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Database: UniProt
Entry: P35968
LinkDB: P35968
Original site: P35968 
ID   VGFR2_HUMAN             Reviewed;        1356 AA.
AC   P35968; A2RRS0; B5A925; C5IFA0; O60723; Q14178;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   19-MAR-2014, entry version 163.
DE   RecName: Full=Vascular endothelial growth factor receptor 2;
DE            Short=VEGFR-2;
DE            EC=2.7.10.1;
DE   AltName: Full=Fetal liver kinase 1;
DE            Short=FLK-1;
DE   AltName: Full=Kinase insert domain receptor;
DE            Short=KDR;
DE   AltName: Full=Protein-tyrosine kinase receptor flk-1;
DE   AltName: CD_antigen=CD309;
DE   Flags: Precursor;
GN   Name=KDR; Synonyms=FLK1, VEGFR2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH VEGFC, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=18593464; DOI=10.1186/ar2447;
RA   Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
RA   Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
RT   "Novel splice variants derived from the receptor tyrosine kinase
RT   superfamily are potential therapeutics for rheumatoid arthritis.";
RL   Arthritis Res. Ther. 10:R73-R73(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN INHIBITION OF
RP   LYMPHANGIOGENESIS, INTERACTION WITH VEGFC, AND TISSUE SPECIFICITY.
RX   PubMed=19668192; DOI=10.1038/nm.2018;
RA   Albuquerque R.J., Hayashi T., Cho W.G., Kleinman M.E., Dridi S.,
RA   Takeda A., Baffi J.Z., Yamada K., Kaneko H., Green M.G., Chappell J.,
RA   Wilting J., Weich H.A., Yamagami S., Amano S., Mizuki N.,
RA   Alexander J.S., Peterson M.L., Brekken R.A., Hirashima M., Capoor S.,
RA   Usui T., Ambati B.K., Ambati J.;
RT   "Alternatively spliced vascular endothelial growth factor receptor-2
RT   is an essential endogenous inhibitor of lymphatic vessel growth.";
RL   Nat. Med. 15:1023-1030(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Yin L.Y., Wu Y., Patterson C.;
RT   "Full length human KDR/flk-1 sequence.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Umbilical vein;
RA   Yu Y., Whitney R.G., Sato J.D.;
RT   "Coding region for human VEGF receptor KDR (VEGFR-2).";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   HIS-472.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-1356 (ISOFORM 1), AND VARIANT GLU-848.
RC   TISSUE=Umbilical vein;
RX   PubMed=1656371;
RA   Terman B.I., Carrion M.E., Kovacs E., Rasmussen B.A., Eddy R.L.,
RA   Shows T.B.;
RT   "Identification of a new endothelial cell growth factor receptor
RT   tyrosine kinase.";
RL   Oncogene 6:1677-1683(1991).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX   PubMed=7559454; DOI=10.1074/jbc.270.39.23111;
RA   Patterson C., Perrella M.A., Hsieh C.-M., Yoshizumi M., Lee M.-E.,
RA   Harber E.;
RT   "Cloning and functional analysis of the promoter for KDR/flk-1, a
RT   receptor for vascular endothelial growth factor.";
RL   J. Biol. Chem. 270:23111-23118(1995).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VEGFA.
RX   PubMed=1417831; DOI=10.1016/0006-291X(92)90483-2;
RA   Terman B.I., Dougher-Vermazen M., Carrion M.E., Dimitrov D.,
RA   Armellino D.C., Gospodarowicz D., Boehlen P.;
RT   "Identification of the KDR tyrosine kinase as a receptor for vascular
RT   endothelial cell growth factor.";
RL   Biochem. Biophys. Res. Commun. 187:1579-1586(1992).
RN   [10]
RP   FUNCTION AS VEGFA RECEPTOR; IN REGULATION OF CELL SHAPE; ACTIN
RP   CYTOSKELETON REORGANIZATION; CELL MIGRATION AND CELL PROLIFERATION,
RP   AND AUTOPHOSPHORYLATION.
RX   PubMed=7929439;
RA   Waltenberger J., Claesson-Welsh L., Siegbahn A., Shibuya M.,
RA   Heldin C.H.;
RT   "Different signal transduction properties of KDR and Flt1, two
RT   receptors for vascular endothelial growth factor.";
RL   J. Biol. Chem. 269:26988-26995(1994).
RN   [11]
RP   FUNCTION IN VEGFA SIGNALING; PHOSPHORYLATION OF PLCG1; ACTIVATION OF
RP   MAP KINASES AND IN PROMOTING PROLIFERATION OF ENDOTHELIAL CELLS,
RP   INTERACTION WITH VEGFA AND PLCG1, AUTOPHOSPHORYLATION, SUBCELLULAR
RP   LOCATION, AND GLYCOSYLATION.
RX   PubMed=9160888; DOI=10.1038/sj.onc.1201047;
RA   Takahashi T., Shibuya M.;
RT   "The 230 kDa mature form of KDR/Flk-1 (VEGF receptor-2) activates the
RT   PLC-gamma pathway and partially induces mitotic signals in NIH3T3
RT   fibroblasts.";
RL   Oncogene 14:2079-2089(1997).
RN   [12]
RP   FUNCTION IN INDUCTION OF NOS2 AND NOS3.
RX   PubMed=9837777; DOI=10.1006/bbrc.1998.9719;
RA   Kroll J., Waltenberger J.;
RT   "VEGF-A induces expression of eNOS and iNOS in endothelial cells via
RT   VEGF receptor-2 (KDR).";
RL   Biochem. Biophys. Res. Commun. 252:743-746(1998).
RN   [13]
RP   FUNCTION IN ACTIVATION OF THE PHOSPHATIDYLINOSITOL 3-KINASE AND AKT1
RP   SIGNALING PATHWAY.
RX   PubMed=9804796; DOI=10.1074/jbc.273.46.30336;
RA   Gerber H.P., McMurtrey A., Kowalski J., Yan M., Keyt B.A., Dixit V.,
RA   Ferrara N.;
RT   "Vascular endothelial growth factor regulates endothelial cell
RT   survival through the phosphatidylinositol 3'-kinase/Akt signal
RT   transduction pathway. Requirement for Flk-1/KDR activation.";
RL   J. Biol. Chem. 273:30336-30343(1998).
RN   [14]
RP   FUNCTION IN NITRIC OXIDE RELEASE.
RX   PubMed=10600473; DOI=10.1006/bbrc.1999.1729;
RA   Kroll J., Waltenberger J.;
RT   "A novel function of VEGF receptor-2 (KDR): rapid release of nitric
RT   oxide in response to VEGF-A stimulation in endothelial cells.";
RL   Biochem. Biophys. Res. Commun. 265:636-639(1999).
RN   [15]
RP   CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT GLU-848,
RP   PHOSPHORYLATION AT TYR-1054 AND TYR-1059, AND ENZYME REGULATION.
RX   PubMed=10037737; DOI=10.1074/jbc.274.10.6453;
RA   Kendall R.L., Rutledge R.Z., Mao X., Tebben A.J., Hungate R.W.,
RA   Thomas K.A.;
RT   "Vascular endothelial growth factor receptor KDR tyrosine kinase
RT   activity is increased by autophosphorylation of two activation loop
RT   tyrosine residues.";
RL   J. Biol. Chem. 274:6453-6460(1999).
RN   [16]
RP   FUNCTION IN PHOSPHORYLATION OF PLCG1 AND PTK2/FAK1, INTERACTION WITH
RP   VEGFA, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-996; TYR-1054 AND
RP   TYR-1059, MUTAGENESIS OF TYR-996; TYR-1054 AND TYR-1059, SUBCELLULAR
RP   LOCATION, AND ENZYME REGULATION.
