MET_RAT
ID MET_RAT Reviewed; 1382 AA.
AC P97523; P97579; Q63119; Q63964;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Hepatocyte growth factor receptor;
DE Short=HGF receptor;
DE EC=2.7.10.1;
DE AltName: Full=HGF/SF receptor;
DE AltName: Full=Proto-oncogene c-Met;
DE AltName: Full=Scatter factor receptor;
DE Short=SF receptor;
DE AltName: Full=Tyrosine-protein kinase Met;
DE Flags: Precursor;
GN Name=Met;
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; TISSUE=Liver;
RX PubMed=9271668; DOI=10.1007/s003359900533;
RA Wallenius V.R., Rawet H., Skrtic S., Helou K., Qiu Y., Levan G., Ekberg S.,
RA Carlsson B., Isaksson O.G.P., Nakamura T., Jansson J.-O.;
RT "Chromosomal localization of rat hepatocyte growth factor (Hgf) and HGF
RT receptor (Met) and characterization of HGF receptor cDNA.";
RL Mamm. Genome 8:661-667(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8853431; DOI=10.1152/ajprenal.1996.271.3.f679;
RA Liu Y., Tolbert E.M., Sun A.M., Dworkin L.D.;
RT "Primary structure of rat HGF receptor and induced expression in glomerular
RT mesangial cells.";
RL Am. J. Physiol. 271:F679-F688(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 364-495.
RC STRAIN=Sprague-Dawley; TISSUE=Gastric mucosa;
RX PubMed=8166728; DOI=10.1006/bbrc.1994.1481;
RA Tsujii M., Kawano S., Tsuji S., Ito T., Hayashi N., Horimoto M., Mita E.,
RA Nagano K., Masuda E., Hayashi N., Fusamoto H., Kamada T.;
RT "Increased expression of c-met messenger RNA following acute gastric injury
RT in rats.";
RL Biochem. Biophys. Res. Commun. 200:536-541(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 851-1002.
RC TISSUE=Intestine;
RX PubMed=7628535; DOI=10.1006/excr.1995.1220;
RA Pepper M.S., Soriano J.V., Menoud P.-A., Sappino A.-P., Orci L.,
RA Montesano R.;
RT "Modulation of hepatocyte growth factor and c-met in the rat mammary gland
RT during pregnancy, lactation, and involution.";
RL Exp. Cell Res. 219:204-210(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1129-1267.
RA Kikuchi Y.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor tyrosine kinase that transduces signals from the
CC extracellular matrix into the cytoplasm by binding to hepatocyte growth
CC factor/HGF ligand. Regulates many physiological processes including
CC proliferation, scattering, morphogenesis and survival. Ligand binding
CC at the cell surface induces autophosphorylation of MET on its
CC intracellular domain that provides docking sites for downstream
CC signaling molecules. Following activation by ligand, interacts with the
CC PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1.
CC Recruitment of these downstream effectors by MET leads to the
CC activation of several signaling cascades including the RAS-ERK, PI3
CC kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with
CC the morphogenetic effects while PI3K/AKT coordinates prosurvival
CC effects. During embryonic development, MET signaling plays a role in
CC gastrulation, development and migration of muscles and neuronal
CC precursors, angiogenesis and kidney formation. In adults, participates
CC in wound healing as well as organ regeneration and tissue remodeling.
CC Promotes also differentiation and proliferation of hematopoietic cells
CC (By similarity). {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: In its inactive state, the C-terminal tail
CC interacts with the catalytic domain and inhibits the kinase activity.
CC Upon ligand binding, the C-terminal tail is displaced and becomes
CC phosphorylated, thus increasing the kinase activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer made of an alpha chain (50 kDa) and a beta chain
CC (145 kDa) which are disulfide linked. Binds PLXNB1. Interacts when
CC phosphorylated with downstream effectors including STAT3, PIK3R1, SRC,
CC PCLG1, GRB2 and GAB1. Interacts with SPSB1, SPSB2 and SPSB4. Interacts
CC with INPP5D/SHIP1. When phosphorylated at Tyr-1357, interacts with
CC INPPL1/SHIP2. Interacts with RANBP9 and RANBP10, as well as SPSB1,
CC SPSB2, SPSB3 and SPSB4. SPSB1 binding occurs in the presence and in the
CC absence of HGF, however HGF treatment has a positive effect on this
CC interaction. Interacts with MUC20; prevents interaction with GRB2 and
CC suppresses hepatocyte growth factor-induced cell proliferation.
CC Interacts with GRB10. Interacts with PTPN1 and PTPN2. Interacts with
CC HSP90AA1 and HSP90AB1; the interaction suppresses MET kinase activity.
CC {ECO:0000250|UniProtKB:P08581, ECO:0000250|UniProtKB:P16056}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in lung, liver and
CC kidney, also expressed in stomach, intestine, spleen, testis and brain.
CC Not expressed in heart or muscle.
CC -!- DEVELOPMENTAL STAGE: Expression is down-regulated during pregnancy and
CC is virtually undetectable during lactation. Expression progressively
CC increases post-lactation.
