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Vascular endothelial growth factor receptor 3 (VEGFR-3) (EC 2.7.10.1) (Fms-like tyrosine kinase 4) (FLT-4) (Tyrosine-protein kinase receptor FLT4)

 VGFR3_HUMAN             Reviewed;        1363 AA.
P35916; A8K6L4; B5A926; Q16067; Q86W07; Q86W08;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
16-NOV-2011, sequence version 3.
22-NOV-2017, entry version 198.
RecName: Full=Vascular endothelial growth factor receptor 3;
Short=VEGFR-3;
EC=2.7.10.1;
AltName: Full=Fms-like tyrosine kinase 4;
Short=FLT-4;
AltName: Full=Tyrosine-protein kinase receptor FLT4;
Flags: Precursor;
Name=FLT4; Synonyms=VEGFR3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=1327515;
Pajusola K., Aprelikova O., Korhonen J., Kaipainen A., Pertovaara L.,
Alitalo R., Alitalo K.;
"FLT4 receptor tyrosine kinase contains seven immunoglobulin-like
loops and is expressed in multiple human tissues and cell lines.";
Cancer Res. 52:5738-5743(1992).
[2]
ERRATUM.
Pajusola K., Aprelikova O., Korhonen J., Kaipainen A., Pertovaara L.,
Alitalo R., Alitalo K.;
Cancer Res. 53:3845-3845(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1319394; DOI=10.1016/0888-7543(92)90277-Y;
Galland F., Karamysheva A., Mattei M.-G., Rosnet O., Marchetto S.,
Birnbaum D.;
"Chromosomal localization of FLT4, a novel receptor-type tyrosine
kinase gene.";
Genomics 13:475-478(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS GLN-890 AND
HIS-1146.
TISSUE=Placenta;
PubMed=8386825;
Galland F., Karamysheva A., Pebusque M.-J., Borg J.-P., Rottapel R.,
Dubreuil P., Rosnet O., Birnbaum D.;
"The FLT4 gene encodes a transmembrane tyrosine kinase related to the
vascular endothelial growth factor receptor.";
Oncogene 8:1233-1240(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH VEGFC,
PHOSPHORYLATION, AND FUNCTION IN CELL PROLIFERATION.
PubMed=8700872; DOI=10.1073/pnas.93.5.1988;
Lee J., Gray A., Yuan J., Luoh S.-M., Avraham H., Wood W.I.;
"Vascular endothelial growth factor-related protein: a ligand and
specific activator of the tyrosine kinase receptor Flt4.";
Proc. Natl. Acad. Sci. U.S.A. 93:1988-1992(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH VEGFD, AND
SUBCELLULAR LOCATION.
PubMed=18593464; DOI=10.1186/ar2447;
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
"Novel splice variants derived from the receptor tyrosine kinase
superfamily are potential therapeutics for rheumatoid arthritis.";
Arthritis Res. Ther. 10:R73-R73(2008).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS GLN-890
AND HIS-1146.
Lian Z., Feitelson M.;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
GLN-890.
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 761-1190.
PubMed=1310071;
Aprelikova O., Pajusola K., Partanen J., Armstrong E., Alitalo R.,
Bailey S.K., McMahon J., Wasmuth J., Huebner K., Alitalo K.;
"FLT4, a novel class III receptor tyrosine kinase in chromosome 5q33-
qter.";
Cancer Res. 52:746-748(1992).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 1293-1363 (ISOFORM 1), AND ALTERNATIVE
SPLICING.
PubMed=7692369;
Pajusola K., Aprelikova O., Armstrong E., Morris S., Alitalo K.;
"Two human FLT4 receptor tyrosine kinase isoforms with distinct
carboxy terminal tails are produced by alternative processing of
primary transcripts.";
Oncogene 8:2931-2937(1993).
[12]
PROTEIN SEQUENCE OF 25-39.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[13]
CATALYTIC ACTIVITY, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=7898938;
Borg J.P., deLapeyriere O., Noguchi T., Rottapel R., Dubreuil P.,
Birnbaum D.;
"Biochemical characterization of two isoforms of FLT4, a VEGF
receptor-related tyrosine kinase.";
Oncogene 10:973-984(1995).
[14]
FUNCTION IN CELL PROLIFERATION AND PHOSPHORYLATION OF SHC1,
CHARACTERIZATION OF ISOFORM 1 AND ISOFORM 2, INTERACTION WITH SHC1 AND
GRB2, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-1333; TYR-1337 AND
TYR-1363, AND TISSUE SPECIFICITY.
PubMed=7675451;
Fournier E., Dubreuil P., Birnbaum D., Borg J.P.;
"Mutation at tyrosine residue 1337 abrogates ligand-dependent
transforming capacity of the FLT4 receptor.";
Oncogene 11:921-931(1995).
[15]
INTERACTION WITH VEGFD, FUNCTION AS VEGFD RECEPTOR, AND
AUTOPHOSPHORYLATION.
PubMed=9435229; DOI=10.1073/pnas.95.2.548;
Achen M.G., Jeltsch M., Kukk E., Maekinen T., Vitali A., Wilks A.F.,
Alitalo K., Stacker S.A.;
"Vascular endothelial growth factor D (VEGF-D) is a ligand for the
tyrosine kinases VEGF receptor 2 (Flk1) and VEGF receptor 3 (Flt4).";
Proc. Natl. Acad. Sci. U.S.A. 95:548-553(1998).
[16]
FUNCTION AS RECEPTOR FOR VEGFC AND VEGFD IN CELL SURVIVAL;
PROLIFERATION AND MIGRATION, AND FUNCTION IN ACTIVATION OF PROTEIN
KINASE C; AKT1; PIK3R1; MAPK1/ERK2 AND MAPK3/ERK1.
PubMed=11532940; DOI=10.1093/emboj/20.17.4762;
Makinen T., Veikkola T., Mustjoki S., Karpanen T., Catimel B.,
Nice E.C., Wise L., Mercer A., Kowalski H., Kerjaschki D.,
Stacker S.A., Achen M.G., Alitalo K.;
"Isolated lymphatic endothelial cells transduce growth, survival and
migratory signals via the VEGF-C/D receptor VEGFR-3.";
EMBO J. 20:4762-4773(2001).