RX   PubMed=10102632; DOI=10.1038/sj.onc.1202478;
RA   Dougher M., Terman B.I.;
RT   "Autophosphorylation of KDR in the kinase domain is required for
RT   maximal VEGF-stimulated kinase activity and receptor
RT   internalization.";
RL   Oncogene 18:1619-1627(1999).
RN   [17]
RP   INTERACTION WITH HIV-1 TAT.
RX   PubMed=10590123; DOI=10.1128/JVI.74.1.344-353.2000;
RA   Mitola S., Soldi R., Zanon I., Barra L., Gutierrez M.I., Berkhout B.,
RA   Giacca M., Bussolino F.;
RT   "Identification of specific molecular structures of human
RT   immunodeficiency virus type 1 Tat relevant for its biological effects
RT   on vascular endothelial cells.";
RL   J. Virol. 74:344-353(2000).
RN   [18]
RP   FUNCTION IN ENDOTHELIAL CELL PROLIFERATION; PHOSPHORYLATION OF PLCG1
RP   AND ACTIVATION OF MAP KINASES, PHOSPHORYLATION AT TYR-1175 AND
RP   TYR-1214, AND MUTAGENESIS OF LYS-868 AND TYR-1175.
RX   PubMed=11387210; DOI=10.1093/emboj/20.11.2768;
RA   Takahashi T., Yamaguchi S., Chida K., Shibuya M.;
RT   "A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-
RT   A-dependent activation of PLC-gamma and DNA synthesis in vascular
RT   endothelial cells.";
RL   EMBO J. 20:2768-2778(2001).
RN   [19]
RP   UBIQUITINATION, FUNCTION IN NITRIC OXIDE PRODUCTION, SUBCELLULAR
RP   LOCATION, AND INTERACTION WITH CBL.
RX   PubMed=12649282; DOI=10.1074/jbc.M301410200;
RA   Duval M., Bedard-Goulet S., Delisle C., Gratton J.P.;
RT   "Vascular endothelial growth factor-dependent down-regulation of Flk-
RT   1/KDR involves Cbl-mediated ubiquitination. Consequences on nitric
RT   oxide production from endothelial cells.";
RL   J. Biol. Chem. 278:20091-20097(2003).
RN   [20]
RP   INTERACTION WITH FLT4.
RX   PubMed=12881528; DOI=10.1074/jbc.M304499200;
RA   Dixelius J., Makinen T., Wirzenius M., Karkkainen M.J., Wernstedt C.,
RA   Alitalo K., Claesson-Welsh L.;
RT   "Ligand-induced vascular endothelial growth factor receptor-3 (VEGFR-
RT   3) heterodimerization with VEGFR-2 in primary lymphatic endothelial
RT   cells regulates tyrosine phosphorylation sites.";
RL   J. Biol. Chem. 278:40973-40979(2003).
RN   [21]
RP   INTERACTION WITH SHB, AND FUNCTION IN CELL MIGRATION.
RX   PubMed=15026417; DOI=10.1074/jbc.M312729200;
RA   Holmqvist K., Cross M.J., Rolny C., Haegerkvist R., Rahimi N.,
RA   Matsumoto T., Claesson-Welsh L., Welsh M.;
RT   "The adaptor protein shb binds to tyrosine 1175 in vascular
RT   endothelial growth factor (VEGF) receptor-2 and regulates VEGF-
RT   dependent cellular migration.";
RL   J. Biol. Chem. 279:22267-22275(2004).
RN   [22]
RP   SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=14991896; DOI=10.1002/path.1520;
RA   Fox S.B., Turley H., Cheale M., Blazquez C., Roberts H., James N.,
RA   Cook N., Harris A., Gatter K.;
RT   "Phosphorylated KDR is expressed in the neoplastic and stromal
RT   elements of human renal tumours and shuttles from cell membrane to
RT   nucleus.";
RL   J. Pathol. 202:313-320(2004).
RN   [23]
RP   INTERACTION WITH VEGFA AND VEGFD, PHOSPHORYLATION AT TYR-1054 AND
RP   TYR-1059, FUNCTION IN VEGFA AND VEGFD SIGNALING; ACTIVATION OF
RP   MAPK1/ERK2 AND MAPK3/ERK1; ACTIVATION OF AKT1; PHOSPHORYLATION OF
RP   PLCG1 AND NOS3; MODULATION OF INTRACELLULAR CA(2+) LEVELS; CELL
RP   SURVIVAL AND POSITIVE REGULATION OF CELL PROLIFERATION; CELL MIGRATION
RP   AND ANGIOGENESIS, AND ENZYME REGULATION.
RX   PubMed=15215251; DOI=10.1074/jbc.M401538200;
RA   Jia H., Bagherzadeh A., Bicknell R., Duchen M.R., Liu D., Zachary I.;
RT   "Vascular endothelial growth factor (VEGF)-D and VEGF-A differentially
RT   regulate KDR-mediated signaling and biological function in vascular
RT   endothelial cells.";
RL   J. Biol. Chem. 279:36148-36157(2004).
RN   [24]
RP   FUNCTION IN CELL MIGRATION; PHOSPHORYLATION OF PLCG1; ACTIVATION OF
RP   MAPK1/ERK2; MAPK3/ERK1 AND THE MAP KINASES AND IN REGULATION OF ACTIN
RP   CYTOSKELETON REORGANIZATION, INTERACTION WITH SH2D2A/TSAD,
RP   PHOSPHORYLATION AT TYR-951; TYR-1054; TYR-1059; TYR-1214; TYR-1305;
RP   TYR-1309 AND TYR-1319, AND MUTAGENESIS OF TYR-951.
RX   PubMed=15962004; DOI=10.1038/sj.emboj.7600709;
RA   Matsumoto T., Bohman S., Dixelius J., Berge T., Dimberg A.,
RA   Magnusson P., Wang L., Wikner C., Qi J.H., Wernstedt C., Wu J.,
RA   Bruheim S., Mugishima H., Mukhopadhyay D., Spurkland A.,
RA   Claesson-Welsh L.;
RT   "VEGF receptor-2 Y951 signaling and a role for the adapter molecule
RT   TSAd in tumor angiogenesis.";
RL   EMBO J. 24:2342-2353(2005).
RN   [25]
RP   FUNCTION IN ENDOTHELIAL CELL MIGRATION; ACTIVATION OF MAP KINASES AND
RP   IN PHOSPHORYLATION OF FYN; SRC AND NCK1, INTERACTION WITH GRB2; FYN
RP   AND NCK1, AND MUTAGENESIS OF TYR-1214.
RX   PubMed=16966330; DOI=10.1074/jbc.M603928200;
RA   Lamalice L., Houle F., Huot J.;
RT   "Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of
RT   Nck and activation of Fyn leading to SAPK2/p38 activation and
RT   endothelial cell migration in response to VEGF.";
RL   J. Biol. Chem. 281:34009-34020(2006).
RN   [26]
RP   SUBCELLULAR LOCATION, UBIQUITINATION, AND DEGRADATION.
RX   PubMed=17004325; DOI=10.1111/j.1600-0854.2006.00462.x;
RA   Ewan L.C., Jopling H.M., Jia H., Mittar S., Bagherzadeh A.,
RA   Howell G.J., Walker J.H., Zachary I.C., Ponnambalam S.;
RT   "Intrinsic tyrosine kinase activity is required for vascular
RT   endothelial growth factor receptor 2 ubiquitination, sorting and
RT   degradation in endothelial cells.";
RL   Traffic 7:1270-1282(2006).
RN   [27]
RP   FUNCTION IN ACTIVATION OF AKT1; PHOSPHORYLATION OF PLCG1 AND NOS3 AND
RP   REGULATION OF NITRIC OXIDE PRODUCTION, PHOSPHORYLATION AT TYR-801, AND
RP   MUTAGENESIS OF TYR-801.