CC -!- INDUCTION: By interleukin-6 and acute acid-induced gastric injury.
CC Inhibited by prolactin.
CC -!- DOMAIN: The kinase domain is involved in SPSB1 binding. {ECO:0000250}.
CC -!- DOMAIN: The beta-propeller Sema domain mediates binding to HGF.
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated in response to ligand binding on Tyr-1235 and
CC Tyr-1236 in the kinase domain leading to further phosphorylation of
CC Tyr-1350 and Tyr-1357 in the C-terminal multifunctional docking site.
CC Dephosphorylated by PTPRJ at Tyr-1350 and Tyr-1366. Dephosphorylated by
CC PTPN1 and PTPN2 (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor
CC stability and activity through proteasomal degradation (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X96786; CAA65582.1; -; mRNA.
DR EMBL; U65007; AAB19189.1; -; mRNA.
DR EMBL; S69881; AAB30575.1; -; mRNA.
DR EMBL; Z46374; CAA86508.1; -; mRNA.
DR EMBL; AB012281; BAA28171.1; -; Genomic_DNA.
DR PIR; PC2131; PC2131.
DR RefSeq; NP_113705.1; NM_031517.2.
DR AlphaFoldDB; P97523; -.
DR SMR; P97523; -.
DR STRING; 10116.ENSRNOP00000009662; -.
DR GlyGen; P97523; 10 sites.
DR iPTMnet; P97523; -.
DR PhosphoSitePlus; P97523; -.
DR PaxDb; P97523; -.
DR PRIDE; P97523; -.
DR GeneID; 24553; -.
DR KEGG; rno:24553; -.
DR UCSC; RGD:3082; rat.
DR CTD; 4233; -.
DR RGD; 3082; Met.
DR eggNOG; KOG1095; Eukaryota.
DR eggNOG; KOG3610; Eukaryota.
DR InParanoid; P97523; -.
DR OrthoDB; 408584at2759; -.
DR PhylomeDB; P97523; -.
DR BRENDA; 2.7.10.1; 5301.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-6806942; MET Receptor Activation.
DR Reactome; R-RNO-6807004; Negative regulation of MET activity.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-8851805; MET activates RAS signaling.
DR Reactome; R-RNO-8851907; MET activates PI3K/AKT signaling.
DR Reactome; R-RNO-8865999; MET activates PTPN11.
DR Reactome; R-RNO-8874081; MET activates PTK2 signaling.
DR Reactome; R-RNO-8875513; MET interacts with TNS proteins.
DR Reactome; R-RNO-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-RNO-8875656; MET receptor recycling.
DR Reactome; R-RNO-8875791; MET activates STAT3.
DR Reactome; R-RNO-9734091; Drug-mediated inhibition of MET activation.
DR PRO; PR:P97523; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009925; C:basal plasma membrane; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; NAS:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0036126; C:sperm flagellum; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008013; F:beta-catenin binding; IPI:RGD.
DR GO; GO:0005008; F:hepatocyte growth factor receptor activity; IMP:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IDA:RGD.
DR GO; GO:0043274; F:phospholipase binding; IPI:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0017154; F:semaphorin receptor activity; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISO:RGD.
DR GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IEP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0071241; P:cellular response to inorganic substance; IEP:RGD.
DR GO; GO:0071354; P:cellular response to interleukin-6; IEP:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IEP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0001886; P:endothelial cell morphogenesis; ISO:RGD.
DR GO; GO:0061436; P:establishment of skin barrier; ISO:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0014812; P:muscle cell migration; ISO:RGD.
DR GO; GO:0007517; P:muscle organ development; ISO:RGD.
DR GO; GO:0051450; P:myoblast proliferation; ISO:RGD.
DR GO; GO:0014902; P:myotube differentiation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; ISO:RGD.
DR GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; ISO:RGD.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:RGD.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:RGD.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0071635; P:negative regulation of transforming growth factor beta production; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IDA:RGD.
DR GO; GO:0014003; P:oligodendrocyte development; IEP:RGD.
DR GO; GO:0031016; P:pancreas development; IEP:RGD.
DR GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR GO; GO:0001890; P:placenta development; ISO:RGD.
DR GO; GO:0050918; P:positive chemotaxis; ISS:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISO:RGD.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:RGD.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:RGD.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; ISO:RGD.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0032675; P:regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0010447; P:response to acidic pH; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016244; Tyr_kinase_HGF/MSP_rcpt.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PTHR22625; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 3.
