Receptor domena kinazne insercije (KDR, tip IV receptora tirozin-kinaza), znan i kao receptor 2 vaskularnog endotelnog faktora rasta (VEGFR-2) jest VEGF-receptor koji je kod ljudi kodiran genom KDR sa hromosoma 4. Označava se i kao CD309 (klaster diferencijacije 309) i kao Flk1 (eng. Fetal Liver Kinase 1 = fetusna jetrena kinaza).

KDR
Dostupne strukture
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

1VR2, 1Y6A, 1Y6B, 1YWN, 2M59, 2MET, 2MEU, 2OH4, 2P2H, 2P2I, 2QU5, 2QU6, 2RL5, 2X1W, 2X1X, 2XIR, 3B8Q, 3B8R, 3BE2, 3C7Q, 3CJF, 3CJG, 3CP9, 3CPB, 3CPC, 3DTW, 3EFL, 3EWH, 3KVQ, 3S35, 3S36, 3S37, 3U6J, 3VHE, 3VHK, 3VID, 3VNT, 3VO3, 3WZD, 3WZE, 4AG8, 4AGC, 4AGD, 4ASD, 4ASE, 5EW3

Identifikatori
AliasiKDR
Vanjski ID-jeviOMIM: 191306 MGI: 96683 HomoloGene: 55639 GeneCards: KDR
Lokacija gena (čovjek)
Hromosom 4 (čovjek)
Hrom.Hromosom 4 (čovjek)[1]
Hromosom 4 (čovjek)
Genomska lokacija za KDR
Genomska lokacija za KDR
Bend4q12Početak55,078,481 bp[1]
Kraj55,125,595 bp[1]
Lokacija gena (miš)
Hromosom 5 (miš)
Hrom.Hromosom 5 (miš)[2]
Hromosom 5 (miš)
Genomska lokacija za KDR
Genomska lokacija za KDR
Bend5 C3.3|5 40.23 cMPočetak76,093,487 bp[2]
Kraj76,139,118 bp[2]
Obrazac RNK ekspresije
Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija aktivnost sa transferazom
Hsp90 protein binding
nucleotide binding
protein kinase activity
growth factor binding
vascular endothelial growth factor binding
kinase activity
integrin binding
GO:0001948, GO:0016582 vezivanje za proteine
ATP binding
transmembrane receptor protein tyrosine kinase activity
vascular endothelial growth factor-activated receptor activity
protein tyrosine kinase activity
vezivanje identičnih proteina
Receptorska tirozin-kinaza
transmembrane signaling receptor activity
cadherin binding
Ćelijska komponenta citoplazma
integral component of membrane
Golđijev aparat
membrana
integral component of plasma membrane
extracellular region
međućelijske veze
early endosome
Lipidni splav
sorting endosome
GO:0016023 citoplazmatska vezikula
jedro
endozom
ćelijska membrana
Endoplazmatski retikulum
receptor complex
Biološki proces negative regulation of endothelial cell apoptotic process
Ćelijska diferencijacija
positive regulation of protein phosphorylation
positive regulation of mitochondrial fission
positive regulation of endothelial cell proliferation
Fosforilacija
extracellular matrix organization
negative regulation of apoptotic process
positive regulation of nitric-oxide synthase biosynthetic process
cell migration involved in sprouting angiogenesis
positive regulation of angiogenesis
Vaskulogeneza
positive regulation of endothelial cell migration
multicellular organism development
protein phosphorylation
positive regulation of macroautophagy
positive regulation of mitochondrial depolarization
positive regulation of vasculogenesis
embryonic hemopoiesis
endothelium development
regulation of cell shape
positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway
positive regulation of ERK1 and ERK2 cascade
peptidyl-tyrosine autophosphorylation
protein autophosphorylation
positive regulation of focal adhesion assembly
positive regulation of phosphatidylinositol 3-kinase signaling
peptidyl-tyrosine phosphorylation
cellular response to vascular endothelial growth factor stimulus
GO:0022415 viral process
calcium-mediated signaling using intracellular calcium source
positive regulation of MAPK cascade
positive regulation of positive chemotaxis
transmembrane receptor protein tyrosine kinase signaling pathway
vascular endothelial growth factor receptor signaling pathway
positive regulation of cell population proliferation
Angiogeneza
positive regulation of cell migration
protein kinase B signaling
ERK1 and ERK2 cascade
negative regulation of gene expression
positive regulation of blood vessel endothelial cell migration
cellular response to hydrogen sulfide
positive regulation of cell migration involved in sprouting angiogenesis
negative regulation of signal transduction
sprouting angiogenesis
Ćelijska migracija
endothelial cell differentiation
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez
Ensembl
UniProt
RefSeq (mRNK)

NM_002253

NM_010612
NM_001363216

RefSeq (bjelančevina)