RX   PubMed=17303569; DOI=10.1074/jbc.M609048200;
RA   Blanes M.G., Oubaha M., Rautureau Y., Gratton J.P.;
RT   "Phosphorylation of tyrosine 801 of vascular endothelial growth factor
RT   receptor-2 is necessary for Akt-dependent endothelial nitric-oxide
RT   synthase activation and nitric oxide release from endothelial cells.";
RL   J. Biol. Chem. 282:10660-10669(2007).
RN   [28]
RP   INTERACTION WITH DAB2IP.
RX   PubMed=19033661; DOI=10.1172/JCI36168;
RA   Zhang H., He Y., Dai S., Xu Z., Luo Y., Wan T., Luo D., Jones D.,
RA   Tang S., Chen H., Sessa W.C., Min W.;
RT   "AIP1 functions as an endogenous inhibitor of VEGFR2-mediated
RT   signaling and inflammatory angiogenesis in mice.";
RL   J. Clin. Invest. 118:3904-3916(2008).
RN   [29]
RP   PHOSPHORYLATION AT TYR-951; TYR-1175 AND TYR-1214, AND
RP   DEPHOSPHORYLATION BY PTPRB.
RX   PubMed=19136612; DOI=10.1096/fj.08-123810;
RA   Mellberg S., Dimberg A., Bahram F., Hayashi M., Rennel E., Ameur A.,
RA   Westholm J.O., Larsson E., Lindahl P., Cross M.J., Claesson-Welsh L.;
RT   "Transcriptional profiling reveals a critical role for tyrosine
RT   phosphatase VE-PTP in regulation of VEGFR2 activity and endothelial
RT   cell morphogenesis.";
RL   FASEB J. 23:1490-1502(2009).
RN   [30]
RP   PHOSPHORYLATION AT TYR-801; TYR-951; TYR-996; TYR-1054; TYR-1059;
RP   TYR-1175 AND TYR-1214; DEPHOSPHORYLATION BY PTPRJ AT TYR-951; TYR-996;
RP   TYR-1054; TYR-1059; TYR-1175 AND TYR-1214.
RX   PubMed=18936167; DOI=10.1128/MCB.01374-08;
RA   Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.;
RT   "New role for the protein tyrosine phosphatase DEP-1 in Akt activation
RT   and endothelial cell survival.";
RL   Mol. Cell. Biol. 29:241-253(2009).
RN   [31]
RP   FUNCTION AS VEGFA RECEPTOR IN TUMOR ANGIOGENESIS, SUBCELLULAR
RP   LOCATION, AND UBIQUITINATION.
RX   PubMed=19834490; DOI=10.1038/cdd.2009.152;
RA   Zhang Z., Neiva K.G., Lingen M.W., Ellis L.M., Nor J.E.;
RT   "VEGF-dependent tumor angiogenesis requires inverse and reciprocal
RT   regulation of VEGFR1 and VEGFR2.";
RL   Cell Death Differ. 17:499-512(2010).
RN   [32]
RP   FUNCTION IN LYMPHANGIOGENESIS (ISOFORM 2).
RX   PubMed=20179233; DOI=10.1158/1078-0432.CCR-09-1936;
RA   Becker J., Pavlakovic H., Ludewig F., Wilting F., Weich H.A.,
RA   Albuquerque R., Ambati J., Wilting J.;
RT   "Neuroblastoma progression correlates with downregulation of the
RT   lymphangiogenesis inhibitor sVEGFR-2.";
RL   Clin. Cancer Res. 16:1431-1441(2010).
RN   [33]
RP   INTERACTION WITH VEGFC AND FLT4, SUBCELLULAR LOCATION, AND FUNCTION IN
RP   ANGIOGENESIS.
RX   PubMed=20224550; DOI=10.1038/emboj.2010.30;
RA   Nilsson I., Bahram F., Li X., Gualandi L., Koch S., Jarvius M.,
RA   Soderberg O., Anisimov A., Kholova I., Pytowski B., Baldwin M.,
RA   Yla-Herttuala S., Alitalo K., Kreuger J., Claesson-Welsh L.;
RT   "VEGF receptor 2/-3 heterodimers detected in situ by proximity
RT   ligation on angiogenic sprouts.";
RL   EMBO J. 29:1377-1388(2010).
RN   [34]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21539813; DOI=10.1016/j.bbrc.2011.04.093;
RA   Jopling H.M., Howell G.J., Gamper N., Ponnambalam S.;
RT   "The VEGFR2 receptor tyrosine kinase undergoes constitutive endosome-
RT   to-plasma membrane recycling.";
RL   Biochem. Biophys. Res. Commun. 410:170-176(2011).
RN   [35]
RP   FUNCTION IN LYMPHANGIOGENESIS, AND INTERACTION WITH FLT4 AND VEGFC.
RX   PubMed=20705758; DOI=10.1182/blood-2010-02-267427;
RA   Nakao S., Zandi S., Hata Y., Kawahara S., Arita R., Schering A.,
RA   Sun D., Melhorn M.I., Ito Y., Lara-Castillo N., Ishibashi T.,
RA   Hafezi-Moghadam A.;
RT   "Blood vessel endothelial VEGFR-2 delays lymphangiogenesis: an
RT   endogenous trapping mechanism links lymph- and angiogenesis.";
RL   Blood 117:1081-1090(2011).
RN   [36]
RP   REVIEW ON ROLE IN ANGIOGENESIS.
RX   PubMed=17002866;
RA   Shibuya M.;
RT   "Differential roles of vascular endothelial growth factor receptor-1
RT   and receptor-2 in angiogenesis.";
RL   J. Biochem. Mol. Biol. 39:469-478(2006).
RN   [37]
RP   REVIEW.
RX   PubMed=17658244; DOI=10.1016/j.cellsig.2007.05.013;
RA   Holmes K., Roberts O.L., Thomas A.M., Cross M.J.;
RT   "Vascular endothelial growth factor receptor-2: structure, function,
RT   intracellular signalling and therapeutic inhibition.";
RL   Cell. Signal. 19:2003-2012(2007).
RN   [38]
RP   REVIEW ON STRUCTURE AND FUNCTION.
RX   PubMed=18680722; DOI=10.1016/j.bbrc.2008.07.121;
RA   Roskoski R. Jr.;
RT   "VEGF receptor protein-tyrosine kinases: structure and regulation.";
RL   Biochem. Biophys. Res. Commun. 375:287-291(2008).
RN   [39]
RP   REVIEW ON ROLE IN ANGIOGENESIS AND CANCER.
RX   PubMed=19230644; DOI=10.1016/j.ceb.2008.12.012;
RA   Lohela M., Bry M., Tammela T., Alitalo K.;
RT   "VEGFs and receptors involved in angiogenesis versus
RT   lymphangiogenesis.";
RL   Curr. Opin. Cell Biol. 21:154-165(2009).
RN   [40]
RP   REVIEW ON LIGAND SPECIFICITY; FUNCTION; STRUCTURE; PHOSPHORYLATION AND
RP   SIGNALING.
RX   PubMed=19761875; DOI=10.1016/j.bbapap.2009.09.002;
RA   Grunewald F.S., Prota A.E., Giese A., Ballmer-Hofer K.;
RT   "Structure-function analysis of VEGF receptor activation and the role
RT   of coreceptors in angiogenic signaling.";
RL   Biochim. Biophys. Acta 1804:567-580(2010).
RN   [41]
RP   REVIEW ON ROLE IN ANGIOGENESIS AND CANCER.
RX   PubMed=20462514; DOI=10.1016/j.bbcan.2010.04.004;
RA   Guo S., Colbert L.S., Fuller M., Zhang Y., Gonzalez-Perez R.R.;
RT   "Vascular endothelial growth factor receptor-2 in breast cancer.";
RL   Biochim. Biophys. Acta 1806:108-121(2010).
RN   [42]
RP   REVIEW ON ROLE IN ANGIOGENESIS AND CANCER.