DR PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00429; IPT; 4.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF81296; SSF81296; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1382
FT /note="Hepatocyte growth factor receptor"
FT /id="PRO_0000024442"
FT TOPO_DOM 25..935
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 936..956
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 957..1379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..516
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 564..656
FT /note="IPT/TIG 1"
FT DOMAIN 658..740
FT /note="IPT/TIG 2"
FT DOMAIN 743..837
FT /note="IPT/TIG 3"
FT DOMAIN 1079..1346
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1213..1382
FT /note="Interaction with RANBP9"
FT /evidence="ECO:0000250"
FT REGION 1321..1360
FT /note="Interaction with MUC20"
FT /evidence="ECO:0000250"
FT ACT_SITE 1205
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 1085..1093
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 308..309
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 978
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 1004
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 1231
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 1235
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 1236
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 1290
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 1350
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 1357
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT MOD_RES 1366
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08581"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 786
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 98..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 133..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 173..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 299..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 386..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 521..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 527..562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 530..546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 542..552
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 53
FT /note="H -> Q (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="P -> H (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="P -> G (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="R -> A (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="Y -> H (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
FT CONFLICT 490..495
FT /note="EVIVEH -> GAAGIR (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="P -> A (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="R -> G (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="V -> F (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
FT CONFLICT 808
FT /note="R -> Q (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
FT CONFLICT 890..893
FT /note="SEAL -> TASV (in Ref. 4; CAA86508)"
FT /evidence="ECO:0000305"
FT CONFLICT 907
FT /note="Missing (in Ref. 4; CAA86508)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="K -> E (in Ref. 4; CAA86508)"
FT /evidence="ECO:0000305"
FT CONFLICT 934
FT /note="A -> R (in Ref. 4; CAA86508)"
FT /evidence="ECO:0000305"
FT CONFLICT 1028
FT /note="L -> P (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
FT CONFLICT 1068
FT /note="P -> Q (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
FT CONFLICT 1197
FT /note="V -> A (in Ref. 2 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 1331
FT /note="V -> F (in Ref. 2; AAB19189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1382 AA; 153941 MW; 66B8F2C88FE34427 CRC64;
MKAPTALAPG ILLLLLTLAQ RSHGECKEAL VKSEMNVNMK YQLPNFTAET PIHNVVLPGH
HIYLGATNYI YVLNDKDLQK VSEFKTGPVV EHPDCFPCQD CSSKANVSGG VWKDNVNMAL
LVDTYYDDQL ISCGSVNRGT CQRHVLPPDN AADIQSEVHC MFSPLAEEES GQCPDCVVSA
LGAKVLLSEK DRFINFFVGN TINSSYPPDY SLHSISVRRL KETQDGFKFL TDQSYIDVLP
EFRDSYPIKY IHAFESNHFI YFLTVQKETL DAQTFHTRII RFCSVDSGLH SYMEMPLECI
LTEKRRKRST REEVFNILQA AYVSKPGANL AKQIGASPYD DILYGVFAQS KPDSAEPMNR
SAVCAFPIKY VNDFFNKIVN KNNVRCLQHF YGPNHEHCFN RTLLRNSSGC EVRSDEYRTE
FTTALQRVDL FMGRLNHVLL TSISTFIKGD LTIANLGTSE GRFMQVVLSR TAHFTPHVNF
LLDSYPVSPE VIVEHPSNQN GYTLVVTGKK ITKIPLNGLG CGHFQSCSQC LSPPYFIQCG
WCHNRCVHSN ECPSGTWTQE ICLPAVYKVF PTSAPLEGGT MLTICGWDFG FKKNNKFDLR
KTKVLLGNES CTLTLSESTT NTLKCTVGPA MSEHFNVSVI VSNSRETTQY SAFSYVDPVI
TSISPRYGPH AGGTLLTLTG KYLNSGNSRH ISIGGKTCTL KSVSDSILEC YTPGHTVSAE
FPVKLKIDLA DRVTSSFSYR EDPVVSEIHP TKSFISGGST ITGIGKNLNS VSTPKLVIEV
HDVGVNYTVA CQHRSSSEII CCTTPSLRQL DLQLPLKTKA FFLLDGILSK HFDLTYVHDP
MFKPFEKPVM ISMGNENVVE IKGDDIDPEA VKGEVLKVGN KSCENLHWHS EALLCTVPSD
LLKLNGGELN IEWKQAVSST VLGKVIVQPD QNFAGLIIGA VSISVVVLLV SGLFLWLRKR
KHKDLGSELV RYDARVHTPH LDRLVSARSV SPTTEMVSNE SVDYRATFPE DQFPNSSQNG
ACRQVQYLLT DLSPILTSGD SDISSPLLQN TVHIDLSALN PELVQAVPHV VIGPSSLIVH
FNEVIGRGHF GCVYHGTLLD SDGKKIHCAV KSLNRITDIE EVSQFLTEGI IMKDFSHPNV
LSLLGICLRS EGSPLVVLPY MKHGDLRNFI RNETHNPTVK DLIGFGLQVA KGMKYLVSKK
FVHRDLAARN CMLDEKFTVK VADFGLARDM YDKEYYSVHN KTGAKLPVKW MALESLQTQK
FTTKSDVWSF GVLLWELMTR GAPPYPDVNT FDITIYLLQG RRLLQPEYCP DALYEVMLKC
WHPKAEMRPS VSELVSRISS IFSTFIGEHY VHVNATYVNV KCVAPYPSLL PSQDNIDGEA
NT