[17]
INTERACTION WITH KDR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION,
CHARACTERIZATION OF VARIANT LMPH1A PRO-1041, MUTAGENESIS OF LYS-879;
TYR-1230; TYR-1231; TYR-1265; TYR-1333; TYR-1337 AND TYR-1363, AND
PHOSPHORYLATION AT TYR-1230; TYR-1231; TYR-1265; TYR-1333; TYR-1337
AND TYR-1363.
PubMed=12881528; DOI=10.1074/jbc.M304499200;
Dixelius J., Makinen T., Wirzenius M., Karkkainen M.J., Wernstedt C.,
Alitalo K., Claesson-Welsh L.;
"Ligand-induced vascular endothelial growth factor receptor-3 (VEGFR-
3) heterodimerization with VEGFR-2 in primary lymphatic endothelial
cells regulates tyrosine phosphorylation sites.";
J. Biol. Chem. 278:40973-40979(2003).
[18]
FUNCTION IN KDR SIGNALING AND IN ANGIOGENESIS, INTERACTION WITH KDR,
AND PHOSPHORYLATION.
PubMed=15474514; DOI=10.1016/j.bbrc.2004.08.237;
Alam A., Herault J.P., Barron P., Favier B., Fons P.,
Delesque-Touchard N., Senegas I., Laboudie P., Bonnin J., Cassan C.,
Savi P., Ruggeri B., Carmeliet P., Bono F., Herbert J.M.;
"Heterodimerization with vascular endothelial growth factor receptor-2
(VEGFR-2) is necessary for VEGFR-3 activity.";
Biochem. Biophys. Res. Commun. 324:909-915(2004).
[19]
FUNCTION IN CELL SURVIVAL, PHOSPHORYLATION IN RESPONSE TO OXIDATIVE
STRESS, INTERACTION WITH PIK3R1; SHC1; GRB2; PTPN11 AND PLCG1, ENZYME
REGULATION BY MAZ51, AND CHARACTERIZATION OF VARIANT LMPH1A ARG-857.
PubMed=15102829; DOI=10.1074/jbc.M314015200;
Wang J.F., Zhang X., Groopman J.E.;
"Activation of vascular endothelial growth factor receptor-3 and its
downstream signaling promote cell survival under oxidative stress.";
J. Biol. Chem. 279:27088-27097(2004).
[20]
FUNCTION IN ACTIVATION OF AKT1; MAPK1/ERK2; MAPK3/ERK1 AND MAPK8,
FUNCTION IN PROMOTING CELL SURVIVAL; PROLIFERATION AND MIGRATION,
CHARACTERIZATION OF ISOFORM 1 AND ISOFORM 2, INTERACTION WITH CRK AND
GRB2, PHOSPHORYLATION AT TYR-1063; TYR-1068; TYR-1230; TYR-1231 AND
TYR-1337, AND MUTAGENESIS OF TYR-1063; TYR-1068; TYR-1230 AND
TYR-1231.
PubMed=16076871; DOI=10.1182/blood-2005-04-1388;
Salameh A., Galvagni F., Bardelli M., Bussolino F., Oliviero S.;
"Direct recruitment of CRK and GRB2 to VEGFR-3 induces proliferation,
migration, and survival of endothelial cells through the activation of
ERK, AKT, and JNK pathways.";
Blood 106:3423-3431(2005).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-527.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[22]
FUNCTION IN PROMOTING CELL SURVIVAL, INTERACTION WITH PTK2/FAK1, AND
SUBCELLULAR LOCATION.
PubMed=16452200; DOI=10.1158/0008-5472.CAN-05-1661;
Garces C.A., Kurenova E.V., Golubovskaya V.M., Cance W.G.;
"Vascular endothelial growth factor receptor-3 and focal adhesion
kinase bind and suppress apoptosis in breast cancer cells.";
Cancer Res. 66:1446-1454(2006).
[23]
FUNCTION IN LYMPHANGIOGENESIS.
PubMed=17210781; DOI=10.1096/fj.06-6656com;
Goldman J., Rutkowski J.M., Shields J.D., Pasquier M.C., Cui Y.,
Schmokel H.G., Willey S., Hicklin D.J., Pytowski B., Swartz M.A.;
"Cooperative and redundant roles of VEGFR-2 and VEGFR-3 signaling in
adult lymphangiogenesis.";
FASEB J. 21:1003-1012(2007).
[24]
ROLE IN CANCER, FUNCTION AS VEGFC RECEPTOR IN TUMOR LYMPHANGIOGENESIS;
CELL PROLIFERATION; CELL SURVIVAL; IN ACTIVATION OF PIK3R1; AKT1 AND
MAP KINASES AND IN UP-REGULATION OF VEGFA AND VEGFC EXPRESSION, ENZYME
REGULATION, AND AUTOPHOSPHORYLATION.
PubMed=19779139; DOI=10.2353/ajpath.2009.081139;
Matsuura M., Onimaru M., Yonemitsu Y., Suzuki H., Nakano T.,
Ishibashi H., Shirasuna K., Sueishi K.;
"Autocrine loop between vascular endothelial growth factor (VEGF)-C
and VEGF receptor-3 positively regulates tumor-associated
lymphangiogenesis in oral squamoid cancer cells.";
Am. J. Pathol. 175:1709-1721(2009).
[25]
ROLE IN CANCER, AND INTERACTION WITH PTK2/FAK1.
PubMed=19610651; DOI=10.1021/jm900159g;
Kurenova E.V., Hunt D.L., He D., Magis A.T., Ostrov D.A., Cance W.G.;
"Small molecule chloropyramine hydrochloride (C4) targets the binding
site of focal adhesion kinase and vascular endothelial growth factor
receptor 3 and suppresses breast cancer growth in vivo.";
J. Med. Chem. 52:4716-4724(2009).
[26]
INTERACTION WITH PTPN14.
PubMed=20826270; DOI=10.1016/j.ajhg.2010.08.008;
Au A.C., Hernandez P.A., Lieber E., Nadroo A.M., Shen Y.M.,
Kelley K.A., Gelb B.D., Diaz G.A.;
"Protein tyrosine phosphatase PTPN14 is a regulator of lymphatic
function and choanal development in humans.";
Am. J. Hum. Genet. 87:436-444(2010).