RX   PubMed=21779435; DOI=10.1177/1947601910392987;
RA   Shibuya M.;
RT   "Tyrosine kinase receptor Flt/VEGFR family: its characterization
RT   related to angiogenesis and cancer.";
RL   Genes Cancer 1:1119-1123(2010).
RN   [43]
RP   REVIEW ON LIGAND SPECIFICITY; FUNCTION; STRUCTURE; PHOSPHORYLATION AND
RP   SIGNALING.
RX   PubMed=21711246; DOI=10.1042/BJ20110301;
RA   Koch S., Tugues S., Li X., Gualandi L., Claesson-Welsh L.;
RT   "Signal transduction by vascular endothelial growth factor
RT   receptors.";
RL   Biochem. J. 437:169-183(2011).
RN   [44]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-982 AND SER-984, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [45]
RP   FUNCTION, AND INTERACTION WITH PDCD6.
RX   PubMed=21893193; DOI=10.1016/j.cellsig.2011.08.013;
RA   Rho S.B., Song Y.J., Lim M.C., Lee S.H., Kim B.R., Park S.Y.;
RT   "Programmed cell death 6 (PDCD6) inhibits angiogenesis through
RT   PI3K/mTOR/p70S6K pathway by interacting of VEGFR-2.";
RL   Cell. Signal. 24:131-139(2012).
RN   [46]
RP   ENZYME REGULATION, REDOX-ACTIVE DISULFIDE BOND, AND MUTAGENESIS OF
RP   CYS-1045.
RX   PubMed=23199280; DOI=10.1089/ars.2012.4565;
RA   Tao B.B., Liu S.Y., Zhang C.C., Fu W., Cai W.J., Wang Y., Shen Q.,
RA   Wang M.J., Chen Y., Zhang L.J., Zhu Y.Z., Zhu Y.C.;
RT   "VEGFR2 functions as an H(2)S-targeting receptor protein kinase with
RT   its novel Cys1045-Cys1024 disulfide bond serving as a specific
RT   molecular switch for hydrogen sulfide actions in vascular endothelial
RT   cells.";
RL   Antioxid. Redox Signal. 19:448-464(2013).
RN   [47]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 806-1171, FUNCTION,
RP   PHOSPHORYLATION AT TYR-1059, AND MASS SPECTROMETRY.
RX   PubMed=10368301; DOI=10.1016/S0969-2126(99)80042-2;
RA   McTigue M.A., Wickersham J.A., Pinko C., Showalter R.E., Parast C.V.,
RA   Tempczyk-Russell A., Gehring M.R., Mroczkowski B., Kan C.-C.,
RA   Villafranca J.E., Appelt K.;
RT   "Crystal structure of the kinase domain of human vascular endothelial
RT   growth factor receptor 2: a key enzyme in angiogenesis.";
RL   Structure 7:319-330(1999).
RN   [48]
RP   X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 806-1171 IN COMPLEX WITH
RP   SYNTHETIC INHIBITOR.
RX   PubMed=15837294; DOI=10.1016/j.bmcl.2005.03.034;
RA   Miyazaki Y., Matsunaga S., Tang J., Maeda Y., Nakano M.,
RA   Philippe R.J., Shibahara M., Liu W., Sato H., Wang L., Nolte R.T.;
RT   "Novel 4-amino-furo[2,3-d]pyrimidines as Tie-2 and VEGFR2 dual
RT   inhibitors.";
RL   Bioorg. Med. Chem. Lett. 15:2203-2207(2005).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 815-1171 IN COMPLEX WITH
RP   SYNTHETIC INHIBITOR.
RX   PubMed=17253678; DOI=10.1021/jm061107l;
RA   Hodous B.L., Geuns-Meyer S.D., Hughes P.E., Albrecht B.K., Bellon S.,
RA   Bready J., Caenepeel S., Cee V.J., Chaffee S.C., Coxon A., Emery M.,
RA   Fretland J., Gallant P., Gu Y., Hoffman D., Johnson R.E., Kendall R.,
RA   Kim J.L., Long A.M., Morrison M., Olivieri P.R., Patel V.F.,
RA   Polverino A., Rose P., Tempest P., Wang L., Whittington D.A., Zhao H.;
RT   "Evolution of a highly selective and potent 2-(pyridin-2-yl)-1,3,5-
RT   triazine Tie-2 kinase inhibitor.";
RL   J. Med. Chem. 50:611-626(2007).
RN   [50]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 806-1171 IN COMPLEX WITH
RP   SYNTHETIC INHIBITOR, AND FUNCTION.
RX   PubMed=18529047; DOI=10.1021/jm8001185;
RA   Peifer C., Selig R., Kinkel K., Ott D., Totzke F., Schaechtele C.,
RA   Heidenreich R., Roecken M., Schollmeyer D., Laufer S.;
RT   "Design, synthesis, and biological evaluation of novel 3-aryl-4-(1H-
RT   indole-3yl)-1,5-dihydro-2H-pyrrole-2-ones as vascular endothelial
RT   growth factor receptor (VEGF-R) inhibitors.";
RL   J. Med. Chem. 51:3814-3824(2008).
RN   [51]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 657-764, SUBUNIT,
RP   AUTOPHOSPHORYLATION, FUNCTION IN VEGFA SIGNALING AND ACTIVATION OF
RP   MAPK1/ERK2 AND MAPK3/ERK1, AND MUTAGENESIS OF ARG-726 AND ASP-731.
RX   PubMed=20080685; DOI=10.1073/pnas.0914052107;
RA   Yang Y., Xie P., Opatowsky Y., Schlessinger J.;
RT   "Direct contacts between extracellular membrane-proximal domains are
RT   required for VEGF receptor activation and cell signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:1906-1911(2010).
RN   [52]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 120-326 IN COMPLEX WITH
RP   VEGFC, INTERACTION WITH VEGFC, DOMAIN, DISULFIDE BONDS, AND
RP   GLYCOSYLATION AT ASN-143; ASN-245 AND ASN-318.
RX   PubMed=20145116; DOI=10.1073/pnas.0914318107;
RA   Leppanen V.M., Prota A.E., Jeltsch M., Anisimov A., Kalkkinen N.,
RA   Strandin T., Lankinen H., Goldman A., Ballmer-Hofer K., Alitalo K.;
RT   "Structural determinants of growth factor binding and specificity by
RT   VEGF receptor 2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:2425-2430(2010).
RN   [53]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 220-338 IN COMPLEX WITH
RP   ANTIBODY FRAGMENT, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-245 AND
RP   ASN-318.
RX   PubMed=21827946; DOI=10.1016/j.str.2011.01.019;
RA   Franklin M.C., Navarro E.C., Wang Y., Patel S., Singh P., Zhang Y.,
RA   Persaud K., Bari A., Griffith H., Shen L., Balderes P., Kussie P.;
RT   "The structural basis for the function of two anti-VEGF receptor 2
RT   antibodies.";
RL   Structure 19:1097-1107(2011).
RN   [54]
RP   VARIANT HCI SER-1147.
RX   PubMed=11807987; DOI=10.1002/gcc.10028;
RA   Walter J.W., North P.E., Waner M., Mizeracki A., Blei F.,
RA   Walker J.W.T., Reinisch J.F., Marchuk D.A.;
RT   "Somatic mutation of vascular endothelial growth factor receptors in
RT   juvenile hemangioma.";
RL   Genes Chromosomes Cancer 33:295-303(2002).
RN   [55]
RP   VARIANTS [LARGE SCALE ANALYSIS] LEU-275 AND ARG-873.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [56]
RP   VARIANTS [LARGE SCALE ANALYSIS] ARG-2; MET-136; GLY-248; ILE-297;
RP   VAL-462; HIS-472; ARG-482; ARG-539; MET-689; ASN-814 AND THR-1065.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [57]
RP   VARIANT HCI SUSCEPTIBILITY ARG-482.
