(data stored in ACNUC1130 zone)

HOVERGEN: 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   13-OCT-2009, entry version 97.
DE   RecName: Full=Hepatocyte growth factor receptor;
DE            Short=HGF receptor;
DE            EC=2.7.10.1;
DE   AltName: Full=Scatter factor receptor;
DE            Short=SF receptor;
DE   AltName: Full=HGF/SF receptor;
DE   AltName: Full=Met proto-oncogene tyrosine kinase;
DE   AltName: Full=c-Met;
DE   Flags: Precursor;
GN   Name=Met;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   MEDLINE=97419268; PubMed=9271668; DOI=10.1007/s003359900533;
RA   Wallenius V.R., Rawet H., Skrtic S., Helou K., Qiu Y., Levan G.,
RA   Ekberg S., Carlsson B., Isaksson O.G.P., Nakamura T., Jansson J.-O.;
RT   "Chromosomal localization of rat hepatocyte growth factor (Hgf) and
RT   HGF 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   MEDLINE=97006137; PubMed=8853431;
RA   Liu Y., Tolbert E.M., Sun A.M., Dworkin L.D.;
RT   "Primary structure of rat HGF receptor and induced expression in
RT   glomerular 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   MEDLINE=94220137; PubMed=8166728; DOI=10.1006/bbrc.1994.1481;
RA   Tsujii M., Kawano S., Tsuji S., Ito T., Hayashi N., Horimoto M.,
RA   Mita E., Nagano K., Masuda E., Hayashi N., Fusamoto H., Kamada T.;
RT   "Increased expression of c-met messenger RNA following acute gastric
RT   injury in rats.";
RL   Biochem. Biophys. Res. Commun. 200:536-541(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 851-1002.
RC   TISSUE=Intestine;
RX   MEDLINE=95354758; 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
RT   gland 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 for hepatocyte growth factor and scatter
CC       factor. Has a tyrosine-protein kinase activity. Functions in cell
CC       proliferation, scattering, morphogenesis and survival (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Heterodimer formed of an alpha chain (50 kDa) and a beta
CC       chain (145 kDa) which are disulfide linked. Binds PLXNB1 and GRB2.
CC       Interacts with INPP5D/SHIP1. When phosphorylated at Tyr-1357,
CC       interacts with INPPL1/SHIP2. Interacts with RANBP9 and RANBP10, as
CC       well as SPSB1, SPSB2, SPSB3 and SPSB4. SPSB1 binding occurs in the
CC       presence and in the absence of HGF, however HGF treatment has a
CC       positive effect on this interaction. Interacts with MUC20;
CC       prevents interaction with GRB2 and suppresses hepatocyte growth
CC       factor-induced cell proliferation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in lung, liver and
CC       kidney, also expressed in stomach, intestine, spleen, testis and
CC       brain. Not expressed in heart or muscle.
CC   -!- DEVELOPMENTAL STAGE: Expression is down-regulated during pregnancy
CC       and is virtually undetectable during lactation. Expression
CC       progressively 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 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family.
CC   -!- SIMILARITY: Contains 3 IPT/TIG domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 Sema domain.
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CC   -!- GENE_FAMILY: HBG006348 [ FAMILY / ALN / TREE ]
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   IPI; IPI00326236; -.
DR   PIR; PC2131; PC2131.
DR   RefSeq; NP_113705.1; -.
DR   UniGene; Rn.10617; -.
DR   HSSP; P11362; 1FGK.
DR   SMR; P97523; 40-565, 1047-1347.
DR   STRING; P97523; -.
DR   PhosphoSite; P97523; -.
DR   Ensembl; ENSRNOT00000009662; ENSRNOP00000009662; ENSRNOG00000007079; Rattus norvegicus.
DR   GeneID; 24553; -.
DR   KEGG; rno:24553; -.
DR   UCSC; NM_031517; rat.
DR   CTD; 24553; -.
DR   RGD; 3082; Met.
DR   HOVERGEN; P97523; -.
DR   BRENDA; 2.7.10.1; 248.
DR   NextBio; 603662; -.
DR   ArrayExpress; P97523; -.
DR   Genevestigator; P97523; -.
DR   GO; GO:0019861; C:flagellum; IDA:RGD.
DR   GO; GO:0016021; C:integral to membrane; NAS:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kin...; IEA:EC.
DR   GO; GO:0007420; P:brain development; IEP:RGD.
DR   GO; GO:0007595; P:lactation; IEP:RGD.
DR   GO; GO:0001764; P:neuron migration; IDA:RGD.
DR   GO; GO:0046777; P:protein amino acid autophosphorylation; IDA:RGD.
DR   GO; GO:0030317; P:sperm motility; IMP:RGD.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR001245; Tyr_pkinase.
DR   InterPro; IPR008266; Tyr_pkinase_AS.
