PGFRB_RAT
ID PGFRB_RAT Reviewed; 1097 AA.
AC Q05030; Q8R406; Q925F7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Platelet-derived growth factor receptor beta;
DE Short=PDGF-R-beta;
DE Short=PDGFR-beta;
DE EC=2.7.10.1;
DE AltName: Full=Beta platelet-derived growth factor receptor;
DE AltName: Full=Beta-type platelet-derived growth factor receptor;
DE AltName: Full=CD140 antigen-like family member B;
DE AltName: Full=Platelet-derived growth factor receptor 1;
DE Short=PDGFR-1;
DE AltName: CD_antigen=CD140b;
DE Flags: Precursor;
GN Name=Pdgfrb; Synonyms=Pdgfr, Pdgfr1;
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].
RC STRAIN=Sprague-Dawley;
RA Wang Y., Culty M.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-533.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8318539; DOI=10.1016/0167-4781(93)90127-y;
RA Herren B., Weyer K.A., Rouge M., Loetscher P., Pech M.;
RT "Conservation in sequence and affinity of human and rodent PDGF ligands and
RT receptors.";
RL Biochim. Biophys. Acta 1173:294-302(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 528-1090.
RC STRAIN=Wistar;
RX PubMed=11346654; DOI=10.1074/jbc.m102995200;
RA Okuyama H., Shimahara Y., Kawada N., Seki S., Kristensen D.B.,
RA Yoshizato K., Uyama N., Yamaoka Y.;
RT "Regulation of cell growth by redox-mediated extracellular proteolysis of
RT platelet-derived growth factor receptor beta.";
RL J. Biol. Chem. 276:28274-28280(2001).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA
CC and PDGFB, and plays an essential role in the regulation of embryonic
CC development, cell proliferation, survival, differentiation, chemotaxis
CC and migration. Plays an essential role in blood vessel development by
CC promoting proliferation, migration and recruitment of pericytes and
CC smooth muscle cells to endothelial cells. Plays a role in the migration
CC of vascular smooth muscle cells and the formation of neointima at
CC vascular injury sites. Required for normal development of the
CC cardiovascular system. Required for normal recruitment of pericytes
CC (mesangial cells) in the kidney glomerulus, and for normal formation of
CC a branched network of capillaries in kidney glomeruli. Promotes
CC rearrangement of the actin cytoskeleton and the formation of membrane
CC ruffles. Binding of its cognate ligands - homodimeric PDGFB,
CC heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to
CC the activation of several signaling cascades; the response depends on
CC the nature of the bound ligand and is modulated by the formation of
CC heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1,
CC PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the
CC production of the cellular signaling molecules diacylglycerol and
CC inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the
CC activation of protein kinase C. Phosphorylation of PIK3R1, the
CC regulatory subunit of phosphatidylinositol 3-kinase, leads to the
CC activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or
CC of the C-terminus of PTPN11, creates a binding site for GRB2, resulting
CC in the activation of HRAS, RAF1 and down-stream MAP kinases, including
CC MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation
CC of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and
CC STAM. Receptor signaling is down-regulated by protein phosphatases that
CC dephosphorylate the receptor and its down-stream effectors, and by
CC rapid internalization of the activated receptor (By similarity).
CC {ECO:0000250}.
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. Binding of PDGFB and/or PDGFD leads to dimerization
CC and activation by autophosphorylation on tyrosine residues (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with homodimeric PDGFB and PDGFD, and with
CC heterodimers formed by PDGFA and PDGFB. May also interact with
CC homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction
CC with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or
CC homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA
CC homodimers and heterodimers with PDGFRB are observed. Interacts with
CC SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB.
CC Interacts (tyrosine phosphorylated) with PIK3R1 and RASA1. Interacts
CC (tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated)
CC with SRC and SRC family kinases. Interacts (tyrosine phosphorylated)
CC with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated)
CC with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by
CC SHC1. Interacts (via C-terminus) with SLC9A3R1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}.
CC Lysosome lumen {ECO:0000250}. Note=After ligand binding, the
CC autophosphorylated receptor is ubiquitinated and internalized, leading
CC to its degradation. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. After autophosphorylation, the receptor is
CC polyubiquitinated, leading to its degradation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
CC Autophosphorylation occurs in trans, i.e. one subunit of the dimeric
CC receptor phosphorylates tyrosine residues on the other subunit.