[27]
PHOSPHORYLATION AT TYR-830; TYR-833; TYR-853; TYR-1063; TYR-1068;
TYR-1333 AND TYR-1337, IDENTIFICATION IN A COMPLEX WITH SRC AND ITGB1,
MUTAGENESIS OF TYR-1063; TYR-1068 AND TYR-1337, ENZYME REGULATION BY
MAZ51, INTERACTION WITH ITGB1; CRK AND SHC1, FUNCTION IN ACTIVATION OF
MAPK8 AND IN REGULATION OF ANGIOGENIC SPROUTING, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=20431062; DOI=10.1161/CIRCRESAHA.109.206326;
Galvagni F., Pennacchini S., Salameh A., Rocchigiani M., Neri F.,
Orlandini M., Petraglia F., Gotta S., Sardone G.L., Matteucci G.,
Terstappen G.C., Oliviero S.;
"Endothelial cell adhesion to the extracellular matrix induces c-Src-
dependent VEGFR-3 phosphorylation without the activation of the
receptor intrinsic kinase activity.";
Circ. Res. 106:1839-1848(2010).
[28]
INTERACTION WITH KDR, FUNCTION IN MODULATING KDR SIGNALING AND IN
ANGIOGENESIS, AND TISSUE SPECIFICITY.
PubMed=20224550; DOI=10.1038/emboj.2010.30;
Nilsson I., Bahram F., Li X., Gualandi L., Koch S., Jarvius M.,
Soderberg O., Anisimov A., Kholova I., Pytowski B., Baldwin M.,
Yla-Herttuala S., Alitalo K., Kreuger J., Claesson-Welsh L.;
"VEGF receptor 2/-3 heterodimers detected in situ by proximity
ligation on angiogenic sprouts.";
EMBO J. 29:1377-1388(2010).
[29]
FUNCTION IN ACTIVATION OF SIGNALING PATHWAYS, AND SUBCELLULAR
LOCATION.
PubMed=20445537; DOI=10.1038/nature09002;
Wang Y., Nakayama M., Pitulescu M.E., Schmidt T.S., Bochenek M.L.,
Sakakibara A., Adams S., Davy A., Deutsch U., Luthi U., Barberis A.,
Benjamin L.E., Makinen T., Nobes C.D., Adams R.H.;
"Ephrin-B2 controls VEGF-induced angiogenesis and lymphangiogenesis.";
Nature 465:483-486(2010).
[30]
FUNCTION IN LYMPHANGIOGENESIS.
PubMed=21273538; DOI=10.1167/iovs.10-6408;
Yuen D., Pytowski B., Chen L.;
"Combined blockade of VEGFR-2 and VEGFR-3 inhibits inflammatory
lymphangiogenesis in early and middle stages.";
Invest. Ophthalmol. Vis. Sci. 52:2593-2597(2011).
[31]
REVIEW ON STRUCTURE AND FUNCTION.
PubMed=18680722; DOI=10.1016/j.bbrc.2008.07.121;
Roskoski R. Jr.;
"VEGF receptor protein-tyrosine kinases: structure and regulation.";
Biochem. Biophys. Res. Commun. 375:287-291(2008).
[32]
REVIEW ON ROLE IN LYMPHANGIOGENESIS AND CANCER.
PubMed=19230644; DOI=10.1016/j.ceb.2008.12.012;
Lohela M., Bry M., Tammela T., Alitalo K.;
"VEGFs and receptors involved in angiogenesis versus
lymphangiogenesis.";
Curr. Opin. Cell Biol. 21:154-165(2009).
[33]
REVIEW ON LIGAND SPECIFICITY; FUNCTION; STRUCTURE; PHOSPHORYLATION AND
SIGNALING.
PubMed=21711246; DOI=10.1042/BJ20110301;
Koch S., Tugues S., Li X., Gualandi L., Claesson-Welsh L.;
"Signal transduction by vascular endothelial growth factor
receptors.";
Biochem. J. 437:169-183(2011).
[34]
REVIEW ON FUNCTION IN LYMPHANGIOGENESIS AND ROLE IN CANCER.
PubMed=21196198; DOI=10.2741/3715;
Al-Rawi M.A., Jiang W.G.;
"Lymphangiogenesis and cancer metastasis.";
Front. Biosci. 16:723-739(2011).
[35]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 23-229 AND 330-553 IN
COMPLEX WITH VEGFC, GLYCOSYLATION AT ASN-33; ASN-104; ASN-166; ASN-411
AND ASN-515, DISULFIDE BOND, INTERACTION WITH VEGFC, MUTAGENESIS OF
THR-446; LYS-516 AND ARG-737, AUTOPHOSPHORYLATION, HOMODIMER, AND
DOMAIN.
PubMed=23878260; DOI=10.1073/PNAS.1301415110;
Leppanen V.M., Tvorogov D., Kisko K., Prota A.E., Jeltsch M.,
Anisimov A., Markovic-Mueller S., Stuttfeld E., Goldie K.N.,
Ballmer-Hofer K., Alitalo K.;
"Structural and mechanistic insights into VEGF receptor 3 ligand
binding and activation.";
Proc. Natl. Acad. Sci. U.S.A. 110:12960-12965(2013).
[36]
VARIANT LMPH1A LEU-1114.
PubMed=9817924; DOI=10.1093/hmg/7.13.2073;
Ferrell R.E., Levinson K.L., Esman J.H., Kimak M.A., Lawrence E.C.,
Barmada M.M., Finegold D.N.;
"Hereditary lymphedema: evidence for linkage and genetic
heterogeneity.";
Hum. Mol. Genet. 7:2073-2078(1998).
[37]
INVOLVEMENT IN LMPH1A, AND CHARACTERIZATION OF VARIANT LMPH1A
ARG-1035.
PubMed=10856194; DOI=10.1086/303019;
Irrthum A., Karkkainen M.J., Devriendt K., Alitalo K., Vikkula M.;
"Congenital hereditary lymphedema caused by a mutation that
inactivates VEGFR3 tyrosine kinase.";
Am. J. Hum. Genet. 67:295-301(2000).
[38]
VARIANTS LMPH1A ARG-857; PRO-1041; PRO-1044 AND LEU-1114, VARIANT
SER-641, AND CHARACTERIZATION OF VARIANTS.
PubMed=10835628; DOI=10.1038/75997;
Karkkainen M.J., Ferrell R.E., Lawrence E.C., Kimak M.A.,
Levinson K.L., McTigue M.A., Alitalo K., Finegold D.N.;
"Missense mutations interfere with VEGFR-3 signalling in primary
lymphoedema.";
Nat. Genet. 25:153-159(2000).