DR   InterPro; IPR016244; TyrPK_HGF-R.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 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   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00429; IPT; 4.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SMART; SM00219; TyrKc; 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;
DR   PRODOM; P97523.
DR   SWISS-2DPAGE; P97523.
KW   ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor; Repeat;
KW   Signal; Transferase; Transmembrane; Tyrosine-protein kinase.
FT   DOMAIN        1     39       PRODOM:2005.1:PD686693  6
FT   DOMAIN       40    146       PRODOM:2005.1:PD003973  45
FT   DOMAIN      156    227       PRODOM:2005.1:PD962738  14
FT   DOMAIN      238    373       PRODOM:2005.1:PD331587  41
FT   DOMAIN      374    475       PRODOM:2005.1:PDA1E5D6  5
FT   DOMAIN      476    524       PRODOM:2005.1:PD608132  8
FT   DOMAIN      525    630       PRODOM:2005.1:PD001668  42
FT   DOMAIN      658    718       PRODOM:2005.1:PD003981  45
FT   DOMAIN      719    805       PRODOM:2005.1:PD591320  41
FT   DOMAIN      808    840       PRODOM:2005.1:PDA1E4F1  5
FT   DOMAIN      841    901       PRODOM:2005.1:PDA19518  6
FT   DOMAIN      902   1083       PRODOM:2005.1:PD464849  8
FT   DOMAIN     1083   1330       PRODOM:2005.1:PD000001  8496
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25   1382       Hepatocyte growth factor receptor.
FT                                /FTId=PRO_0000024442.
FT   TOPO_DOM     25    935       Extracellular (Potential).
FT   TRANSMEM    936    956       Potential.
FT   TOPO_DOM    957   1379       Cytoplasmic (Potential).
FT   DOMAIN       27    516       Sema.
FT   DOMAIN      564    656       IPT/TIG 1.
FT   DOMAIN      658    740       IPT/TIG 2.
FT   DOMAIN      743    837       IPT/TIG 3.
FT   DOMAIN     1079   1346       Protein kinase.
FT   NP_BIND    1085   1093       ATP (By similarity).
FT   REGION     1213   1382       Interaction with RANBP9 (By similarity).
FT   REGION     1321   1360       Interaction with MUC20 (By similarity).
FT   ACT_SITE   1205   1205       Proton acceptor (By similarity).
FT   BINDING    1111   1111       ATP (By similarity).
FT   SITE        308    309       Cleavage (Potential).
FT   MOD_RES     967    967       Phosphoserine (By similarity).
FT   MOD_RES     978    978       Phosphothreonine (By similarity).
FT   MOD_RES     989    989       Phosphoserine (By similarity).
FT   MOD_RES     991    991       Phosphoserine (By similarity).
FT   MOD_RES     998    998       Phosphoserine (By similarity).
FT   MOD_RES    1001   1001       Phosphoserine (By similarity).
FT   MOD_RES    1004   1004       Phosphotyrosine (By similarity).
FT   MOD_RES    1231   1231       Phosphotyrosine (By similarity).
FT   MOD_RES    1235   1235       Phosphotyrosine (By similarity).
FT   MOD_RES    1236   1236       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1357   1357       Phosphotyrosine (By similarity).
FT   CARBOHYD     45     45       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    106    106       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    203    203       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    359    359       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    400    400       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    406    406       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    608    608       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    636    636       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    786    786       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    880    880       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     53     53       H -> Q (in Ref. 2; AAB19189).
FT   CONFLICT     58     58       P -> H (in Ref. 2; AAB19189).
FT   CONFLICT    240    240       P -> G (in Ref. 2; AAB19189).
FT   CONFLICT    427    427       R -> A (in Ref. 2; AAB19189).
FT   CONFLICT    485    485       Y -> H (in Ref. 2; AAB19189).
FT   CONFLICT    490    495       EVIVEH -> GAAGIR (in Ref. 3).
FT   CONFLICT    533    533       P -> A (in Ref. 2; AAB19189).
FT   CONFLICT    740    740       R -> G (in Ref. 2; AAB19189).
FT   CONFLICT    744    744       V -> F (in Ref. 2; AAB19189).
FT   CONFLICT    808    808       R -> Q (in Ref. 2; AAB19189).
FT   CONFLICT    890    893       SEAL -> TASV (in Ref. 4; CAA86508).
FT   CONFLICT    907    907       Missing (in Ref. 4; CAA86508).
FT   CONFLICT    924    924       K -> E (in Ref. 4; CAA86508).
FT   CONFLICT    934    934       A -> R (in Ref. 4; CAA86508).
FT   CONFLICT   1028   1028       L -> P (in Ref. 2; AAB19189).
FT   CONFLICT   1068   1068       P -> Q (in Ref. 2; AAB19189).
FT   CONFLICT   1197   1197       V -> A (in Ref. 2 and 5).
FT   CONFLICT   1331   1331       V -> F (in Ref. 2; AAB19189).
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
//

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