Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5MD89

- VGFR3_DANRE

UniProt

Q5MD89 - VGFR3_DANRE

Protein

Vascular endothelial growth factor receptor 3

Gene

flt4

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Feb 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Tyrosine-protein kinase that acts as a cell-surface receptor for vegf or vegfc. Combinations of multiple VEGF receptors are required for development of different blood vessel types in the embryo. Involved in angiogenesis, specifically in VEGF-induced sprouting of new blood vessels, but not required for proper vasculogenesis or hematopoiesis.1 Publication

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei900 – 9001ATPPROSITE-ProRule annotation
    Active sitei1045 – 10451Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi872 – 8809ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. vascular endothelial growth factor-activated receptor activity Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW
    3. vascular endothelial growth factor receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Angiogenesis, Differentiation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vascular endothelial growth factor receptor 3 (EC:2.7.10.1)
    Short name:
    VEGFR-3
    Gene namesi
    Name:flt4
    Synonyms:flt-4, vegfr3
    OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
    Taxonomic identifieri7955 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
    ProteomesiUP000000437: Unplaced

    Organism-specific databases

    ZFINiZDB-GENE-980526-326. flt4.

    Subcellular locationi

    Cell membrane By similarity; Single-pass type I membrane protein By similarity
    Note: Ligand-mediated autophosphorylation leads to rapid internalization.By similarity

    GO - Cellular componenti

    1. integral component of plasma membrane Source: InterPro

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 13571333Vascular endothelial growth factor receptor 3PRO_0000249464Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi51 ↔ 121PROSITE-ProRule annotation
    Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi173 ↔ 225PROSITE-ProRule annotation
    Glycosylationi216 – 2161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi272 ↔ 331PROSITE-ProRule annotation
    Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi473 ↔ 562PROSITE-ProRule annotation
    Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi606 ↔ 674PROSITE-ProRule annotation
    Glycosylationi610 – 6101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi660 – 6601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi707 – 7071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi711 – 7111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi720 ↔ 772PROSITE-ProRule annotation
    Glycosylationi751 – 7511N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1071 – 10711Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1076 – 10761Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1226 – 12261Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1227 – 12271Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1334 – 13341Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1338 – 13381Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    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 By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiQ5MD89.

    Interactioni

    Subunit structurei

    Interacts with vegfc and vegfd. Monomer in the absence of bound vegfc or vegfd. Homodimer in the presence of bound vegfc or vegfd By similarity.By similarity

    Protein-protein interaction databases

    STRINGi7955.ENSDARP00000005480.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5MD89.
    SMRiQ5MD89. Positions 848-1185.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 796772ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini818 – 1357540CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei797 – 81721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 12197Ig-like C2-type 1Add
    BLAST
    Domaini138 – 244107Ig-like C2-type 2Add
    BLAST
    Domaini255 – 34389Ig-like C2-type 3Add
    BLAST
    Domaini352 – 44291Ig-like C2-type 4Add
    BLAST
    Domaini453 – 583131Ig-like C2-type 5Add
    BLAST
    Domaini583 – 690108Ig-like C2-type 6Add
    BLAST
    Domaini699 – 78587Ig-like C2-type 7Add
    BLAST
    Domaini866 – 1181316Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000037949.
    HOVERGENiHBG053432.
    InParanoidiQ5GIT2.
    KOiK05097.
    PhylomeDBiQ5MD89.

