VGFR4_DANRE
ID VGFR4_DANRE Reviewed; 1302 AA.
AC Q8AXB3; A1L1P1; B0R127; O42377; P79743; Q8UUW9; Q98891; Q9PTL0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Vascular endothelial growth factor receptor kdr-like;
DE EC=2.7.10.1;
DE AltName: Full=Fetal liver kinase 1;
DE Short=FLK-1;
DE AltName: Full=Kinase insert domain receptor-A;
DE AltName: Full=Kinase insert domain receptor-like;
DE AltName: Full=Protein-tyrosine kinase receptor flk-1;
DE AltName: Full=Vascular endothelial growth factor receptor 4;
DE Short=VEGFR-4;
DE Flags: Precursor;
GN Name=kdrl;
GN Synonyms=flk {ECO:0000312|EMBL:AAB41042.1}, flk-1,
GN flk1 {ECO:0000303|PubMed:12194822}, flka, kdr, kdra, vegfr2, vegfr4, vegr2;
GN ORFNames=si:ch211-276g21.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AAN47136.1};
RN [1] {ECO:0000312|EMBL:AAL16381.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo {ECO:0000269|PubMed:12086862};
RX PubMed=12086862; DOI=10.1016/s1535-6108(02)00042-9;
RA Chan J., Bayliss P.E., Wood J.M., Roberts T.M.;
RT "Dissection of angiogenic signaling in zebrafish using a chemical genetic
RT approach.";
RL Cancer Cell 1:257-267(2002).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=12194822; DOI=10.1016/s0960-9822(02)01044-8;
RA Habeck H., Odenthal J., Walderich B., Maischein H.-M., Schulte-Merker S.;
RT "Analysis of a zebrafish VEGF receptor mutant reveals specific disruption
RT of angiogenesis.";
RL Curr. Biol. 12:1405-1412(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18296487; DOI=10.1101/gr.7187808;
RA Bushell K.M., Soellner C., Schuster-Boeckler B., Bateman A., Wright G.J.;
RT "Large-scale screening for novel low-affinity extracellular protein
RT interactions.";
RL Genome Res. 18:622-630(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 131-1302.
RC TISSUE=Kidney {ECO:0000269|PubMed:9630750};
RX PubMed=9630750; DOI=10.1006/dbio.1998.8887;
RA Thompson M.A., Ransom D.G., Pratt S.J., MacLennan H., Kieran M.W.,
RA Detrich H.W. III, Vail B., Huber T.L., Paw B., Brownlie A.J., Oates A.C.,
RA Fritz A., Gates M.A., Amores A., Bahary N., Talbot W.S., Her H.,
RA Beier D.R., Postlethwait J.H., Zon L.I.;
RT "The cloche and spadetail genes differentially affect hematopoiesis and
RT vasculogenesis.";
RL Dev. Biol. 197:248-269(1998).
RN [7] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 859-1145, AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:9178253};
RX PubMed=9178253; DOI=10.1016/s0925-4773(97)00671-0;
RA Sumoy L., Keasey J.B., Dittman T.D., Kimelman D.;
RT "A role for notochord in axial vascular development revealed by analysis of
RT phenotype and the expression of VEGR-2 in zebrafish flh and ntl mutant
RT embryos.";
RL Mech. Dev. 63:15-27(1997).
RN [8] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 960-1302, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo {ECO:0000269|PubMed:9119113};
RX PubMed=9119113; DOI=10.1006/dbio.1996.8495;
RA Fouquet B., Weinstein B.M., Serluca F.C., Fishman M.C.;
RT "Vessel patterning in the embryo of the zebrafish: guidance by notochord.";
RL Dev. Biol. 183:37-48(1997).
RN [9] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 978-1302, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo {ECO:0000269|PubMed:9053314};
RX PubMed=9053314; DOI=10.1242/dev.124.2.381;
RA Liao W., Bisgrove B.W., Sawyer H., Hug B., Bell B., Peters K.,
RA Grunwald D.J., Stainier D.Y.R.;
RT "The zebrafish gene cloche acts upstream of a flk-1 homologue to regulate
RT endothelial cell differentiation.";
RL Development 124:381-389(1997).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LEU-845.