RX   PubMed=18931684; DOI=10.1038/nm.1877;
RA   Jinnin M., Medici D., Park L., Limaye N., Liu Y., Boscolo E.,
RA   Bischoff J., Vikkula M., Boye E., Olsen B.R.;
RT   "Suppressed NFAT-dependent VEGFR1 expression and constitutive VEGFR2
RT   signaling in infantile hemangioma.";
RL   Nat. Med. 14:1236-1246(2008).
CC   -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface
CC       receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in
CC       the regulation of angiogenesis, vascular development, vascular
CC       permeability, and embryonic hematopoiesis. Promotes proliferation,
CC       survival, migration and differentiation of endothelial cells.
CC       Promotes reorganization of the actin cytoskeleton. Isoforms
CC       lacking a transmembrane domain, such as isoform 2 and isoform 3,
CC       may function as decoy receptors for VEGFA, VEGFC and/or VEGFD.
CC       Isoform 2 plays an important role as negative regulator of VEGFA-
CC       and VEGFC-mediated lymphangiogenesis by limiting the amount of
CC       free VEGFA and/or VEGFC and preventing their binding to FLT4.
CC       Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding
CC       of vascular growth factors to isoform 1 leads to the activation of
CC       several signaling cascades. Activation of PLCG1 leads to the
CC       production of the cellular signaling molecules diacylglycerol and
CC       inositol 1,4,5-trisphosphate and the activation of protein kinase
CC       C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP
CC       kinase signaling pathway, as well as of the AKT1 signaling
CC       pathway. Mediates phosphorylation of PIK3R1, the regulatory
CC       subunit of phosphatidylinositol 3-kinase, reorganization of the
CC       actin cytoskeleton and activation of PTK2/FAK1. Required for
CC       VEGFA-mediated induction of NOS2 and NOS3, leading to the
CC       production of the signaling molecule nitric oxide (NO) by
CC       endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation
CC       of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- ENZYME REGULATION: Present in an inactive conformation in the
CC       absence of bound ligand. Binding of VEGFA, VEGFC or VEGFD leads to
CC       dimerization and activation by autophosphorylation on tyrosine
CC       residues. Inhibited by the small molecule PTK inhibitor SU5614
CC       ((3Z)-5-Chloro-3-[(3,5-dimethyl-1H-pyrrol-2-yl)methylene]-1,3-
CC       dihydro-2H-indol-2-one). May be regulated by hydrogen sulfide
CC       (H(2)S) levels via a H(2)S-sensitive intracellular disulfide bond.
CC   -!- SUBUNIT: Homodimer in the presence of bound dimeric VEGFA, VEGFC
CC       or VEGFD ligands; monomeric in the absence of bound ligands. Can
CC       also form heterodimers with FLT1/VEGFR1 and FLT4/VEGFR2. Interacts
CC       (tyrosine phosphorylated) with LFYN, NCK1, PLCG1. Interacts
CC       (tyrosine-phosphorylated active form preferentially) with DAB2IP
CC       (via C2 domain and active form preferentially); the interaction
CC       occurs at the late phase of VEGFA response and inhibits KDR/VEGFR2
CC       activity. Interacts with SHBSH2D2A/TSAD, GRB2, MYOF, CBL and
CC       PDCD6. Interacts with HIV-1 Tat.
CC   -!- INTERACTION:
CC       P46108:CRK; NbExp=2; IntAct=EBI-1005487, EBI-886;
CC       P35916:FLT4; NbExp=5; IntAct=EBI-1005487, EBI-1005467;
CC       P98160:HSPG2; NbExp=4; IntAct=EBI-1005487, EBI-947664;
CC       P08581:MET; NbExp=3; IntAct=EBI-1005487, EBI-1039152;
CC       P16333:NCK1; NbExp=3; IntAct=EBI-1005487, EBI-389883;
CC       O14786:NRP1; NbExp=2; IntAct=EBI-1005487, EBI-1187100;
CC       O75340:PDCD6; NbExp=4; IntAct=EBI-1005487, EBI-352915;
CC       Q12913:PTPRJ; NbExp=4; IntAct=EBI-1005487, EBI-2264500;
CC       P12931:SRC; NbExp=2; IntAct=EBI-1005487, EBI-621482;
CC       P15692:VEGFA; NbExp=2; IntAct=EBI-1005487, EBI-1026643;
CC       P15692-4:VEGFA; NbExp=2; IntAct=EBI-1005487, EBI-1026691;
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein. Cytoplasm. Nucleus. Cytoplasmic vesicle. Early
CC       endosome. Note=Detected on caveolae-enriched lipid rafts at the
CC       cell surface. Is recycled from the plasma membrane to endosomes
CC       and back again. Phosphorylation triggered by VEGFA binding
CC       promotes internalization and subsequent degradation. VEGFA binding
CC       triggers internalization and translocation to the nucleus.
CC   -!- SUBCELLULAR LOCATION: Cell junction (By similarity).
CC       Note=Localized with RAP1A at cell-cell junctions (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Secreted (Probable).
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=mbVegfr-2;
CC         IsoId=P35968-1; Sequence=Displayed;
CC       Name=2; Synonyms=sVegfr-2;
CC         IsoId=P35968-2; Sequence=VSP_041988, VSP_041989;
CC       Name=3; Synonyms=VEGFR2-712;
CC         IsoId=P35968-3; Sequence=VSP_041990, VSP_041991;
CC   -!- TISSUE SPECIFICITY: Detected in cornea (at protein level). Widely
CC       expressed.
CC   -!- DOMAIN: The second and third Ig-like C2-type (immunoglobulin-like)
CC       domains are sufficient for VEGFC binding.
CC   -!- PTM: N-glycosylated.
CC   -!- PTM: Ubiquitinated. Tyrosine phosphorylation of the receptor
CC       promotes its poly-ubiquitination, leading to its degradation via
CC       the proteasome or lysosomal proteases.
CC   -!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
CC       Autophosphorylation occurs in trans, i.e. one subunit of the
CC       dimeric receptor phosphorylates tyrosine residues on the other
CC       subunit. Phosphorylation at Tyr-951 is important for interaction
CC       with SH2D2A/TSAD and VEGFA-mediated reorganization of the actin
CC       cytoskeleton. Phosphorylation at Tyr-1175 is important for
CC       interaction with PLCG1 and SHB. Phosphorylation at Tyr-1214 is
CC       important for interaction with NCK1 and FYN. Dephosphorylated by
CC       PTPRB. Dephosphorylated by PTPRJ at Tyr-951, Tyr-996, Tyr-1054,
CC       Tyr-1059, Tyr-1175 and Tyr-1214.
CC   -!- PTM: The inhibitory disulfide bond between Cys-1024 and Cys-1045
CC       may serve as a specific molecular switch for H(2)S-induced
CC       modification that regulates VEGFR2 function.
CC   -!- DISEASE: Hemangioma, capillary infantile (HCI) [MIM:602089]: A
CC       condition characterized by dull red, firm, dome-shaped
CC       hemangiomas, sharply demarcated from surrounding skin, usually
CC       presenting at birth or occurring within the first two or three
CC       months of life. They result from highly proliferative, localized
CC       growth of capillary endothelium and generally undergo regression
CC       and involution without scarring. Note=Disease susceptibility is
CC       associated with variations affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Note=Plays a major role in tumor angiogenesis. In case of
CC       HIV-1 infection, the interaction with extracellular viral Tat
CC       protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. CSF-1/PDGF receptor subfamily.
CC   -!- SIMILARITY: Contains 7 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; EU826563; ACF47599.1; -; mRNA.
DR   EMBL; FJ899739; ACR78514.1; -; mRNA.
DR   EMBL; AF035121; AAB88005.1; -; mRNA.
DR   EMBL; AF063658; AAC16450.1; -; mRNA.
