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   24-JAN-2024, entry version 193.
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       Interacts with tensin TNS3 (By similarity). Interacts (when
CC       phosphorylated) with tensin TNS4 (via SH2 domain); the interaction
CC       increases MET protein stability by inhibiting MET endocytosis and
CC       subsequent lysosomal degradation (By similarity).
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|UniProtKB:P08581}.
CC   -!- PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor
CC       stability and activity through proteasomal degradation (By similarity).
CC       {ECO:0000250|UniProtKB:P08581}.
CC   -!- PTM: O-mannosylation of IPT/TIG domains by TMEM260 is required for
CC       protein maturation. O-mannosylated residues are composed of single
CC       mannose glycans that are not elongated or modified.
CC       {ECO:0000250|UniProtKB:P08581}.
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.ENSRNOP00000070486; -.
DR   GlyCosmos; P97523; 10 sites, No reported glycans.
DR   GlyGen; P97523; 10 sites.
DR   iPTMnet; P97523; -.
DR   PhosphoSitePlus; P97523; -.
DR   PaxDb; 10116-ENSRNOP00000009662; -.
DR   GeneID; 24553; -.
DR   KEGG; rno:24553; -.
DR   UCSC; RGD:3082; rat.
DR   AGR; RGD:3082; -.
DR   CTD; 4233; -.
DR   RGD; 3082; Met.
DR   eggNOG; KOG1095; Eukaryota.
DR   eggNOG; KOG3610; Eukaryota.
DR   InParanoid; P97523; -.
DR   OrthoDB; 1614410at2759; -.
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: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:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0043025; C:neuronal cell body; 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:0140677; F:molecular function activator activity; 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:0030534; P:adult behavior; ISO:RGD.
DR   GO; GO:0007420; P:brain development; ISO: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:0051649; P:establishment of localization in cell; 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:1904659; P:glucose transmembrane transport; 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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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: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:0045944; P:positive regulation of transcription by RNA polymerase II; IMP: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: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   CDD; cd00603; IPT_PCSR; 1.
DR   CDD; cd01180; IPT_plexin_repeat1; 1.
DR   CDD; cd01179; IPT_plexin_repeat2; 1.
DR   CDD; cd05058; PTKc_Met_Ron; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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; IPR002165; Plexin_repeat.
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:SF61; HEPATOCYTE GROWTH FACTOR RECEPTOR; 1.
DR   PANTHER; PTHR22625; PLEXIN; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01437; PSI; 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; SSF81296; E set domains; 3.
DR   SUPFAM; SSF103575; Plexin repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF101912; Sema domain; 1.
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        583
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P08581"
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        677
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P08581"
FT   CARBOHYD        762
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P08581"
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
//