[39]
VARIANTS HCI SER-954 AND SER-1137, AND VARIANTS ALA-494; GLN-890 AND
HIS-1146.
PubMed=11807987; DOI=10.1002/gcc.10028;
Walter J.W., North P.E., Waner M., Mizeracki A., Blei F.,
Walker J.W.T., Reinisch J.F., Marchuk D.A.;
"Somatic mutation of vascular endothelial growth factor receptors in
juvenile hemangioma.";
Genes Chromosomes Cancer 33:295-303(2002).
[40]
VARIANTS LMPH1A MET-878; THR-1086 AND PHE-1108 DEL, VARIANT GLN-1035,
AND INVOLVEMENT IN LMPH1A.
PubMed=16965327; DOI=10.1111/j.1399-0004.2006.00687.x;
Ghalamkarpour A., Morlot S., Raas-Rothschild A., Utkus A.,
Mulliken J.B., Boon L.M., Vikkula M.;
"Hereditary lymphedema type I associated with VEGFR3 mutation: the
first de novo case and atypical presentations.";
Clin. Genet. 70:330-335(2006).
[41]
VARIANT LMPH1A LYS-1106, AND INVOLVEMENT IN LMPH1A.
PubMed=16924388; DOI=10.1007/s10038-006-0031-3;
Spiegel R., Ghalamkarpour A., Daniel-Spiegel E., Vikkula M.,
Shalev S.A.;
"Wide clinical spectrum in a family with hereditary lymphedema type I
due to a novel missense mutation in VEGFR3.";
J. Hum. Genet. 51:846-850(2006).
[42]
VARIANT LMPH1A LEU-1020.
PubMed=17458866; DOI=10.1002/ajmg.a.31703;
Butler M.G., Dagenais S.L., Rockson S.G., Glover T.W.;
"A novel VEGFR3 mutation causes Milroy disease.";
Am. J. Med. Genet. A 143A:1212-1217(2007).
[43]
VARIANTS [LARGE SCALE ANALYSIS] ASP-149; CYS-378; ALA-494; SER-527;
SER-641; TYR-868; ILE-1010; GLN-1031; ASN-1049; GLN-1075 AND HIS-1146.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[44]
VARIANT LMPH1A THR-855, AND CHARACTERIZATION OF VARIANT LMPH1A
THR-855.
PubMed=19289394; DOI=10.1136/jmg.2008.064469;
Ghalamkarpour A., Holnthoner W., Saharinen P., Boon L.M.,
Mulliken J.B., Alitalo K., Vikkula M.;
"Recessive primary congenital lymphoedema caused by a VEGFR3
mutation.";
J. Med. Genet. 46:399-404(2009).
[45]
VARIANT LMPH1A CYS-1235.
PubMed=26091405; DOI=10.1089/lrb.2014.0044;
Melikhan-Revzin S., Kurolap A., Dagan E., Mory A., Gershoni-Baruch R.;
"A novel missense mutation in FLT4 causes autosomal recessive
hereditary lymphedema.";
Lymphat. Res. Biol. 13:107-111(2015).
-!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface
receptor for VEGFC and VEGFD, and plays an essential role in adult
lymphangiogenesis and in the development of the vascular network
and the cardiovascular system during embryonic development.
Promotes proliferation, survival and migration of endothelial
cells, and regulates angiogenic sprouting. Signaling by activated
FLT4 leads to enhanced production of VEGFC, and to a lesser degree
VEGFA, thereby creating a positive feedback loop that enhances
FLT4 signaling. Modulates KDR signaling by forming heterodimers.
The secreted isoform 3 may function as a decoy receptor for VEGFC
and/or VEGFD and play an important role as a negative regulator of
VEGFC-mediated lymphangiogenesis and angiogenesis. Binding of
vascular growth factors to isoform 1 or isoform 2 leads to the
activation of several signaling cascades; isoform 2 seems to be
less efficient in signal transduction, because it has a truncated
C-terminus and therefore lacks several phosphorylation sites.
Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling
pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1
signaling pathway. Phosphorylates SHC1. Mediates phosphorylation
of PIK3R1, the regulatory subunit of phosphatidylinositol 3-
kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-
185', and of AKT1 at 'Ser-473'. {ECO:0000269|PubMed:11532940,
ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:15474514,
ECO:0000269|PubMed:16076871, ECO:0000269|PubMed:16452200,
ECO:0000269|PubMed:17210781, ECO:0000269|PubMed:19610651,
ECO:0000269|PubMed:19779139, ECO:0000269|PubMed:20224550,
ECO:0000269|PubMed:20431062, ECO:0000269|PubMed:20445537,
ECO:0000269|PubMed:21273538, ECO:0000269|PubMed:7675451,
ECO:0000269|PubMed:8700872, ECO:0000269|PubMed:9435229}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:12881528,
ECO:0000269|PubMed:7898938}.
-!- ENZYME REGULATION: Present in an inactive conformation in the
absence of bound ligand. Binding of VEGFC or VEGFD leads to
dimerization and activation by autophosphorylation on tyrosine
residues. Inhibited by MAZ51. {ECO:0000269|PubMed:15102829,
ECO:0000269|PubMed:19779139, ECO:0000269|PubMed:20431062}.
-!- SUBUNIT: Interacts with VEGFC and VEGFD. Monomer in the absence of
bound VEGFC or VEGFD. Homodimer in the presence of bound VEGFC or
VEGFD. Can also form a heterodimer with KDR. Interacts with
PTPN14; the interaction is enhanced by stimulation with VEGFC.
Interacts with CRK, GRB2, PTK2/FAK1, SHC1, PIK3R1 and PTPN11/SHP-
2. Identified in a complex with SRC and ITGB1.
{ECO:0000269|PubMed:12881528, ECO:0000269|PubMed:15102829,
ECO:0000269|PubMed:15474514, ECO:0000269|PubMed:16076871,
ECO:0000269|PubMed:16452200, ECO:0000269|PubMed:18593464,
ECO:0000269|PubMed:19610651, ECO:0000269|PubMed:20224550,
ECO:0000269|PubMed:20431062, ECO:0000269|PubMed:20826270,
ECO:0000269|PubMed:23878260, ECO:0000269|PubMed:7675451,
ECO:0000269|PubMed:8700872, ECO:0000269|PubMed:9435229}.