DR   EMBL; AC021220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC111194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC131822; AAI31823.1; -; mRNA.
DR   EMBL; L04947; AAA59459.1; -; mRNA.
DR   EMBL; X61656; CAA43837.1; -; mRNA.
DR   EMBL; X89776; CAA61916.1; -; Genomic_DNA.
DR   PIR; JC1402; JC1402.
DR   RefSeq; NP_002244.1; NM_002253.2.
DR   UniGene; Hs.479756; -.
DR   PDB; 1VR2; X-ray; 2.40 A; A=806-1171.
DR   PDB; 1Y6A; X-ray; 2.10 A; A=806-1171.
DR   PDB; 1Y6B; X-ray; 2.10 A; A=806-1171.
DR   PDB; 1YWN; X-ray; 1.71 A; A=806-1171.
DR   PDB; 2OH4; X-ray; 2.05 A; A=806-1171.
DR   PDB; 2P2H; X-ray; 1.95 A; A=815-1171.
DR   PDB; 2P2I; X-ray; 2.40 A; A/B=815-1171.
DR   PDB; 2QU5; X-ray; 2.95 A; A=815-1171.
DR   PDB; 2QU6; X-ray; 2.10 A; A/B=815-1171.
DR   PDB; 2RL5; X-ray; 2.65 A; A=815-1171.
DR   PDB; 2X1W; X-ray; 2.70 A; L/M/N/O=120-326.
DR   PDB; 2X1X; X-ray; 3.10 A; R=120-326.
DR   PDB; 2XIR; X-ray; 1.50 A; A=806-1171.
DR   PDB; 3B8Q; X-ray; 2.75 A; A/B=815-1171.
DR   PDB; 3B8R; X-ray; 2.70 A; A/B=815-1171.
DR   PDB; 3BE2; X-ray; 1.75 A; A=815-1171.
DR   PDB; 3C7Q; X-ray; 2.10 A; A=806-1171.
DR   PDB; 3CJF; X-ray; 2.15 A; A=806-1168.
DR   PDB; 3CJG; X-ray; 2.25 A; A=806-1168.
DR   PDB; 3CP9; X-ray; 2.50 A; A/B=815-1171.
DR   PDB; 3CPB; X-ray; 2.70 A; A/B=815-1171.
DR   PDB; 3CPC; X-ray; 2.40 A; A/B=815-1171.
DR   PDB; 3DTW; X-ray; 2.90 A; A/B=815-1171.
DR   PDB; 3EFL; X-ray; 2.20 A; A/B=815-1171.
DR   PDB; 3EWH; X-ray; 1.60 A; A=815-1171.
DR   PDB; 3KVQ; X-ray; 2.70 A; A=657-764.
DR   PDB; 3S35; X-ray; 2.20 A; X=220-338.
DR   PDB; 3S36; X-ray; 3.20 A; X=220-338.
DR   PDB; 3S37; X-ray; 2.70 A; X=220-338.
DR   PDB; 3U6J; X-ray; 2.15 A; A=815-1171.
DR   PDB; 3V2A; X-ray; 3.20 A; R=2-764.
DR   PDB; 3V6B; X-ray; 3.20 A; R=132-548.
DR   PDB; 3VHE; X-ray; 1.55 A; A=811-1169.
DR   PDB; 3VHK; X-ray; 2.49 A; A=806-1171.
DR   PDB; 3VID; X-ray; 2.30 A; A=813-1168.
DR   PDB; 3VNT; X-ray; 1.64 A; A=806-1171.
DR   PDB; 3VO3; X-ray; 1.52 A; A=806-1171.
DR   PDB; 4AG8; X-ray; 1.95 A; A=806-1171.
DR   PDB; 4AGC; X-ray; 2.00 A; A=787-1171.
DR   PDB; 4AGD; X-ray; 2.81 A; A=787-1171.
DR   PDB; 4ASD; X-ray; 2.03 A; A=787-1171.
DR   PDB; 4ASE; X-ray; 1.83 A; A=787-1171.
DR   PDBsum; 1VR2; -.
DR   PDBsum; 1Y6A; -.
DR   PDBsum; 1Y6B; -.
DR   PDBsum; 1YWN; -.
DR   PDBsum; 2OH4; -.
DR   PDBsum; 2P2H; -.
DR   PDBsum; 2P2I; -.
DR   PDBsum; 2QU5; -.
DR   PDBsum; 2QU6; -.
DR   PDBsum; 2RL5; -.
DR   PDBsum; 2X1W; -.
DR   PDBsum; 2X1X; -.
DR   PDBsum; 2XIR; -.
DR   PDBsum; 3B8Q; -.
DR   PDBsum; 3B8R; -.
DR   PDBsum; 3BE2; -.
DR   PDBsum; 3C7Q; -.
DR   PDBsum; 3CJF; -.
DR   PDBsum; 3CJG; -.
DR   PDBsum; 3CP9; -.
DR   PDBsum; 3CPB; -.
DR   PDBsum; 3CPC; -.
DR   PDBsum; 3DTW; -.
DR   PDBsum; 3EFL; -.
DR   PDBsum; 3EWH; -.
DR   PDBsum; 3KVQ; -.
DR   PDBsum; 3S35; -.
DR   PDBsum; 3S36; -.
DR   PDBsum; 3S37; -.
DR   PDBsum; 3U6J; -.
DR   PDBsum; 3V2A; -.
DR   PDBsum; 3V6B; -.
DR   PDBsum; 3VHE; -.
DR   PDBsum; 3VHK; -.
DR   PDBsum; 3VID; -.
DR   PDBsum; 3VNT; -.
DR   PDBsum; 3VO3; -.
DR   PDBsum; 4AG8; -.
DR   PDBsum; 4AGC; -.
DR   PDBsum; 4AGD; -.
DR   PDBsum; 4ASD; -.
DR   PDBsum; 4ASE; -.
DR   ProteinModelPortal; P35968; -.
DR   SMR; P35968; 32-756, 815-1209.
DR   BioGrid; 109992; 29.
DR   DIP; DIP-486N; -.
DR   IntAct; P35968; 19.
DR   MINT; MINT-127732; -.
DR   STRING; 9606.ENSP00000263923; -.
DR   BindingDB; P35968; -.
DR   ChEMBL; CHEMBL2111336; -.
DR   DrugBank; DB00398; Sorafenib.
DR   DrugBank; DB01268; Sunitinib.
DR   GuidetoPHARMACOLOGY; 1813; -.
DR   PhosphoSite; P35968; -.
DR   DMDM; 9087218; -.
DR   PaxDb; P35968; -.
DR   PRIDE; P35968; -.
DR   DNASU; 3791; -.
DR   Ensembl; ENST00000263923; ENSP00000263923; ENSG00000128052. [P35968-1]
DR   GeneID; 3791; -.
DR   KEGG; hsa:3791; -.
DR   UCSC; uc003has.3; human. [P35968-1]
DR   UCSC; uc011bzx.2; human. [P35968-2]
DR   CTD; 3791; -.
DR   GeneCards; GC04M055944; -.
DR   HGNC; HGNC:6307; KDR.
DR   HPA; CAB004028; -.
DR   MIM; 191306; gene.
DR   MIM; 602089; phenotype.
DR   neXtProt; NX_P35968; -.
DR   Orphanet; 91415; Familial capillary hemangioma.
DR   PharmGKB; PA30086; -.
DR   eggNOG; COG0515; -.
DR   HOVERGEN; HBG053432; -.
DR   InParanoid; P35968; -.
DR   KO; K05098; -.
DR   OMA; AGMVFCE; -.
DR   OrthoDB; EOG75F4CC; -.
DR   PhylomeDB; P35968; -.
DR   TreeFam; TF325768; -.
DR   BRENDA; 2.7.10.1; 2681.
DR   Reactome; REACT_111102; Signal Transduction.