RX PubMed=16617120; DOI=10.1073/pnas.0506886103;
RA Covassin L.D., Villefranc J.A., Kacergis M.C., Weinstein B.M., Lawson N.D.;
RT "Distinct genetic interactions between multiple Vegf receptors are required
RT for development of different blood vessel types in zebrafish.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6554-6559(2006).
RN [11]
RP FUNCTION, INTERACTION WITH VEGFAA AND VEGFAB, TISSUE SPECIFICITY, AND
RP PHOSPHORYLATION.
RX PubMed=17698971; DOI=10.1182/blood-2006-04-016378;
RA Bahary N., Goishi K., Stuckenholz C., Weber G., Leblanc J., Schafer C.A.,
RA Berman S.S., Klagsbrun M., Zon L.I.;
RT "Duplicate VegfA genes and orthologues of the KDR receptor tyrosine kinase
RT family mediate vascular development in the zebrafish.";
RL Blood 110:3627-3636(2007).
RN [12]
RP TISSUE SPECIFICITY, AND ORTHOLOGY.
RX PubMed=17722983; DOI=10.1371/journal.pgen.0030140;
RA Bussmann J., Bakkers J., Schulte-Merker S.;
RT "Early endocardial morphogenesis requires Scl/Tal1.";
RL PLoS Genet. 3:1425-1437(2007).
RN [13]
RP NOMENCLATURE AND ORTHOLOGY.
RX PubMed=18516225; DOI=10.1371/journal.pgen.1000064;
RA Bussmann J., Lawson N., Zon L., Schulte-Merker S.;
RT "Zebrafish VEGF receptors: a guideline to nomenclature.";
RL PLoS Genet. 4:E1000064-E1000064(2008).
CC -!- FUNCTION: Receptor for VEGF or VEGFC. Has a tyrosine-protein kinase
CC activity. Combinations of multiple VEGF receptors are required for
CC development of different blood vessel types in the embryo. Involved in
CC angiogenesis, specifically in VEGF-induced sprouting of new blood
CC vessels. Particularly involved in artery formation. Does not appear to
CC be required for hematopoiesis. {ECO:0000269|PubMed:12194822,
CC ECO:0000269|PubMed:16617120, ECO:0000269|PubMed:17698971}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:16617120};
CC -!- SUBUNIT: Interacts with isoform VEGF165 of vegfaa and isoform VEGF171
CC of vegfab. {ECO:0000269|PubMed:17698971}.
CC -!- INTERACTION:
CC Q8AXB3; A4JYN2: bcan; NbExp=2; IntAct=EBI-2267980, EBI-2268253;
CC Q8AXB3; Q8UVD6: boc; NbExp=2; IntAct=EBI-2267980, EBI-2268159;
CC Q8AXB3; A8BBB9: epyc; NbExp=2; IntAct=EBI-2267980, EBI-2268109;
CC Q8AXB3; A4JYI8: fgfr2; NbExp=2; IntAct=EBI-2267980, EBI-2268196;
CC Q8AXB3; A4JYQ2: fgfr3; NbExp=2; IntAct=EBI-2267980, EBI-2268403;
CC Q8AXB3; Q6NW92: igfbp7; NbExp=2; IntAct=EBI-2267980, EBI-1579483;
CC Q8AXB3; Q6NZ26: igsf8; NbExp=2; IntAct=EBI-2267980, EBI-2268334;
CC Q8AXB3; A8BBG3: lrrtm1; NbExp=2; IntAct=EBI-2267980, EBI-2263357;
CC Q8AXB3; A8BB40: lrrtm4l1; NbExp=2; IntAct=EBI-2267980, EBI-2263384;
CC Q8AXB3; A8BBE6: optc; NbExp=2; IntAct=EBI-2267980, EBI-2268084;
CC Q8AXB3; Q6P5M1: pdgfrl; NbExp=2; IntAct=EBI-2267980, EBI-2268346;
CC Q8AXB3; Q90Z69: robo3; NbExp=4; IntAct=EBI-2267980, EBI-2267985;
CC Q8AXB3; A4JYE7: vstm4b; NbExp=2; IntAct=EBI-2267980, EBI-2268137;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: First expressed in embryos between 5- and 7-
CC somites. At 7 somites, expressed in discrete bilateral stripes both
CC anteriorly and posteriorly, and in a transverse ectodermal stripe in
CC the hindbrain. From 7-somites, expression seems to extend caudally from
CC the head, and in both directions in the trunk region, until by 20-
CC somites, expression is detected as a continuous band from the anterior
CC head region to the tailbud. Concurrently, cells expressing kdrl in the
CC mid- and posterior trunk regions converge medially. By 24 hours post-
CC fertilization (hpf), expressed in all the endothelial cells lining the
CC vasculature. {ECO:0000269|PubMed:17698971, ECO:0000269|PubMed:17722983,
CC ECO:0000269|PubMed:9053314, ECO:0000269|PubMed:9119113,
CC ECO:0000269|PubMed:9178253}.
