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Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)

 MET_RABIT               Reviewed;        1382 AA.
Q09YN5;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 1.
22-NOV-2017, entry version 95.
RecName: Full=Hepatocyte growth factor receptor;
Short=HGF receptor;
EC=2.7.10.1;
AltName: Full=HGF/SF receptor;
AltName: Full=Proto-oncogene c-Met;
AltName: Full=Scatter factor receptor;
Short=SF receptor;
AltName: Full=Tyrosine-protein kinase Met;
Flags: Precursor;
Name=MET;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J.,
Hansen N., Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P.,
Laric P., Larson S., Lee-Lin S.-Q., Legaspi R., Madden M.,
Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C., Maskeri B.,
McDowell J., Mojidi H.A., Mullikin J.C., Oestreicher J.S., Park M.,
Portnoy M.E., Prasad A., Puri O., Reddix-Dugue N., Schandler K.,
Schueler M.G., Sison C., Stantripop S., Stephen E., Taye A.,
Thomas J.W., Thomas P.J., Tsipouri V., Ung L., Vogt J.L.,
Wetherby K.D., Young A., Green E.D.;
"NISC comparative sequencing initiative.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Receptor tyrosine kinase that transduces signals from
the extracellular matrix into the cytoplasm by binding to
hepatocyte growth factor/HGF ligand. Regulates many physiological
processes including proliferation, scattering, morphogenesis and
survival. Ligand binding at the cell surface induces
autophosphorylation of MET on its intracellular domain that
provides docking sites for downstream signaling molecules.
Following activation by ligand, interacts with the PI3-kinase
subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1.
Recruitment of these downstream effectors by MET leads to the
activation of several signaling cascades including the RAS-ERK,
PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is
associated with the morphogenetic effects while PI3K/AKT
coordinates prosurvival effects. During embryonic development, MET
signaling plays a role in gastrulation, development and migration
of muscles and neuronal precursors, angiogenesis and kidney
formation. In adults, participates in wound healing as well as
organ regeneration and tissue remodeling. Promotes also
differentiation and proliferation of hematopoietic cells (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: In its inactive state, the C-terminal tail
interacts with the catalytic domain and inhibits the kinase
activity. Upon ligand binding, the C-terminal tail is displaced
and becomes phosphorylated, thus increasing the kinase activity
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer made of an alpha chain (50 kDa) and a beta
chain (145 kDa) which are disulfide linked. Binds PLXNB1.
Interacts when phosphorylated with downstream effectors including
STAT3, PIK3R1, SRC, PCLG1, GRB2 and GAB1. Interacts with SPSB1,
SPSB2 and SPSB4. Interacts with INPP5D/SHIP1. When phosphorylated
at Tyr-1357, interacts with INPPL1/SHIP2. Interacts with RANBP9
and RANBP10, as well as SPSB1, SPSB2, SPSB3 and SPSB4. SPSB1
binding occurs in the presence and in the absence of HGF, however
HGF treatment has a positive effect on this interaction. Interacts
with MUC20; prevents interaction with GRB2 and suppresses
hepatocyte growth factor-induced cell proliferation. Interacts
with GRB10. Interacts with PTPN1 and PTPN2. Interacts with
HSP90AA1 and HSP90AB1; the interaction suppresses MET kinase
activity. {ECO:0000250|UniProtKB:P08581,
ECO:0000250|UniProtKB:P16056}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}.
-!- DOMAIN: The kinase domain is involved in SPSB1 binding.
{ECO:0000250}.
-!- DOMAIN: The beta-propeller Sema domain mediates binding to HGF.
{ECO:0000250}.
-!- PTM: Autophosphorylated in response to ligand binding on Tyr-1235
and Tyr-1236 in the kinase domain leading to further
phosphorylation of Tyr-1350 and Tyr-1357 in the C-terminal
multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-
1350 and Tyr-1366. Dephosphorylated by PTPN1 and PTPN2 (By
similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor
stability and activity through proteasomal degradation (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; DP000006; AAY89012.1; -; Genomic_DNA.
RefSeq; NP_001164511.1; NM_001171040.1.
UniGene; Ocu.7439; -.
ProteinModelPortal; Q09YN5; -.
SMR; Q09YN5; -.
STRING; 9986.ENSOCUP00000011247; -.
PRIDE; Q09YN5; -.
Ensembl; ENSOCUT00000013064; ENSOCUP00000011247; ENSOCUG00000013060.
GeneID; 100126565; -.
KEGG; ocu:100126565; -.
CTD; 4233; -.
eggNOG; KOG1095; Eukaryota.
eggNOG; KOG3610; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00810000125384; -.
HOGENOM; HOG000220900; -.
HOVERGEN; HBG006348; -.
InParanoid; Q09YN5; -.
KO; K05099; -.
OMA; QCPDCVV; -.
OrthoDB; EOG091G0751; -.
TreeFam; TF317402; -.
Proteomes; UP000001811; Chromosome 7.
Bgee; ENSOCUG00000013060; -.
GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
GO; GO:0001886; P:endothelial cell morphogenesis; IEA:Ensembl.
GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; IEA:Ensembl.
GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; IEA:Ensembl.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; IEA:Ensembl.
GO; GO:0050918; P:positive chemotaxis; ISS:UniProtKB.
GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISS:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR016201; PSI.
InterPro; IPR001627; Semap_dom.
InterPro; IPR036352; Semap_dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016244; Tyr_kinase_HGF/MSP_rcpt.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01403; Sema; 1.
