=10.1172/jci32409;
RA Ben-Dov I.Z., Galitzer H., Lavi-Moshayoff V., Goetz R., Kuro-o M.,
RA Mohammadi M., Sirkis R., Naveh-Many T., Silver J.;
RT "The parathyroid is a target organ for FGF23 in rats.";
RL J. Clin. Invest. 117:4003-4008(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000250|UniProtKB:P16092}.
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:0000250|UniProtKB:P11362, ECO:0000255|PROSITE-
CC 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|UniProtKB:P11362}.
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
CC vitro). Ligand specificity is determined by tissue-specific expression
CC of isoforms, and differences in the third Ig-like domain are crucial
CC for ligand specificity. Affinity for fibroblast growth factors (FGFs)
CC is increased by heparan sulfate glycosaminoglycans that function as
CC coreceptors. Likewise, KLB increases the affinity for FGF19, FGF21 and
CC FGF23. Interacts (phosphorylated on Tyr-766) with PLCG1 (via SH2
CC domains). Interacts with FRS2. Interacts (via C-terminus) with NEDD4
CC (via WW3 domain). Interacts with RPS6KA1 (PubMed:15117958). Interacts
CC with KL (By similarity). Interacts with SHB (via SH2 domain) and GRB10.
CC Interacts with ANOS1; this interaction does not interfere with FGF2-
CC binding to FGFR1, but prevents binding of heparin-bound FGF2. Interacts
CC with SOX2 and SOX3 (By similarity). Interacts with FLRT1, FLRT2 and
CC FLRT3. Found in a ternary complex with FGF1 and ITGAV:ITGB3 (By
CC similarity). {ECO:0000250|UniProtKB:P11362,
CC ECO:0000250|UniProtKB:P16092, ECO:0000269|PubMed:15117958}.
CC -!- INTERACTION:
CC Q04589; P19327: Htr1a; NbExp=5; IntAct=EBI-2480918, EBI-6570156;
CC Q04589; P10686: Plcg1; NbExp=2; IntAct=EBI-2480918, EBI-520788;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15117958};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15117958}.
CC Nucleus {ECO:0000269|PubMed:15117958}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:15117958}. Cytoplasmic vesicle {ECO:0000250}.
CC Note=After ligand binding, both receptor and ligand are rapidly
CC internalized. Can translocate to the nucleus after internalization, or
CC by translocation from the endoplasmic reticulum or Golgi apparatus to
CC the cytosol, and from there to the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the parathyroid.
CC {ECO:0000269|PubMed:17992255}.
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 (By similarity). {ECO:0000250|UniProtKB:P11362}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fibroblast growth factor receptor subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; D12498; BAA02059.1; -; mRNA.
DR PIR; S29840; S29840.
DR RefSeq; NP_077060.1; NM_024146.1.
DR AlphaFoldDB; Q04589; -.
DR BMRB; Q04589; -.
DR SMR; Q04589; -.
DR BioGRID; 249399; 4.
DR CORUM; Q04589; -.
DR IntAct; Q04589; 3.
DR MINT; Q04589; -.
DR STRING; 10116.ENSRNOP00000036885; -.
DR ChEMBL; CHEMBL4523276; -.
DR GlyGen; Q04589; 8 sites.
DR iPTMnet; Q04589; -.
DR jPOST; Q04589; -.
DR PaxDb; Q04589; -.
DR PRIDE; Q04589; -.
DR GeneID; 79114; -.
DR KEGG; rno:79114; -.
DR UCSC; RGD:620713; rat.
DR CTD; 2260; -.
DR RGD; 620713; Fgfr1.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; Q04589; -.
DR PhylomeDB; Q04589; -.
DR BRENDA; 2.7.10.1; 5301.
DR Reactome; R-RNO-109704; PI3K Cascade.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-190370; FGFR1b ligand binding and activation.
DR Reactome; R-RNO-190373; FGFR1c ligand binding and activation.
DR Reactome; R-RNO-190374; FGFR1c and Klotho ligand binding and activation.
DR Reactome; R-RNO-445144; Signal transduction by L1.
DR Reactome; R-RNO-5654219; Phospholipase C-mediated cascade: FGFR1.