    Family and domain databases

    Gene3Di2.60.40.10. 7 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR013106. Ig_V-set.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR001824. Tyr_kinase_rcpt_3_CS.
    IPR009137. VEGFR3_rcpt.
    [Graphical view]
    PANTHERiPTHR24416:SF49. PTHR24416:SF49. 1 hit.
    PfamiPF07679. I-set. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view]
    PRINTSiPR01835. VEGFRECEPTR3.
    SMARTiSM00409. IG. 3 hits.
    SM00408. IGc2. 2 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS50835. IG_LIKE. 5 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5MD89-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRDFTFFCR IWIGIPFFSG LVNGFSMSPP TLDNTKDQLV INANDTLNIT     50
    CRGQRILDWS WPEESLSKVE FTDRQGQQSP TDTPGYREIR LKECQGVAGK 100
    PYCKILILTN AQANDSGYYR CFYKDIKAVI DGTTAASIFV FVRDPEHPFI 150
    KRGDNDMETI FITDSETHIE VPCLVSDPDL KVTLFSLVPY PEPVDGSVVT 200
    WNNKKGWSIP RHIIQNTSTF IGFYCSISVQ NSQHTSSIYV VQVIGLKFYE 250
    FKLFPEDSPV ELMQGESLVL NCTALVDFNT GVDFQWDYPG KKENRLASLQ 300
    PLRNVLDEAT EISSILSIRN IHLDDSGYYT CWANTLEMKR ELTTVVIVHE 350
    KPFISLDYRN GSVIEAKEGQ KSVRLSVKVS AYPSPEIQWY KNGKLISSKN 400
    SSRFKVQQHS LQIRDVCKQD AGEYMLVLKN SPAALEKRLN FTLIVNVPPQ 450
    IHEKEAAPPT NLYGKGTRQI LTCTADGSPP ASISWQWRPW SPCDLERTRR 500
    ALRRRGGRDQ SPFCHNWMDL DPEHAVNPIE SIDTLTQMVD GKEKTVGRVV 550
    IQNASVPAMY KCLAENRVGK DERLIYFYVT TIPEGFDIEM EPSEDPLEQD 600
    LVQLKCNADN FTYENLRWYR LDPQTVPPEL DCKSLHQYAT FLEGQLSFQT 650
    TSNNWVLQLN ITNIQLQDEG NYVCEVQNRR TGVKHCHRKY IPVKAMEAPR 700
    YRHNPTNHTV NVSESLQMNC DVEGTPFPQL SWFKDNQPLH QISGILLQDS 750
    NRTLSIQRVR EEDAGLYTCS ACNQKGCVQS SATVSVIGSD DKTNVEIVIL 800
    IGTGVIAIFF WVLLLVIFCN VKRVNPADIK TGYLSIIMDP GEVPLEEQCE 850
    YLPYDSSQWE ISRDRLRLGK VLGHGAFGKV IEASIFGHDK KSSANTVAVK 900
    MLKEGATASE HKALMSELKI LIHIGNHLNV VNLLGACTKP NGPLMVIVEY 950
    CKYGNLSNFL RAKREFFLPY RDRSPKTQSQ VRRMIEAGQA SQSEHQPSTS 1000
    STNPPRVTVD DLWKTPLTIE DLICYSFQVA RGMEFLASRK CIHRDLAARN 1050
    ILLSENNVVK ICDFGLARDI YKDPDYVRKG NARLPLKWMA PESIFDKVYT 1100
    SQSDVWSFGV LLWEIFSLGA SPYPGIQIDE DFCKRLKDGT RMRAPDNASP 1150
    EIYGIMLACW QGEPRERPTF PALVEILGDL LQENSLPEIP FNVSQSSEDD 1200
    GFSQASSRPP SQEEIRLACN TLPTRYYNCV PFAGCVMVGP SSTCHSRVKT 1250
    FEELPMEMTS HKTQHDSQTD SGMVLASDEL ERFEHKHRGA MLTTATTGQS 1300
    TDRLISCPSV SSSGSGGGLL RPVFFTQLSG QTFYNNEYGH LSEEGVSDYF 1350
    SSSDQAV 1357
    Length:1,357
    Mass (Da):153,178
    Last modified:February 1, 2005 - v1
    Checksum:iD68C197828BE278E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti567 – 5671R → K in AAS92272. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY524001 mRNA. Translation: AAS92272.1.
    AY833404 mRNA. Translation: AAV93318.1.
    RefSeqiNP_571020.1. NM_130945.1.
    UniGeneiDr.81298.

    Genome annotation databases

    GeneIDi30121.
    KEGGidre:30121.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY524001 mRNA. Translation: AAS92272.1 .
    AY833404 mRNA. Translation: AAV93318.1 .
    RefSeqi NP_571020.1. NM_130945.1.
    UniGenei Dr.81298.

    3D structure databases

    ProteinModelPortali Q5MD89.
    SMRi Q5MD89. Positions 848-1185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7955.ENSDARP00000005480.

    Proteomic databases

    PRIDEi Q5MD89.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 30121.
    KEGGi dre:30121.

    Organism-specific databases

    CTDi 2324.
    ZFINi ZDB-GENE-980526-326. flt4.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000037949.
    HOVERGENi HBG053432.
    InParanoidi Q5GIT2.
    KOi K05097.
    PhylomeDBi Q5MD89.

    Miscellaneous databases

    NextBioi 20806600.
    PROi Q5MD89.

    Family and domain databases

    Gene3Di 2.60.40.10. 7 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR013106. Ig_V-set.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR001824. Tyr_kinase_rcpt_3_CS.
    IPR009137. VEGFR3_rcpt.
    [Graphical view ]
    PANTHERi PTHR24416:SF49. PTHR24416:SF49. 1 hit.
    Pfami PF07679. I-set. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view ]
    PRINTSi PR01835. VEGFRECEPTR3.
    SMARTi SM00409. IG. 3 hits.
    SM00408. IGc2. 2 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS50835. IG_LIKE. 5 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Synergistic signaling of vegf receptors is required for vasculogenesis in zebrafish."
      Habeck H., Langhoff J., Vogel A.M., Trowe T., Koblizek T.I., Schulte-Merker S.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Distinct genetic interactions between multiple Vegf receptors are required for development of different blood vessel types in zebrafish."
      Covassin L.D., Villefranc J.A., Kacergis M.C., Weinstein B.M., Lawson N.D.
      Proc. Natl. Acad. Sci. U.S.A. 103:6554-6559(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.

    Entry informationi

    Entry nameiVGFR3_DANRE
    AccessioniPrimary (citable) accession number: Q5MD89
    Secondary accession number(s): Q5GIT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3