DR   Reactome; REACT_118779; Extracellular matrix organization.
DR   SignaLink; P35968; -.
DR   EvolutionaryTrace; P35968; -.
DR   GeneWiki; Kinase_insert_domain_receptor; -.
DR   GenomeRNAi; 3791; -.
DR   NextBio; 14887; -.
DR   PRO; PR:P35968; -.
DR   ArrayExpress; P35968; -.
DR   Bgee; P35968; -.
DR   CleanEx; HS_KDR; -.
DR   Genevestigator; P35968; -.
DR   GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; ISS:BHF-UCL.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051879; F:Hsp90 protein binding; TAS:BHF-UCL.
DR   GO; GO:0004716; F:receptor signaling protein tyrosine kinase activity; TAS:BHF-UCL.
DR   GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; IDA:UniProtKB.
DR   GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
DR   GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IMP:UniProtKB.
DR   GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
DR   GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:BHF-UCL.
DR   GO; GO:0035162; P:embryonic hemopoiesis; ISS:UniProtKB.
DR   GO; GO:0045446; P:endothelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0003158; P:endothelium development; ISS:UniProtKB.
DR   GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR   GO; GO:0001945; P:lymph vessel development; IEA:Ensembl.
DR   GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR   GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISS:BHF-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:BHF-UCL.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR   GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR   GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:BHF-UCL.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:2001214; P:positive regulation of vasculogenesis; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:BHF-UCL.
DR   GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 8.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR   InterPro; IPR009136; VEGFR2_rcpt.
DR   PANTHER; PTHR24416:SF45; PTHR24416:SF45; 1.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF07686; V-set; 1.
DR   PRINTS; PR01834; VEGFRECEPTR2.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 2.
DR   PROSITE; PS50835; IG_LIKE; 5.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Angiogenesis; ATP-binding;
KW   Cell junction; Cell membrane; Complete proteome; Cytoplasm;
KW   Cytoplasmic vesicle; Developmental protein; Differentiation;
KW   Disulfide bond; Endosome; Glycoprotein; Host-virus interaction;
KW   Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
KW   Secreted; Signal; Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase; Ubl conjugation.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20   1356       Vascular endothelial growth factor
FT                                receptor 2.
FT                                /FTId=PRO_0000016771.
FT   TOPO_DOM     20    764       Extracellular (Potential).
FT   TRANSMEM    765    785       Helical; (Potential).
FT   TOPO_DOM    786   1356       Cytoplasmic (Potential).
FT   DOMAIN       46    110       Ig-like C2-type 1.
FT   DOMAIN      141    207       Ig-like C2-type 2.
FT   DOMAIN      224    320       Ig-like C2-type 3.
FT   DOMAIN      328    414       Ig-like C2-type 4.
FT   DOMAIN      421    548       Ig-like C2-type 5.
FT   DOMAIN      551    660       Ig-like C2-type 6.
FT   DOMAIN      667    753       Ig-like C2-type 7.
FT   DOMAIN      834   1162       Protein kinase.
FT   NP_BIND     840    848       ATP (Probable).
FT   ACT_SITE   1028   1028       Proton acceptor (By similarity).
FT   BINDING     868    868       ATP (Probable).
FT   SITE       1175   1175       Interaction with SHB (By similarity).
FT   MOD_RES     801    801       Phosphotyrosine.
FT   MOD_RES     951    951       Phosphotyrosine; by autocatalysis.
FT   MOD_RES     982    982       Phosphoserine.
FT   MOD_RES     984    984       Phosphoserine.
FT   MOD_RES     996    996       Phosphotyrosine; by autocatalysis.
FT   MOD_RES    1054   1054       Phosphotyrosine; by autocatalysis.
FT   MOD_RES    1059   1059       Phosphotyrosine; by autocatalysis.
FT   MOD_RES    1175   1175       Phosphotyrosine; by autocatalysis.
FT   MOD_RES    1214   1214       Phosphotyrosine; by autocatalysis.
FT   MOD_RES    1305   1305       Phosphotyrosine; by autocatalysis.
FT   MOD_RES    1309   1309       Phosphotyrosine; by autocatalysis.
FT   MOD_RES    1319   1319       Phosphotyrosine; by autocatalysis.
FT   CARBOHYD     46     46       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     66     66       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     96     96       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    143    143       N-linked (GlcNAc...).
FT   CARBOHYD    158    158       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    245    245       N-linked (GlcNAc...).
FT   CARBOHYD    318    318       N-linked (GlcNAc...).
FT   CARBOHYD    374    374       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    395    395       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    511    511       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    523    523       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    580    580       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    613    613       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    619    619       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    631    631       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    675    675       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    704    704       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    721    721       N-linked (GlcNAc...) (Potential).
FT   DISULFID     53    103       By similarity.
FT   DISULFID    150    200
FT   DISULFID    246    307
FT   DISULFID    445    530       By similarity.
FT   DISULFID    571    642       By similarity.
FT   DISULFID    688    737       By similarity.
FT   DISULFID   1024   1045       Redox-active.
FT   VAR_SEQ     663    678       ERVAPTITGNLENQTT -> GRETILDHCAEAVGMP (in
FT                                isoform 2).
FT                                /FTId=VSP_041988.
FT   VAR_SEQ     679   1356       Missing (in isoform 2).
FT                                /FTId=VSP_041989.
FT   VAR_SEQ     712    712       G -> E (in isoform 3).
FT                                /FTId=VSP_041990.
FT   VAR_SEQ     713   1356       Missing (in isoform 3).
FT                                /FTId=VSP_041991.
FT   VARIANT       2      2       Q -> R (in a lung adenocarcinoma sample;
FT                                somatic mutation).
FT                                /FTId=VAR_042053.
FT   VARIANT     136    136       V -> M (in dbSNP:rs35636987).
FT                                /FTId=VAR_042054.
FT   VARIANT     248    248       A -> G (in a renal clear cell carcinoma
FT                                sample; somatic mutation).
FT                                /FTId=VAR_042055.
FT   VARIANT     275    275       R -> L (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_036126.
FT   VARIANT     297    297       V -> I (in dbSNP:rs2305948).
FT                                /FTId=VAR_022071.
FT   VARIANT     462    462       L -> V (in dbSNP:rs56286620).
FT                                /FTId=VAR_042056.
FT   VARIANT     472    472       Q -> H (in dbSNP:rs1870377).
FT                                /FTId=VAR_020353.
FT   VARIANT     482    482       C -> R (in HCI susceptibility; expression
FT                                of FLT1 in hemangioma endothelial cells
FT                                is markedly reduced and KDR activity is
FT                                increased compared to controls; low FLT1
FT                                expression in hemangioma cells is caused
FT                                by reduced activity of a pathway
FT                                involving ITGB1, ANTXR1, KDR and
FT                                NFATC2IP; the mutation predicts to result
FT                                in loss-of-function and disruption of the
FT                                normal association of these molecules;
FT                                dbSNP:rs34231037).
FT                                /FTId=VAR_042057.
FT   VARIANT     539    539       G -> R (in dbSNP:rs55716939).
FT                                /FTId=VAR_042058.
FT   VARIANT     689    689       T -> M (in dbSNP:rs34038364).
FT                                /FTId=VAR_042059.
FT   VARIANT     814    814       D -> N (in dbSNP:rs35603373).
FT                                /FTId=VAR_042060.
FT   VARIANT     848    848       V -> E (strongly reduced
FT                                autophosphorylation and kinase activity;
FT                                dbSNP:rs1139776).
FT                                /FTId=VAR_046679.
FT   VARIANT     873    873       G -> R (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_036127.
FT   VARIANT     952    952       V -> I (in dbSNP:rs13129474).
FT                                /FTId=VAR_046680.
FT   VARIANT    1065   1065       A -> T (in dbSNP:rs56302315).