CC -!- PTM: Phosphorylated and activated by vegfaa and vegfab.
CC {ECO:0000269|PubMed:17698971}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- CAUTION: Was originally thought to be an ortholog of KDR, but
CC PubMed:18516225 has shown that it represents a fourth vertebrate
CC vascular endothelial growth factor receptor (VEGFR) that is not present
CC in eutherian mammals (marsupials and placental mammals). {ECO:0000305}.
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DR EMBL; AY056466; AAL16381.1; -; mRNA.
DR EMBL; AF487829; AAN47136.1; -; mRNA.
DR EMBL; CU458916; CAM73177.1; -; mRNA.
DR EMBL; AL935131; CAQ13438.1; -; Genomic_DNA.
DR EMBL; BC129158; AAI29159.1; -; mRNA.
DR EMBL; AF180354; AAF03237.1; -; mRNA.
DR EMBL; U89515; AAB62405.1; -; mRNA.
DR EMBL; U82383; AAB41042.1; -; mRNA.
DR EMBL; U75995; AAB18415.1; -; mRNA.
DR RefSeq; NP_571547.1; NM_131472.1.
DR AlphaFoldDB; Q8AXB3; -.
DR SMR; Q8AXB3; -.
DR IntAct; Q8AXB3; 16.
DR STRING; 7955.ENSDARP00000007209; -.
DR PaxDb; Q8AXB3; -.
DR GeneID; 796537; -.
DR KEGG; dre:796537; -.
DR CTD; 796537; -.
DR ZFIN; ZDB-GENE-000705-1; kdrl.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; Q8AXB3; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; Q8AXB3; -.
DR Reactome; R-DRE-194306; Neurophilin interactions with VEGF and VEGFR.
DR Reactome; R-DRE-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR Reactome; R-DRE-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DRE-5218921; VEGFR2 mediated cell proliferation.
DR SignaLink; Q8AXB3; -.
DR PRO; PR:Q8AXB3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0048844; P:artery morphogenesis; IMP:ZFIN.
DR GO; GO:0001568; P:blood vessel development; IMP:ZFIN.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:ZFIN.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0002040; P:sprouting angiogenesis; IGI:ZFIN.
DR GO; GO:0030878; P:thyroid gland development; IMP:ZFIN.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 6.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR041348; VEGFR-2_TMD.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF17988; VEGFR-2_TMD; 1.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 6.
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 Angiogenesis; ATP-binding; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1302
FT /note="Vascular endothelial growth factor receptor kdr-
FT like"
FT /id="PRO_0000016775"
FT TOPO_DOM 29..740
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 762..1302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..115
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000305"
FT DOMAIN 143..206
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000305"
FT DOMAIN 222..318
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000305"
FT DOMAIN 326..412
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000305"
FT DOMAIN 419..542
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000305"
FT DOMAIN 545..636
FT /note="Ig-like C2-type 6"
FT /evidence="ECO:0000305"
FT DOMAIN 643..728
FT /note="Ig-like C2-type 7"
FT /evidence="ECO:0000305"
FT DOMAIN 809..1139
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 1159..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1003
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 815..823
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17948,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 843
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17948,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1029
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1034
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1150
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 55..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 150..199
FT /evidence="ECO:0000250|UniProtKB:P17948,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 243..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 444..524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 565..618
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 664..712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 845
FT /note="L->R: In y17; abolishes kinase activity and causes
FT specific defects in artery development."