CC Phosphorylation at Tyr-578, and to a lesser degree, Tyr-580 is
CC important for interaction with SRC. Phosphorylation at Tyr-715 is
CC important for interaction with GRB2. Phosphorylation at Tyr-739 and
CC Tyr-750 is important for interaction with PIK3R1. Phosphorylation at
CC Tyr-750 is important for interaction with NCK1. Phosphorylation at Tyr-
CC 770 and Tyr-856 is important for interaction with RASA1/GAP.
CC Phosphorylation at Tyr-856 is important for efficient phosphorylation
CC of PLCG1 and PTPN11, resulting in increased phosphorylation of AKT1,
CC MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and STAM, and in increased
CC cell proliferation. Phosphorylation at Tyr-1008 is important for
CC interaction with PTPN11. Phosphorylation at Tyr-1008 and Tyr-1020 is
CC important for interaction with PLCG1. Dephosphorylated by PTPRJ at Tyr-
CC 750, Tyr-856, Tyr-1008 and Tyr-1020. Dephosphorylated by PTPN2 at Tyr-
CC 578 and Tyr-1020 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AY090783; AAM09098.1; -; mRNA.
DR EMBL; Z14119; CAA78489.1; -; mRNA.
DR EMBL; AF359356; AAK43716.1; -; mRNA.
DR PIR; S33766; S33766.
DR RefSeq; NP_113713.1; NM_031525.1.
DR RefSeq; XP_006254851.1; XM_006254789.3.
DR AlphaFoldDB; Q05030; -.
DR SMR; Q05030; -.
DR BioGRID; 246767; 2.
DR IntAct; Q05030; 2.
DR MINT; Q05030; -.
DR STRING; 10116.ENSRNOP00000060534; -.
DR BindingDB; Q05030; -.
DR ChEMBL; CHEMBL4125; -.
DR GlyGen; Q05030; 11 sites.
DR iPTMnet; Q05030; -.
DR PhosphoSitePlus; Q05030; -.
DR jPOST; Q05030; -.
DR PaxDb; Q05030; -.
DR PRIDE; Q05030; -.
DR ABCD; Q05030; 1 sequenced antibody.
DR GeneID; 24629; -.
DR KEGG; rno:24629; -.
DR UCSC; RGD:3285; rat.
DR CTD; 5159; -.
DR RGD; 3285; Pdgfrb.
DR VEuPathDB; HostDB:ENSRNOG00000018461; -.
DR eggNOG; KOG0200; Eukaryota.
DR HOGENOM; CLU_000288_49_0_1; -.
DR InParanoid; Q05030; -.
DR OMA; PQPGCQE; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; Q05030; -.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-186797; Signaling by PDGF.
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:Q05030; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000018461; Expressed in ovary and 18 other tissues.
DR Genevisible; Q05030; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:RGD.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:RGD.
DR GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; ISS:UniProtKB.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD.
DR GO; GO:0005017; F:platelet-derived growth factor receptor activity; IDA:RGD.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; TAS:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:RGD.
DR GO; GO:0030325; P:adrenal gland development; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0035909; P:aorta morphogenesis; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0060981; P:cell migration involved in coronary angiogenesis; ISS:UniProtKB.
DR GO; GO:0035441; P:cell migration involved in vasculogenesis; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:RGD.
DR GO; GO:0048568; P:embryonic organ development; ISO:RGD.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IMP:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; IEP:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0060437; P:lung growth; IMP:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0072278; P:metanephric comma-shaped body morphogenesis; IEP:UniProtKB.
DR GO; GO:0072277; P:metanephric glomerular capillary formation; ISS:UniProtKB.
DR GO; GO:0072262; P:metanephric glomerular mesangial cell proliferation involved in metanephros development; ISS:UniProtKB.
DR GO; GO:0072223; P:metanephric glomerular mesangium development; ISO:RGD.
DR GO; GO:0072275; P:metanephric glomerulus morphogenesis; IEP:UniProtKB.
DR GO; GO:0035789; P:metanephric mesenchymal cell migration; IDA:UniProtKB.
DR GO; GO:0072075; P:metanephric mesenchyme development; IEP:UniProtKB.
DR GO; GO:0072284; P:metanephric S-shaped body morphogenesis; IEP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0006807; P:nitrogen compound metabolic process; ISO:RGD.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:RGD.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:RGD.
DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; 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:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; ISS:UniProtKB.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:UniProtKB.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:RGD.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0106096; P:response to ceramide; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0034405; P:response to fluid shear stress; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0033993; P:response to lipid; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0097178; P:ruffle assembly; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0071670; P:smooth muscle cell chemotaxis; ISO:RGD.
DR GO; GO:0048745; P:smooth muscle tissue development; ISO:RGD.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
DR Gene3D; 2.60.40.10; -; 5.
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; IPR027288; PGFRB.
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 InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500948; Beta-PDGF_receptor; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
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.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Chemotaxis; Cytoplasmic vesicle;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Kinase; Lysosome; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1097
FT /note="Platelet-derived growth factor receptor beta"
FT /id="PRO_0000016759"
FT TOPO_DOM 32..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..1097
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..119
FT /note="Ig-like C2-type 1"
FT DOMAIN 128..209
FT /note="Ig-like C2-type 2"
FT DOMAIN 213..308
FT /note="Ig-like C2-type 3"
FT DOMAIN 415..523
FT /note="Ig-like C2-type 4"
FT DOMAIN 599..961
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1016..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 825
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 605..613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 561
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 578
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 580
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 685
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000250|UniProtKB:P05622"
FT MOD_RES 715
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 739
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 750
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 762
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 770
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 774
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 777
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 856
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 933
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000250|UniProtKB:P05622"
FT MOD_RES 969
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000250|UniProtKB:P05622"
FT MOD_RES 1008
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 1020
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 148..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 234..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 435..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1097 AA; 122828 MW; 5E6540FA0C5CF22B CRC64;
MGLPEVMPAS VLRGQLLLFV LLLLGPQISQ GLVITPPGPE FVLNISSTFV LTCSSSAPVM
WEQMSQVPWQ EAAMNQDGTF SSVLTLTNVT GGDTGEYFCV YNNSLGPELS ERKRIYIFVP
DPTMGFLPMD SEDLFIFVTD VTETTIPCRV TDPQLEVTLH EKKVDIPLHV PYDHQRGFIG
TFEDKTYICK TTIGDREVDS DTYYVYSLQV SSINVSVNAV QTVVRQGESI TIRCIVMGND
VVNFQWTYPR MKSGRLVEPV TDYLFGVPSR IGSILHIPTA ELSDSGTYTC NVSVSVNDHG
DEKAINVTVI ENGYVRLLET LEDVQIAELH RSRTLQVVFE AYPTPSVLWF KDNRTLGDSS
AGELVLSTRN VSETRYVSEL TLVRVKVSEA GYYTMRAFHA DDQVQLSFKL QVNVPVRVLE
LSESHPANGE QILRCRGRGM PQPNVTWSTC RDLKRCPRKL SPTPLGNSSK EESQLETNVT
FWEEDQEYEV VSTLRLRHVD QPLSVRCMLQ NSMGRDSQEV TVVPHSLPFK VVVISAILAL
VVLTVISLII LIMLWQRKPR YEIRWKVIES VSSDGHEYIY VDPVQLPYDS TWELPRDQLV
LGRTLGSGAF GQVVEATAHG LSHSQATMKV AVKMLKSTAR SSEKQALMSE LKIMSHLGPH
LNVVNLLGAC TKGGPIYIIT EYCRYGDLVD YLHRNKHTFL QRHSNKHCPP STELYSNALP
VGLSLPSHLN LTGESDGGYM DMSKDESVDY VPMLDMKGHI KYADIESSSY MAPYDNYVPS
APERTYRATL INDSPVLSYT DLVGFSYQVA NGMEFLASKN CVHRDLAARN VLICEGKLVK
ICDFGLARDI MRDSNYISKG STFLPLKWMA PESIFNSLYT TLSDVWSFGI LLWEIFTLGG
TPYPELPMND QFYNAIKRGY RMAQPAHASD EIYEIMQKCW EEKFETRPPF SQLVLLLERL
LGEGYKKKYQ QVDEEFLRSD HPAILRSQAR LPGLHSLRSP LDTSSVLYTA VQPNETDNDY
IIPLPDPKPD AADEGLLEGS PSLASSTLNE VNTSSTISCD SPLELQEEPQ AEPEAQLEQP
QDSGCPGPLA EAEDSFL