FT                                /FTId=VAR_042061.
FT   VARIANT    1147   1147       P -> S (in HCI; somatic mutation).
FT                                /FTId=VAR_063147.
FT   MUTAGEN     726    726       R->A: Strongly reduced
FT                                autophosphorylation and activation of MAP
FT                                kinases.
FT   MUTAGEN     731    731       D->A: Strongly reduced
FT                                autophosphorylation and activation of MAP
FT                                kinases.
FT   MUTAGEN     801    801       Y->F: Abolishes stimulation of nitric
FT                                oxide synthesis.
FT   MUTAGEN     868    868       K->M: Loss of enzyme activity.
FT   MUTAGEN     951    951       Y->F: Abolishes reorganization of the
FT                                actin cytoskeleton and cell migration in
FT                                response to VEGFA.
FT   MUTAGEN     996    996       Y->F: Strongly reduced
FT                                autophosphorylation. Reduces
FT                                phosphorylation of PLCG1.
FT   MUTAGEN    1045   1045       C->A: Significantly higher kinase
FT                                activity.
FT   MUTAGEN    1054   1054       Y->F: Strongly reduced
FT                                autophosphorylation. Abolishes
FT                                phosphorylation of downstream signaling
FT                                proteins; when associated with F-1059.
FT   MUTAGEN    1059   1059       Y->F: Strongly reduced
FT                                autophosphorylation. Abolishes
FT                                phosphorylation of downstream signaling
FT                                proteins; when associated with F-1054.
FT   MUTAGEN    1175   1175       Y->F: Abolishes phosphorylation of PLCG1
FT                                and MAP kinases in response to VEGFA.
FT   MUTAGEN    1214   1214       Y->F: Loss of phosphorylation site.
FT                                Abolishes reorganization of the actin
FT                                cytoskeleton in response to VEGFA.
FT   CONFLICT      2      2       Q -> E (in Ref. 4; AAC16450).
FT   CONFLICT    772    772       A -> T (in Ref. 7; AAA59459/CAA43837).
FT   CONFLICT    787    787       R -> G (in Ref. 7; AAA59459/CAA43837).
FT   CONFLICT    835    835       K -> N (in Ref. 7; AAA59459/CAA43837).
FT   CONFLICT   1347   1347       S -> T (in Ref. 7; AAA59459/CAA43837).
FT   STRAND      134    138
FT   STRAND      145    148
FT   STRAND      152    154
FT   STRAND      159    164
FT   TURN        165    167
FT   STRAND      168    170
FT   STRAND      174    176
FT   STRAND      178    180
FT   TURN        181    183
FT   STRAND      184    188
FT   HELIX       189    191
FT   TURN        192    194
FT   STRAND      196    202
FT   STRAND      214    218
FT   STRAND      223    230
FT   STRAND      234    238
FT   STRAND      242    250
FT   STRAND      257    261
FT   HELIX       269    272
FT   STRAND      279    282
FT   STRAND      285    296
FT   HELIX       299    301
FT   STRAND      303    310
FT   STRAND      315    328
FT   STRAND      676    679
FT   STRAND      684    687
FT   STRAND      697    706
FT   STRAND      713    716
FT   TURN        717    720
FT   STRAND      721    724
FT   HELIX       729    731
FT   STRAND      733    740
FT   STRAND      746    755
FT   STRAND      804    806
FT   TURN        808    810
FT   TURN        813    815
FT   HELIX       817    819
FT   HELIX       824    827
FT   HELIX       831    833
FT   STRAND      834    842
FT   STRAND      844    858
FT   STRAND      862    870
FT   HELIX       876    892
FT   STRAND      901    905
FT   STRAND      907    910
FT   STRAND      913    917
FT   HELIX       924    929
FT   TURN        930    933
FT   STRAND      934    936
FT   TURN        995    998
FT   HELIX      1002   1021
FT   STRAND     1024   1026
FT   HELIX      1031   1033
FT   STRAND     1034   1036
FT   HELIX      1038   1040
FT   STRAND     1042   1044
FT   HELIX      1048   1050
FT   TURN       1053   1055
FT   STRAND     1059   1062
FT   STRAND     1065   1067
FT   HELIX      1069   1071
FT   HELIX      1074   1079
FT   HELIX      1084   1099
FT   STRAND     1105   1108
FT   HELIX      1113   1121
FT   HELIX      1133   1142
FT   HELIX      1147   1149
FT   HELIX      1153   1167
SQ   SEQUENCE   1356 AA;  151527 MW;  59E7C44B05CFEBB3 CRC64;
     MQSKVLLAVA LWLCVETRAA SVGLPSVSLD LPRLSIQKDI LTIKANTTLQ ITCRGQRDLD
     WLWPNNQSGS EQRVEVTECS DGLFCKTLTI PKVIGNDTGA YKCFYRETDL ASVIYVYVQD
     YRSPFIASVS DQHGVVYITE NKNKTVVIPC LGSISNLNVS LCARYPEKRF VPDGNRISWD
     SKKGFTIPSY MISYAGMVFC EAKINDESYQ SIMYIVVVVG YRIYDVVLSP SHGIELSVGE
     KLVLNCTART ELNVGIDFNW EYPSSKHQHK KLVNRDLKTQ SGSEMKKFLS TLTIDGVTRS
     DQGLYTCAAS SGLMTKKNST FVRVHEKPFV AFGSGMESLV EATVGERVRI PAKYLGYPPP
     EIKWYKNGIP LESNHTIKAG HVLTIMEVSE RDTGNYTVIL TNPISKEKQS HVVSLVVYVP
     PQIGEKSLIS PVDSYQYGTT QTLTCTVYAI PPPHHIHWYW QLEEECANEP SQAVSVTNPY
     PCEEWRSVED FQGGNKIEVN KNQFALIEGK NKTVSTLVIQ AANVSALYKC EAVNKVGRGE
     RVISFHVTRG PEITLQPDMQ PTEQESVSLW CTADRSTFEN LTWYKLGPQP LPIHVGELPT
     PVCKNLDTLW KLNATMFSNS TNDILIMELK NASLQDQGDY VCLAQDRKTK KRHCVVRQLT
     VLERVAPTIT GNLENQTTSI GESIEVSCTA SGNPPPQIMW FKDNETLVED SGIVLKDGNR
     NLTIRRVRKE DEGLYTCQAC SVLGCAKVEA FFIIEGAQEK TNLEIIILVG TAVIAMFFWL
     LLVIILRTVK RANGGELKTG YLSIVMDPDE LPLDEHCERL PYDASKWEFP RDRLKLGKPL
     GRGAFGQVIE ADAFGIDKTA TCRTVAVKML KEGATHSEHR ALMSELKILI HIGHHLNVVN
     LLGACTKPGG PLMVIVEFCK FGNLSTYLRS KRNEFVPYKT KGARFRQGKD YVGAIPVDLK
     RRLDSITSSQ SSASSGFVEE KSLSDVEEEE APEDLYKDFL TLEHLICYSF QVAKGMEFLA
     SRKCIHRDLA ARNILLSEKN VVKICDFGLA RDIYKDPDYV RKGDARLPLK WMAPETIFDR
     VYTIQSDVWS FGVLLWEIFS LGASPYPGVK IDEEFCRRLK EGTRMRAPDY TTPEMYQTML
     DCWHGEPSQR PTFSELVEHL GNLLQANAQQ DGKDYIVLPI SETLSMEEDS GLSLPTSPVS
     CMEEEEVCDP KFHYDNTAGI SQYLQNSKRK SRPVSVKTFE DIPLEEPEVK VIPDDNQTDS
     GMVLASEELK TLEDRTKLSP SFGGMVPSKS RESVASEGSN QTSGYQSGYH SDDTDTTVYS
     SEEAELLKLI EIGVQTGSTA QILQPDSGTT LSSPPV
//
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