FT /evidence="ECO:0000269|PubMed:16617120"
FT CONFLICT 10
FT /note="A -> G (in Ref. 3; CAM73177)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="G -> E (in Ref. 1; AAL16381)"
FT /evidence="ECO:0000305"
FT CONFLICT 240..243
FT /note="ILNC -> HPSTA (in Ref. 6; AAF03237)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="R -> W (in Ref. 6; AAF03237)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="T -> P (in Ref. 1; AAL16381)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="Missing (in Ref. 1; AAL16381)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="H -> Y (in Ref. 1; AAL16381)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="K -> N (in Ref. 1; AAL16381, 3; CAM73177, 5;
FT AAI29159 and 6; AAF03237)"
FT /evidence="ECO:0000305"
FT CONFLICT 1203
FT /note="L -> R (in Ref. 9; AAB18415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1302 AA; 146950 MW; EB18BDCCB6F5430B CRC64;
MTPLKTSVKA FFTLHVLFSC ISHGLVEGSR LPDPQLLPDG DTHLQHVGGT LTLICRGSTA
LHWRLASRNV SSVRIESCEE RLHKHCSKLV IHNLRHNDTG IYSCSHKKSS DHEVSTYVFV
KDPHHPFVEA YSLPHPLFAY RNDPYFVVPC RTTYPNQNVI LETQMNPMAD DVKRGVQWDP
KKGFTVPLKP YDSYHLITCL TRVDNAEFSS VYLLKRLTME IKNLAIEPER PRVLVGDTLI
LNCSAETTYN GRIHFEWEFH KERINRTHHF STTPVQLAQI MVMSKALIVP NVTMEDKGTY
TCTGSIEFKK LQMSTKVIVY EHPFLNVTHN KRKFTSTVEG RRVQFEPRVN AVPAPDRVLW
YKDGVAISEN STCYETAGYN LTIKQVRQKD AGIFTIALSN QERGLYRNIS YKLEVRVKPK
IFEEDVAPAG PQTFRYDQRH KLTCTAFGIP MPNITWFWQP CDPSANLTEC KLYTDPLPIE
NVDDHFPQNP IKDVNSKVGL LKSKNRTIST LVVKTANVSG VYSCTARNEL GNRTMRIPFY
VDDHPQPFEI EPSTAVAGDD ITLTCRGTRY LYDRLTWYDP LGHKVPKDET TLRIEPYTIS
LSIKLPNVSR NHTLGYECQA LKINTNKVVN VTSALTIDER QGPWLMQNLT NQDVNSSSTL
TLACLAYGVP APFITWYKDK TPVTEGPGIT LKDDGTLIIE RVKKDDEGIY ECRASNDGGE
AKTSAVITVV GEDGKPNIEV IILVSTGAAA TFLWIMLILF IRKLRKPSSA DLKTGYLSII
MDPEQMPLDE QCDRLPYDSN KWEFPQDRLR LGKTLGHGAF GKVVEASAFG IDKISTCKTV
AVKMLKVGAT NNEWRALMSE LKILIHIGHH LNVVNLLGAC TKRGGPLMII VEFCKYGNLS
NYLRSKRGDF VVYKSQDGKA VRSSSGCDLS ELIKRRLESV ASTGSSASSG FIEDKSYCDS
EEEEEEQEDL YKKVLTLEDL ICYSFQVAKG MEFLASRKCI HRDLAARNIL LSENNVVKIC
DFGLARDVYK DPDYVRKGDA RLPLKWMAPE AIFDKIYTTQ SDVWSFGVLM WEIFSLGASP
YPGLHIDEEF CCRLKEGTRM KAPEYSSSEI YQTMLDCWHG EPSQRPTFTE LVERLGDLLQ
ASVQQEGKHY IPINTALLTK ADPSNQSPTE ETSTRPVSLR DSGTAWNIKI RPESVKTFDE
VILENGTNKI HEGGQSDSGI GLSSDDLKTL KRLESLARPR SFMSRAMKRK SKESVLLEGE
MDKYPPLVPS LSLEDSSLDS EMECHSPPPD YNYVVRYSTP PV