-!- INTERACTION:
P08238:HSP90AB1; NbExp=2; IntAct=EBI-1005467, EBI-352572;
P35968:KDR; NbExp=5; IntAct=EBI-1005467, EBI-1005487;
P49767:VEGFC; NbExp=2; IntAct=EBI-1005467, EBI-3405539;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20445537,
ECO:0000269|PubMed:7898938}; Single-pass type I membrane protein.
Cytoplasm {ECO:0000269|PubMed:16452200,
ECO:0000269|PubMed:20445537}. Nucleus
{ECO:0000269|PubMed:16452200}. Note=Ligand-mediated
autophosphorylation leads to rapid internalization.
{ECO:0000269|PubMed:20445537}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein. Note=Ligand-mediated autophosphorylation leads
to rapid internalization.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted. Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Long;
IsoId=P35916-2; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P35916-1; Sequence=VSP_041995;
Name=3; Synonyms=sVegfr3;
IsoId=P35916-3; Sequence=VSP_041993, VSP_041994;
-!- TISSUE SPECIFICITY: Detected in endothelial cells (at protein
level). Widely expressed. Detected in fetal spleen, lung and
brain. Detected in adult liver, muscle, thymus, placenta, lung,
testis, ovary, prostate, heart, and kidney.
{ECO:0000269|PubMed:1327515, ECO:0000269|PubMed:20224550,
ECO:0000269|PubMed:7675451}.
-!- DOMAIN: The first and second Ig-like C2-type (immunoglobulin-like)
domains are sufficient for VEGFC binding (PubMed:23878260). The
fourth and fifth Ig-like C2-type domains are sufficient for
homodimerization (PubMed:23878260). The fifth and seventh Ig-like
C2-type domains are required for autophosphorylation and further
activation (PubMed:23878260). {ECO:0000269|PubMed:23878260}.
-!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
Autophosphorylation occurs in trans, i.e. one subunit of the
dimeric receptor phosphorylates tyrosine residues on the other
subunit. Phosphorylation in response to H(2)O(2) is mediated by a
process that requires SRC and PRKCD activity. Phosphorylation at
Tyr-1068 is required for autophosphorylation at additional
tyrosine residues. Phosphorylation at Tyr-1063 and Tyr-1337 is
important for interaction with CRK and subsequent activation of
MAPK8. Phosphorylation at Tyr-1230, Tyr-1231 and Tyr-1337 is
important for interaction with GRB2 and subsequent activation of
the AKT1 and MAPK1/ERK2 and/or MAPK3/ERK1 signaling pathways. In
response to endothelial cell adhesion onto collagen, can also be
phosphorylated in the absence of FLT4 kinase activity by SRC at
Tyr-830, Tyr-833, Tyr-853, Tyr-1063, Tyr-1333, and Tyr-1337.
{ECO:0000269|PubMed:12881528, ECO:0000269|PubMed:15102829,
ECO:0000269|PubMed:15474514, ECO:0000269|PubMed:16076871,
ECO:0000269|PubMed:20431062, ECO:0000269|PubMed:23878260,
ECO:0000269|PubMed:8700872}.
-!- DISEASE: Lymphedema, hereditary, 1A (LMPH1A) [MIM:153100]: A
chronic disabling condition which results in swelling of the
extremities due to altered lymphatic flow. Patients with
lymphedema suffer from recurrent local infections and physical
impairment. {ECO:0000269|PubMed:10835628,
ECO:0000269|PubMed:10856194, ECO:0000269|PubMed:12881528,
ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:16924388,
ECO:0000269|PubMed:16965327, ECO:0000269|PubMed:17458866,
ECO:0000269|PubMed:19289394, ECO:0000269|PubMed:26091405,
ECO:0000269|PubMed:9817924}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Hemangioma, capillary infantile (HCI) [MIM:602089]: A
condition characterized by dull red, firm, dome-shaped
hemangiomas, sharply demarcated from surrounding skin, usually
presenting at birth or occurring within the first two or three
months of life. They result from highly proliferative, localized
growth of capillary endothelium and generally undergo regression
and involution without scarring. {ECO:0000269|PubMed:11807987}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Note=Plays an important role in tumor lymphangiogenesis,
in cancer cell survival, migration, and formation of metastases.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=CAA48290.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=FLT4 entry;
URL="https://en.wikipedia.org/wiki/FLT4";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X69878; CAA49505.1; -; mRNA.
EMBL; U43143; AAA85215.1; -; mRNA.
EMBL; EU826564; ACF47600.1; -; mRNA.
EMBL; AY233382; AAO89504.1; -; mRNA.
EMBL; AY233383; AAO89505.1; -; mRNA.
EMBL; AK291679; BAF84368.1; -; mRNA.
EMBL; AC122714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X68203; CAA48290.1; ALT_INIT; mRNA.
EMBL; S66407; AAB28539.1; -; mRNA.
CCDS; CCDS43412.1; -. [P35916-1]
CCDS; CCDS4457.1; -. [P35916-2]
PIR; A48999; A48999.
RefSeq; NP_002011.2; NM_002020.4. [P35916-1]
RefSeq; NP_891555.2; NM_182925.4. [P35916-2]
UniGene; Hs.646917; -.
PDB; 4BSJ; X-ray; 2.50 A; A=330-553.
PDB; 4BSK; X-ray; 4.20 A; A=23-229.
PDBsum; 4BSJ; -.
PDBsum; 4BSK; -.
ProteinModelPortal; P35916; -.
SMR; P35916; -.
BioGrid; 108612; 28.
CORUM; P35916; -.
DIP; DIP-5739N; -.
IntAct; P35916; 8.
MINT; MINT-1182429; -.
STRING; 9606.ENSP00000261937; -.
BindingDB; P35916; -.
ChEMBL; CHEMBL1955; -.
DrugBank; DB06080; ABT-869.
DrugBank; DB06626; Axitinib.
DrugBank; DB06101; IMC-1C11.
DrugBank; DB09078; Lenvatinib.
DrugBank; DB09079; Nintedanib.
DrugBank; DB06589; Pazopanib.
DrugBank; DB08896; Regorafenib.
DrugBank; DB00398; Sorafenib.