DR Reactome; R-RNO-5654687; Downstream signaling of activated FGFR1.
DR Reactome; R-RNO-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-RNO-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-RNO-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-RNO-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR PRO; PR:Q04589; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
DR GO; GO:0005007; F:fibroblast growth factor receptor activity; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0090722; F:receptor-receptor interaction; ISO:RGD.
DR GO; GO:0042169; F:SH2 domain binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0060117; P:auditory receptor cell development; ISO:RGD.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; ISO:RGD.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:RGD.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0071420; P:cellular response to histamine; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0071529; P:cementum mineralization; ISO:RGD.
DR GO; GO:0021954; P:central nervous system neuron development; IMP:RGD.
DR GO; GO:0002062; P:chondrocyte differentiation; ISO:RGD.
DR GO; GO:0071344; P:diphosphate metabolic process; ISO:RGD.
DR GO; GO:0043583; P:ear development; ISO:RGD.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0035607; P:fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0048699; P:generation of neurons; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0060484; P:lung-associated mesenchyme development; ISO:RGD.
DR GO; GO:0048762; P:mesenchymal cell differentiation; ISO:RGD.
DR GO; GO:0030901; P:midbrain development; ISO:RGD.
DR GO; GO:0042474; P:middle ear morphogenesis; ISO:RGD.
DR GO; GO:0021837; P:motogenic signaling involved in postnatal olfactory bulb interneuron migration; IMP:RGD.
DR GO; GO:0090272; P:negative regulation of fibroblast growth factor production; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IDA:RGD.
DR GO; GO:0021769; P:orbitofrontal cortex development; ISO:RGD.
DR GO; GO:0001759; P:organ induction; ISO:RGD.
DR GO; GO:0042473; P:outer ear morphogenesis; ISO:RGD.
DR GO; GO:0048339; P:paraxial mesoderm development; ISO:RGD.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:RGD.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISO:RGD.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000546; P:positive regulation of endothelial cell chemotaxis to fibroblast growth factor; ISO:RGD.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:RGD.
DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; IMP:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:RGD.
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:RGD.
DR GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:RGD.
DR GO; GO:1903465; P:positive regulation of mitotic cell cycle DNA replication; ISO:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR GO; GO:2000830; P:positive regulation of parathyroid hormone secretion; ISO:RGD.
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:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:RGD.
DR GO; GO:2001239; P:regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0048378; P:regulation of lateral mesodermal cell fate specification; ISO:RGD.
DR GO; GO:0010966; P:regulation of phosphate transport; ISO:RGD.
DR GO; GO:0051174; P:regulation of phosphorus metabolic process; ISO:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IMP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:1904383; P:response to sodium phosphate; ISO:RGD.
DR GO; GO:0007435; P:salivary gland morphogenesis; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0001657; P:ureteric bud development; ISO:RGD.
DR GO; GO:0021847; P:ventricular zone neuroblast division; ISO:RGD.
DR GO; GO:0070640; P:vitamin D3 metabolic process; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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 ATP-binding; Cell membrane; Cytoplasm; Cytoplasmic vesicle; Disulfide bond;
KW Glycoprotein; Heparin-binding; Immunoglobulin domain; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..822
FT /note="Fibroblast growth factor receptor 1"
FT /id="PRO_0000016782"
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 770..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 COMPBIAS 770..794
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:0000255"
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"
SQ SEQUENCE 822 AA; 91825 MW; E59D924D0A1DE5C5 CRC64;
MWGWRGLLFW AVLVTATLCT ARPAPTLPEQ AQPWGVPVEV ESLLVHPGDL LQLRCRLRDD
VQSINWLRDG VQLAESNRTR ITGEEVEVRD SIPADSGLYA CVTNSPSGSD TTYFSVNVSD
ALPSSEDDDD DDDSSSEEKE TDNTKPNRRP VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS
SGTPSPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN
HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI
GPDNLPYDQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS HHSAWLTVLE
ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIIYKMK 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 NPGVPVEELF KLLKEGHRMD
KPSNCTNELY MMMRDCWNAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS MPLDQDSPSF
PDTRSSTCSS GEDSVFSHEP FPEEPCLPRH PTQLANGGLN RR