Pfam; PF01833; TIG; 3.
PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00429; IPT; 4.
SMART; SM00423; PSI; 1.
SMART; SM00630; Sema; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF101912; SSF101912; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF81296; SSF81296; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS51004; SEMA; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Disulfide bond; Glycoprotein; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Proto-oncogene;
Receptor; Reference proteome; Repeat; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
Ubl conjugation.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 1382 Hepatocyte growth factor receptor.
/FTId=PRO_0000260429.
TOPO_DOM 25 933 Extracellular. {ECO:0000255}.
TRANSMEM 934 956 Helical. {ECO:0000255}.
TOPO_DOM 957 1382 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 516 Sema. {ECO:0000255|PROSITE-
ProRule:PRU00352}.
DOMAIN 564 656 IPT/TIG 1.
DOMAIN 658 740 IPT/TIG 2.
DOMAIN 743 837 IPT/TIG 3.
DOMAIN 1079 1346 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1085 1093 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1213 1382 Interaction with RANBP9. {ECO:0000250}.
REGION 1321 1360 Interaction with MUC20. {ECO:0000250}.
ACT_SITE 1205 1205 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 1111 1111 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 308 309 Cleavage. {ECO:0000255}.
MOD_RES 967 967 Phosphoserine.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 978 978 Phosphothreonine.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 991 991 Phosphoserine.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 998 998 Phosphoserine.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 1001 1001 Phosphoserine.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 1004 1004 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 1231 1231 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 1235 1235 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 1236 1236 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 1290 1290 Phosphothreonine.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 1350 1350 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 1357 1357 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08581}.
MOD_RES 1366 1366 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08581}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 203 203 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 359 359 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 608 608 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 614 614 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 636 636 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 786 786 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 880 880 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 95 101 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 98 160 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 133 141 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 173 176 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 299 364 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 386 398 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 521 539 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 527 562 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 530 546 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 542 552 {ECO:0000255|PROSITE-ProRule:PRU00352}.
SEQUENCE 1382 AA; 153973 MW; 4E0ACE4E90559E9C CRC64;
MKAPAVLAPG ILVLLFTLVP RSHGECKEAL VKSEMNVNMK YQLPNFTAET PIQNVLLHQH
HVYLGAINHI YVLNDKDLQK VAEYTTGPVL EHPDCLPCQD CSSKANSSGA VWKDNINLAL
LVDKYYDDQL ISCGSVNRGT CQRHVLPPDN PADIQSGVYC MFSPQADEEP GQCPDCVVSP
LGAKVLLSKK QRFIYFFVGN TINSSYLPDH SLHSISVRRL KETQDGFKFL TDQSYIDVLP
EFRDSYPIKY VHAFESNHFI YFLTVQKETL DAQTFHTRII RFCSKDSGLH SYMEMPLECI
LTEKRRKRAT REEVFNILQA AYVSKPGAHL ARQIGATPND DILYGVFAQS KPDSAEPMNR
SAVCAFPIKY INEFFNKIVN KNNVKCLQHF YGPNHEHCFN RTLLRNSSDC EARSDEYRTE
LTTALQRVDL FMGQFNQVLL TSISTFIKGD LTIANLGTSE GRFMQVVISR TILNVPHVNF
RLDSHPVSPE VVVEHPLNQN GYTLVVTGNK ITKIPLNGLG CGHFQSCSQC LSAPPFVQCG
WCHDKCVPSE ECPSGTWTQE ICLPAIYKVF PASAPLEGGT TLTICGWDFG FRKNNKFDLK
KTKVLLGNES CALNLSESTT NTLKCTVGAT THEHFNMSIT VSNSRGRTQY STFSYVAPVI
TSISPSYGPK AGGTLLTLTG KYLDSGNSRH ISIGGKTCTL KSMSNSILEC YTPAQTISTE
FPVKLEIDLA SRETSSFSYR EDPIVDEFYP TKSFISGGST ITGVGKNLDS VSVPRMVISV
HEAGSNFTVA CQHRSNSEII CCTTPSLQQL NLHLPLKTKA FFMLDGILSK HFDLTYVHNP
VFKPFEKPVM ISMGNENVLE IKGNDIDPEA VKGEVLKVGN KSCENIHSDS EAVLCTVPND
LLKLNSELNI EWKQAVSSTV LGKVIVQPDQ NFMGLIVGGV SISIILLLLL GLFLWLKKKK
RIKDLGSELV RYDARVHTPH LDRLVSARSV SPTTEMVSNE SVDYRATFPE DQFPNSSQNG
SCRQVQYPLT DLSPILTSGD SDISSPLLQN TVHIDLSALN PELVQAVQHV VIGPSSLIVH
FSEVIGRGHF GCVYHGTLLD NDGKKIHCAV KSLNRITDIG EVSQFLTEGI IMKDFSHPNV
LSLLGICLRS EGSPLVVLPY MKHGDLRNFI RNETHNPTVK DLIGFGLQVA KGMKYLASKK
FVHRDLAARN CMLDEKFTVK VADFGLARDM YDKEYYSVHN KTGAKLPVKW MALESLQTQK
FTTKSDVWSF GVLLWELMTR GAPPYPDVNT FDITVYLLQG RRLLQPEYCP DALYEVMLKC
WHPKAEMRPS FSELVSRIST IFSTFIGEHY VHVNATYVNV KCVAPYPSLL SSQDNVDGTV
DT


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