DrugBank; DB01268; Sunitinib.
DrugBank; DB05075; TG100801.
DrugBank; DB04879; Vatalanib.
GuidetoPHARMACOLOGY; 1814; -.
iPTMnet; P35916; -.
PhosphoSitePlus; P35916; -.
BioMuta; FLT4; -.
DMDM; 357529070; -.
PaxDb; P35916; -.
PeptideAtlas; P35916; -.
PRIDE; P35916; -.
DNASU; 2324; -.
Ensembl; ENST00000261937; ENSP00000261937; ENSG00000037280. [P35916-2]
Ensembl; ENST00000393347; ENSP00000377016; ENSG00000037280. [P35916-1]
GeneID; 2324; -.
KEGG; hsa:2324; -.
UCSC; uc003mlz.4; human. [P35916-2]
CTD; 2324; -.
DisGeNET; 2324; -.
EuPathDB; HostDB:ENSG00000037280.15; -.
GeneCards; FLT4; -.
GeneReviews; FLT4; -.
HGNC; HGNC:3767; FLT4.
HPA; CAB000099; -.
MalaCards; FLT4; -.
MIM; 136352; gene.
MIM; 153100; phenotype.
MIM; 602089; phenotype.
neXtProt; NX_P35916; -.
OpenTargets; ENSG00000037280; -.
Orphanet; 79452; Milroy disease.
PharmGKB; PA28183; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000037949; -.
HOVERGEN; HBG053432; -.
InParanoid; P35916; -.
KO; K05097; -.
OMA; PLEEQCE; -.
OrthoDB; EOG091G01TL; -.
PhylomeDB; P35916; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-195399; VEGF binds to VEGFR leading to receptor dimerization.
SignaLink; P35916; -.
SIGNOR; P35916; -.
ChiTaRS; FLT4; human.
GeneWiki; FLT4; -.
GenomeRNAi; 2324; -.
PRO; PR:P35916; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000037280; -.
CleanEx; HS_FLT4; -.
ExpressionAtlas; P35916; baseline and differential.
Genevisible; P35916; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019838; F:growth factor binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IMP:UniProtKB.
GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; IDA:MGI.
GO; GO:0036328; F:VEGF-C-activated receptor activity; IDA:UniProtKB.
GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:UniProtKB.
GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
GO; GO:0001945; P:lymph vessel development; ISS:BHF-UCL.
GO; GO:0001946; P:lymphangiogenesis; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
GO; GO:0090037; P:positive regulation of protein kinase C signaling; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0060312; P:regulation of blood vessel remodeling; ISS:UniProtKB.
GO; GO:0003016; P:respiratory system process; IEA:Ensembl.
GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:MGI.
GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IDA:UniProtKB.
GO; GO:0001944; P:vasculature development; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
InterPro; IPR009137; VEGFR3_rcpt.
PANTHER; PTHR24416:SF49; PTHR24416:SF49; 2.
Pfam; PF07679; I-set; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00409; IG; 6.
SMART; SM00408; IGc2; 4.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 6.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 6.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; ATP-binding;
Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Kinase; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 24 {ECO:0000269|PubMed:15340161}.
CHAIN 25 1363 Vascular endothelial growth factor
receptor 3.
/FTId=PRO_0000016776.
TOPO_DOM 25 775 Extracellular. {ECO:0000255}.
TRANSMEM 776 796 Helical. {ECO:0000255}.
TOPO_DOM 797 1363 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 127 Ig-like C2-type 1.
DOMAIN 151 213 Ig-like C2-type 2.
DOMAIN 219 326 Ig-like C2-type 3.
DOMAIN 331 415 Ig-like C2-type 4.
DOMAIN 422 552 Ig-like C2-type 5.
DOMAIN 555 671 Ig-like C2-type 6.
DOMAIN 678 764 Ig-like C2-type 7.
DOMAIN 845 1173 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 851 859 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 1037 1037 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 879 879 ATP. {ECO:0000305}.
MOD_RES 830 830 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:20431062}.
MOD_RES 833 833 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:20431062}.
MOD_RES 853 853 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:20431062}.
MOD_RES 1063 1063 Phosphotyrosine; by autocatalysis and
SRC. {ECO:0000269|PubMed:16076871,
ECO:0000269|PubMed:20431062}.
MOD_RES 1068 1068 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16076871,
ECO:0000269|PubMed:20431062}.
MOD_RES 1230 1230 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12881528,
ECO:0000269|PubMed:16076871}.
MOD_RES 1231 1231 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12881528,
ECO:0000269|PubMed:16076871}.
MOD_RES 1265 1265 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12881528}.
MOD_RES 1333 1333 Phosphotyrosine; by autocatalysis and
SRC. {ECO:0000269|PubMed:12881528,
ECO:0000269|PubMed:20431062}.
MOD_RES 1337 1337 Phosphotyrosine; by autocatalysis and
SRC. {ECO:0000269|PubMed:12881528,
ECO:0000269|PubMed:16076871,
ECO:0000269|PubMed:20431062}.
MOD_RES 1363 1363 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12881528}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4BSK,
ECO:0000269|PubMed:23878260}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4BSK,
ECO:0000269|PubMed:23878260}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 411 411 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4BSK,
ECO:0000269|PubMed:23878260}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4BSK,
ECO:0000269|PubMed:23878260}.
CARBOHYD 527 527 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 594 594 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 683 683 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 690 690 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 758 758 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 51 111 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:23878260}.
DISULFID 158 206 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:23878260}.
DISULFID 252 310 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 445 534 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:23878260}.
DISULFID 466 486 {ECO:0000269|PubMed:23878260}.
DISULFID 578 653 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 699 751 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 724 765 VDLADSNQKLSIQRVREEDAGRYLCSVCNAKGCVNSSASVA
V -> REGGPGEGQVRRPARPTIPNPGGPAPPPHPLQESTW
RTPTRS (in isoform 3).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_041993.
VAR_SEQ 766 1298 Missing (in isoform 3).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_041994.
VAR_SEQ 1298 1363 SCKGPGQNVAVTRAHPDSQGRRRRPERGARGGQVFYNSEYG
ELSEPSEEDHCSPSARVTFFTDNSY -> R (in
isoform 2). {ECO:0000303|PubMed:1319394,
ECO:0000303|PubMed:1327515,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:8386825,
ECO:0000303|PubMed:8700872,
ECO:0000303|Ref.7}.
