(data stored in ACNUC1130 zone)

HOVERGEN: MET_LOXAF

ID   MET_LOXAF               Reviewed;        1382 AA.
AC   Q108U6;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   13-OCT-2009, entry version 30.
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   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA   Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA   Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J.,
RA   Hansen N., Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P.,
RA   Laric P., Larson S., Lee-Lin S.-Q., Legaspi R., Madden M.,
RA   Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C., Maskeri B.,
RA   McDowell J., Mojidi H.A., Mullikin J.C., Oestreicher J.S., Park M.,
RA   Portnoy M.E., Prasad A., Puri O., Reddix-Dugue N., Schandler K.,
RA   Schueler M.G., Sison C., Stantripop S., Stephen E., Taye A.,
RA   Thomas J.W., Thomas P.J., Tsipouri V., Ung L., Vogt J.L.,
RA   Wetherby K.D., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (JUL-2006) 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 (By similarity).
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; DP000087; ABG66646.1; -; Genomic_DNA.
DR   SMR; Q108U6; 40-564, 1047-1347.
DR   STRING; Q108U6; -.
DR   HOVERGEN; Q108U6; -.
DR   BRENDA; 2.7.10.1; 294469.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell.
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:0007275; P:multicellular organismal development; IEA:InterPro.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
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   3: Inferred from homology;
DR   PRODOM; Q108U6.
DR   SWISS-2DPAGE; Q108U6.
KW   ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor; Repeat;
KW   Signal; Transferase; Transmembrane; Tyrosine-protein kinase.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25   1382       Hepatocyte growth factor receptor.
FT                                /FTId=PRO_0000250465.
FT   TOPO_DOM     25    935       Extracellular (Potential).
FT   TRANSMEM    936    956       Potential.
FT   TOPO_DOM    957   1382       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    450    450       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    608    608       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    636    636       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    751    751       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    786    786       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    880    880       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    931    931       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1382 AA;  154684 MW;  B22F334F1CC126BC CRC64;
     MKAPAVLAPG VLVLLFTLVR KSHGECEEAL AKSKMNVNMK YQLPNFTADT PIQNVVLHEH
     HIFLGAINNI YVLNDKDLQK VAEYKTGPVL EHPDCLPCQD CSSKANLSGS VWKDNINMAL
     LVDTYYDDQL ITCGSVNRGT CQRHVLPPDN PADIHSKVHC MYSPQADEEP SKCPDCVVSA
     LGTKVLLTEK DRFINFFVGN TVNSSYLPDH SLHSISVRRL KETQDGFKFL TDQSYIDVLP
     EFRDSYPIKY VHAFKHNQFI YFLTVQRETL ESQTFHTRII RFCSVDSGLH SYMEMPLECI
     LTEKRRKRSA REEVFNILQA AYVSKPGAYL AKQIGALPDD DILYGVFAQS KLDSAEPMNR
     SAVCAFPIKY VNDFFNKIVN KNNVRCLQHF YGPNHEHCFN RTLLRNSSGC EVRRDEYRTE
     FTTALQRVDL FTGQFNQVLL TSISTFIKGN LTIANLGTSE GRFMQVVVSR SGLTTPHVNF
     RLDSHAVSPE VILEHPLNQN GYTLVITGKK ITKIPLDGLG CDHFQSCSQC LSAPSFVQCG
     WCHNKCARAE ECPNGMWTQE ICLPTIYEVF PTSAPLEGGT TLTVCGWDFG FRRNNKFDLK
     KTRVLIGNDS CTLTLSESTT NTLKCTVGPA MNKHFNLSII ISNGRGTARY RTFSYVEPVI
     TSISPSYGPK AGGTLVTLTG KYLNSGNSRH ISIGGKTCTL KSVSDSVLEC YTPAQSISTD
     FPVKLKIDLA NREAYSFSYQ EDPTVYEIHP NKSFISGGST ITGIGKNLNS VSVPRMVINV
     QEAGRNFTVA CQHRSNSEII CCTTPSLQQL NLQLPLKTKA FFMLDGIHSN YFDLIYVHNP
     VFKPFKKPVM ISMGNENVLE IKGDYIDPEA VKGEVLKVGN KSCENIHLQS EAVLCTVPND
     LLKLNSELNI EWKQAVSSTV LGKVIVQPDQ NFTGLIVGVV SISIILLLLL GLFLWLKKRK
     QIKDLGSELV RYDARVHTPH LDRLVSARSV SPTTEMVSNE SVDYRATFPE DQFPNSSQNG
     SCRQVQYPLT DMSPILTNGD SDSSIPLLQN NVHIDLSALN PELVQAVQHV VIGPSSLIVH
     FNEVIGRGHF GCVYHGTLLD NGDKKIHCAV KSLNRITDIG EVSQFLTEGI IMKDFSHPNV
     LSLLGICLRS EGSPLVVLPY MKHGDLRNFI RNETHNPTVK DLIGFGLQVA KGMKYLASKK
     FVHRDLAARN CMLDEKFTVK VADFGLARDV YDKEYYSVHN KTGAKLPVKW MALESLQTQK
     FTTKSDVWSF GVLLWELMTR GAPPYPDVNT FDITVYLLQG RRLLQPEYCP DPLYEVMLKC
     WHPKAEMRPS FSELVSRISA IFSTFIGEHY VHVNTTYVNV KCVAPYPSLL SSQDSVDDEV
     DT
//

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