NP_002244

NP_034742
NP_001350145

Lokacija (UCSC)Chr 4: 55.08 – 55.13 MbChr 5: 76.09 – 76.14 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš

Aminokiselinska sekvenca

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Dužina polipeptidnog lanca je 1.356 aminokiselina, а molekulska težina 151.527 Da.[5]

1020304050
MQSKVLLAVALWLCVETRAASVGLPSVSLDLPRLSIQKDILTIKANTTLQ
ITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGA
YKCFYRETDLASVIYVYVQDYRSPFIASVSDQHGVVYITENKNKTVVIPC
LGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFC
EAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTART
ELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRS
DQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRI
PAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVIL
TNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAI
PPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVN
KNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRG
PEITLQPDMQPTEQESVSLWCTADRSTFENLTWYKLGPQPLPIHVGELPT
PVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTK
KRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMW
FKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEA
FFIIEGAQEKTNLEIIILVGTAVIAMFFWLLLVIILRTVKRANGGELKTG
YLSIVMDPDELPLDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIE
ADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVN
LLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYKTKGARFRQGKD
YVGAIPVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEAPEDLYKDFL
TLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLA
RDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFS
LGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQR
PTFSELVEHLGNLLQANAQQDGKDYIVLPISETLSMEEDSGLSLPTSPVS
CMEEEEVCDPKFHYDNTAGISQYLQNSKRKSRPVSVKTFEDIPLEEPEVK
VIPDDNQTDSGMVLASEELKTLEDRTKLSPSFGGMVPSKSRESVASEGSN
QTSGYQSGYHSDDTDTTVYSSEEAELLKLIEIGVQTGSTAQILQPDSGTT
LSSPPV

Funkcija

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Genetička varijanta Q472H zametne linije KDR utiče na fosforilaciju VEGFR-2 i utvrđeno je da je povezana sa gustoćom mikrovaskularnih sudova u karcinomu pluća nemalih ćelija (NSCLC).[6]

Interakcije

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Pokazalo se da receptor domen insercije kinaze ima interakcije sa SHC2,[7] aneksinom A5[8] i SHC1.[9][10]

Također pogledajte

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Reference

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000128052 - Ensembl, maj 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000062960 - Ensembl, maj 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "UniProt, P35968" (jezik: engleski). Pristupljeno 29. 10. 2021.
  6. ^ Glubb DM, Cerri E, Giese A, Zhang W, Mirza O, Thompson EE, Chen P, Das S, Jassem J, Rzyman W, Lingen MW, Salgia R, Hirsch FR, Dziadziuszko R, Ballmer-Hofer K, Innocenti F (august 2011). "Novel functional germline variants in the VEGF receptor 2 gene and their effect on gene expression and microvessel density in lung cancer". Clinical Cancer Research. 17 (16): 5257–67. doi:10.1158/1078-0432.CCR-11-0379. PMC 3156871. PMID 21712447.
  7. ^ Warner AJ, Lopez-Dee J, Knight EL, Feramisco JR, Prigent SA (april 2000). "The Shc-related adaptor protein, Sck, forms a complex with the vascular-endothelial-growth-factor receptor KDR in transfected cells". The Biochemical Journal. 347 (Pt 2): 501–9. doi:10.1042/0264-6021:3470501. PMC 1220983. PMID 10749680.
  8. ^ Wen Y, Edelman JL, Kang T, Sachs G (maj 1999). "Lipocortin V may function as a signaling protein for vascular endothelial growth factor receptor-2/Flk-1". Biochemical and Biophysical Research Communications. 258 (3): 713–21. doi:10.1006/bbrc.1999.0678. PMID 10329451.
  9. ^ Zanetti A, Lampugnani MG, Balconi G, Breviario F, Corada M, Lanfrancone L, Dejana E (april 2002). "Vascular endothelial growth factor induces SHC association with vascular endothelial cadherin: a potential feedback mechanism to control vascular endothelial growth factor receptor-2 signaling". Arteriosclerosis, Thrombosis, and Vascular Biology. 22 (4): 617–22. doi:10.1161/01.ATV.0000012268.84961.AD. PMID 11950700.
  10. ^ D'Angelo G, Martini JF, Iiri T, Fantl WJ, Martial J, Weiner RI (maj 1999). "16K human prolactin inhibits vascular endothelial growth factor-induced activation of Ras in capillary endothelial cells". Molecular Endocrinology. 13 (5): 692–704. doi:10.1210/mend.13.5.0280. PMID 10319320.

Dopunska literatura

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Vanjski linkovi

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Ovaj članak uključuje tekst iz Nacionalne medicinske biblioteke Sjedinjenih Država, koji je u javnom vlasništvu.

Šablon:Transmembranski receptori