/FTId=VSP_041995.
VARIANT 149 149 N -> D (in dbSNP:rs34221241).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042062.
VARIANT 378 378 R -> C (in a renal clear cell carcinoma
sample; somatic mutation;
dbSNP:rs372947534).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042063.
VARIANT 494 494 T -> A (in dbSNP:rs307826).
{ECO:0000269|PubMed:11807987,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_018407.
VARIANT 527 527 N -> S (in dbSNP:rs35874891).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_034379.
VARIANT 641 641 P -> S (in dbSNP:rs55667289).
{ECO:0000269|PubMed:10835628,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_018408.
VARIANT 855 855 A -> T (in LMPH1A; recessive form;
results in reduced autophosphorylation;
results in impaired ligand-induced
receptor internalisation and downstream
signaling; dbSNP:rs121909657).
{ECO:0000269|PubMed:19289394}.
/FTId=VAR_074044.
VARIANT 857 857 G -> R (in LMPH1A; loss of kinase
activity; dbSNP:rs267606818).
{ECO:0000269|PubMed:10835628,
ECO:0000269|PubMed:15102829}.
/FTId=VAR_018409.
VARIANT 868 868 H -> Y (in dbSNP:rs35171798).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042064.
VARIANT 878 878 V -> M (in LMPH1A; dbSNP:rs121909654).
{ECO:0000269|PubMed:16965327}.
/FTId=VAR_074045.
VARIANT 890 890 H -> Q (in dbSNP:rs448012).
{ECO:0000269|PubMed:11807987,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:8386825,
ECO:0000269|Ref.7}.
/FTId=VAR_018410.
VARIANT 954 954 P -> S (in HCI; dbSNP:rs34255532).
{ECO:0000269|PubMed:11807987}.
/FTId=VAR_018411.
VARIANT 1010 1010 T -> I (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042065.
VARIANT 1020 1020 Q -> L (in LMPH1A).
{ECO:0000269|PubMed:17458866}.
/FTId=VAR_074046.
VARIANT 1031 1031 R -> Q (in dbSNP:rs56082504).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042066.
VARIANT 1035 1035 H -> Q (probable disease-associated
mutation found in sporadic congenital
lymphedema; de novo mutation).
{ECO:0000269|PubMed:16965327}.
/FTId=VAR_074047.
VARIANT 1035 1035 H -> R (in LMPH1A; loss of kinase
activity; dbSNP:rs121909653).
{ECO:0000269|PubMed:10856194}.
/FTId=VAR_018412.
VARIANT 1041 1041 R -> P (in LMPH1A; loss of kinase
activity; dbSNP:rs121909650).
{ECO:0000269|PubMed:10835628,
ECO:0000269|PubMed:12881528}.
/FTId=VAR_018413.
VARIANT 1044 1044 L -> P (in LMPH1A; loss of kinase
activity; dbSNP:rs121909651).
{ECO:0000269|PubMed:10835628}.
/FTId=VAR_018414.
VARIANT 1049 1049 D -> N (in dbSNP:rs56310180).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042067.
VARIANT 1075 1075 R -> Q. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_042068.
VARIANT 1086 1086 I -> T (in LMPH1A; dbSNP:rs121909655).
{ECO:0000269|PubMed:16965327}.
/FTId=VAR_074048.
VARIANT 1106 1106 E -> K (in LMPH1A; dbSNP:rs121909656).
{ECO:0000269|PubMed:16924388}.
/FTId=VAR_074049.
VARIANT 1108 1108 Missing (in LMPH1A).
{ECO:0000269|PubMed:16965327}.
/FTId=VAR_074050.
VARIANT 1114 1114 P -> L (in LMPH1A; loss of kinase
activity; dbSNP:rs121909652).
{ECO:0000269|PubMed:10835628,
ECO:0000269|PubMed:9817924}.
/FTId=VAR_018415.
VARIANT 1137 1137 P -> S (in HCI).
{ECO:0000269|PubMed:11807987}.
/FTId=VAR_018416.
VARIANT 1146 1146 R -> H (in dbSNP:rs1130379).
{ECO:0000269|PubMed:11807987,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8386825,
ECO:0000269|Ref.7}.
/FTId=VAR_018417.
VARIANT 1235 1235 S -> C (in LMPH1A; recessive form).
{ECO:0000269|PubMed:26091405}.
/FTId=VAR_074051.
MUTAGEN 446 446 T->E: Decreases autophosphorylation on
tyrosine residues upon ligand binding;
when associated with A-516. Abolishes
autophosphorylation on tyrosine residues
upon ligand binding; when associated with
A-516 and A-737.
{ECO:0000269|PubMed:23878260}.
MUTAGEN 516 516 K->A: Decreases autophosphorylation on
tyrosine residues upon ligand binding;
when associated with E-446. Abolishes
autophosphorylation on tyrosine residues
upon ligand binding; when associated with
E-446 and A-737.
{ECO:0000269|PubMed:23878260}.
MUTAGEN 737 737 R->A: Decreases autophosphorylation on
tyrosine residues upon ligand binding.
Abolishes autophosphorylation on tyrosine
residues upon ligand binding; when
associated with E-446 and A-516.
{ECO:0000269|PubMed:23878260}.
MUTAGEN 879 879 K->G: Abolishes enzyme activity.
{ECO:0000269|PubMed:12881528}.
MUTAGEN 1063 1063 Y->F: Loss of phosphorylation site. No
effect on stimulation of cell
proliferation and cell migration.
{ECO:0000269|PubMed:16076871,
ECO:0000269|PubMed:20431062}.
MUTAGEN 1068 1068 Y->F: Global loss of autophosphorylation.
Abolishes stimulation of cell
proliferation and cell migration.
{ECO:0000269|PubMed:16076871,
ECO:0000269|PubMed:20431062}.
MUTAGEN 1230 1230 Y->F: Loss of phosphorylation site.
Strongly reduces stimulation of cell
proliferation and cell migration.
{ECO:0000269|PubMed:12881528,
ECO:0000269|PubMed:16076871}.
MUTAGEN 1231 1231 Y->F: Loss of phosphorylation site.
Strongly reduces stimulation of cell
proliferation and cell migration.
{ECO:0000269|PubMed:12881528,
ECO:0000269|PubMed:16076871}.
MUTAGEN 1265 1265 Y->F: Loss of phosphorylation site. No
effect on stimulation of cell
proliferation and cell migration.
{ECO:0000269|PubMed:12881528}.
MUTAGEN 1333 1333 Y->F: Loss of phosphorylation site.
Reduced autophosphorylation.
{ECO:0000269|PubMed:12881528,
ECO:0000269|PubMed:7675451}.
MUTAGEN 1337 1337 Y->F: Reduced autophosphorylation.
Strongly reduces stimulation of cell
proliferation and cell migration.
{ECO:0000269|PubMed:12881528,
ECO:0000269|PubMed:20431062,
ECO:0000269|PubMed:7675451}.
MUTAGEN 1363 1363 Y->F: Loss of phosphorylation site.
Slighly reduced autophosphorylation.
{ECO:0000269|PubMed:12881528,
ECO:0000269|PubMed:7675451}.
CONFLICT 24 24 G -> D (in Ref. 3; CAA49505 and 7;
AAO89504/AAO89505). {ECO:0000305}.
CONFLICT 538 538 N -> D (in Ref. 8; BAF84368).
{ECO:0000305}.
CONFLICT 745 745 R -> P (in Ref. 3; CAA49505 and 7;
AAO89504/AAO89505). {ECO:0000305}.
CONFLICT 752 753 NA -> RP (in Ref. 3; CAA49505 and 7;
AAO89504/AAO89505). {ECO:0000305}.
CONFLICT 1128 1128 L -> V (in Ref. 3; CAA49505 and 7;
AAO89504/AAO89505). {ECO:0000305}.
CONFLICT 1164 1164 E -> D (in Ref. 3; CAA49505).
{ECO:0000305}.
STRAND 332 339 {ECO:0000244|PDB:4BSJ}.
STRAND 341 346 {ECO:0000244|PDB:4BSJ}.
STRAND 350 362 {ECO:0000244|PDB:4BSJ}.
STRAND 365 370 {ECO:0000244|PDB:4BSJ}.
STRAND 381 388 {ECO:0000244|PDB:4BSJ}.
HELIX 391 393 {ECO:0000244|PDB:4BSJ}.
STRAND 395 403 {ECO:0000244|PDB:4BSJ}.
TURN 404 407 {ECO:0000244|PDB:4BSJ}.
STRAND 408 424 {ECO:0000244|PDB:4BSJ}.
HELIX 425 428 {ECO:0000244|PDB:4BSJ}.
STRAND 441 451 {ECO:0000244|PDB:4BSJ}.
STRAND 457 464 {ECO:0000244|PDB:4BSJ}.
STRAND 501 511 {ECO:0000244|PDB:4BSJ}.
STRAND 514 524 {ECO:0000244|PDB:4BSJ}.
STRAND 530 538 {ECO:0000244|PDB:4BSJ}.
STRAND 541 549 {ECO:0000244|PDB:4BSJ}.
SEQUENCE 1363 AA; 152757 MW; B1473AAAC95E7E93 CRC64;
MQRGAALCLR LWLCLGLLDG LVSGYSMTPP TLNITEESHV IDTGDSLSIS CRGQHPLEWA
WPGAQEAPAT GDKDSEDTGV VRDCEGTDAR PYCKVLLLHE VHANDTGSYV CYYKYIKARI
EGTTAASSYV FVRDFEQPFI NKPDTLLVNR KDAMWVPCLV SIPGLNVTLR SQSSVLWPDG
QEVVWDDRRG MLVSTPLLHD ALYLQCETTW GDQDFLSNPF LVHITGNELY DIQLLPRKSL
ELLVGEKLVL NCTVWAEFNS GVTFDWDYPG KQAERGKWVP ERRSQQTHTE LSSILTIHNV
SQHDLGSYVC KANNGIQRFR ESTEVIVHEN PFISVEWLKG PILEATAGDE LVKLPVKLAA
YPPPEFQWYK DGKALSGRHS PHALVLKEVT EASTGTYTLA LWNSAAGLRR NISLELVVNV
PPQIHEKEAS SPSIYSRHSR QALTCTAYGV PLPLSIQWHW RPWTPCKMFA QRSLRRRQQQ
DLMPQCRDWR AVTTQDAVNP IESLDTWTEF VEGKNKTVSK LVIQNANVSA MYKCVVSNKV
GQDERLIYFY VTTIPDGFTI ESKPSEELLE GQPVLLSCQA DSYKYEHLRW YRLNLSTLHD
AHGNPLLLDC KNVHLFATPL AASLEEVAPG ARHATLSLSI PRVAPEHEGH YVCEVQDRRS
HDKHCHKKYL SVQALEAPRL TQNLTDLLVN VSDSLEMQCL VAGAHAPSIV WYKDERLLEE
KSGVDLADSN QKLSIQRVRE EDAGRYLCSV CNAKGCVNSS ASVAVEGSED KGSMEIVILV
GTGVIAVFFW VLLLLIFCNM RRPAHADIKT GYLSIIMDPG EVPLEEQCEY LSYDASQWEF
PRERLHLGRV LGYGAFGKVV EASAFGIHKG SSCDTVAVKM LKEGATASEH RALMSELKIL
IHIGNHLNVV NLLGACTKPQ GPLMVIVEFC KYGNLSNFLR AKRDAFSPCA EKSPEQRGRF
RAMVELARLD RRRPGSSDRV LFARFSKTEG GARRASPDQE AEDLWLSPLT MEDLVCYSFQ
VARGMEFLAS RKCIHRDLAA RNILLSESDV VKICDFGLAR DIYKDPDYVR KGSARLPLKW
MAPESIFDKV YTTQSDVWSF GVLLWEIFSL GASPYPGVQI NEEFCQRLRD GTRMRAPELA
TPAIRRIMLN CWSGDPKARP AFSELVEILG DLLQGRGLQE EEEVCMAPRS SQSSEEGSFS
QVSTMALHIA QADAEDSPPS LQRHSLAARY YNWVSFPGCL ARGAETRGSS RMKTFEEFPM
TPTTYKGSVD NQTDSGMVLA SEEFEQIESR HRQESGFSCK GPGQNVAVTR AHPDSQGRRR
RPERGARGGQ VFYNSEYGEL SEPSEEDHCS PSARVTFFTD NSY


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