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FLT1

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FLT1
Dostupne strukture
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

1FLT, 1QSV, 1QSZ, 1QTY, 1RV6, 2XAC, 3HNG, 4CKV, 4CL7, 5EX3

Identifikatori
AliasiFLT1
Vanjski ID-jeviOMIM: 165070 MGI: 95558 HomoloGene: 134179 GeneCards: FLT1
Lokacija gena (čovjek)
Hromosom 13 (čovjek)
Hrom.Hromosom 13 (čovjek)[1]
Hromosom 13 (čovjek)
Genomska lokacija za FLT1
Genomska lokacija za FLT1
Bend13q12.3Početak28,300,346 bp[1]
Kraj28,495,145 bp[1]
Lokacija gena (miš)
Hromosom 5 (miš)
Hrom.Hromosom 5 (miš)[2]
Hromosom 5 (miš)
Genomska lokacija za FLT1
Genomska lokacija za FLT1
Bend5 G3|5 87.01 cMPočetak147,498,414 bp[2]
Kraj147,662,821 bp[2]
Obrazac RNK ekspresije
Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija vascular endothelial growth factor-activated receptor activity
aktivnost sa transferazom
nucleotide binding
protein kinase activity
placental growth factor-activated receptor activity
kinase activity
GO:0001948, GO:0016582 vezivanje za proteine
transmembrane receptor protein tyrosine kinase activity
protein tyrosine kinase activity
ATP binding
growth factor binding
vascular endothelial growth factor binding
Ćelijska komponenta citoplazma
integral component of membrane
endozom
focal adhesion
membrana
receptor complex
integral component of plasma membrane
extracellular region
Vanćelijsko
ćelijska membrana
actin cytoskeleton
Biološki proces positive regulation of vascular endothelial growth factor receptor signaling pathway
Ćelijska diferencijacija
blood vessel morphogenesis
vascular endothelial growth factor receptor-1 signaling pathway
positive regulation of MAP kinase activity
monocyte chemotaxis
positive regulation of phospholipase C activity
transmembrane receptor protein tyrosine kinase signaling pathway
vascular endothelial growth factor signaling pathway
Fosforilacija
positive regulation of angiogenesis
positive regulation of phosphatidylinositol 3-kinase activity
multicellular organism development
Hemotaksija
protein phosphorylation
vascular endothelial growth factor receptor signaling pathway
embryonic morphogenesis
Angiogeneza
protein autophosphorylation
positive regulation of phosphatidylinositol 3-kinase signaling
peptidyl-tyrosine phosphorylation
cellular response to vascular endothelial growth factor stimulus
Ćelijska migracija
positive regulation of MAPK cascade
positive regulation of cell population proliferation
positive regulation of cell migration
sprouting angiogenesis
positive regulation of ERK1 and ERK2 cascade
negative regulation of vascular endothelial cell proliferation
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez
Ensembl
UniProt
RefSeq (mRNK)

NM_001159920
NM_001160030
NM_001160031
NM_002019

NM_010228
NM_001363135

RefSeq (bjelančevina)

NP_001153392
NP_001153502
NP_001153503
NP_002010

NP_034358
NP_001350064

Lokacija (UCSC)Chr 13: 28.3 – 28.5 MbChr 5: 147.5 – 147.66 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš

Receptor 1 vaskularnog endotelnog faktora rasta je protein koji je kod ljudi kodiran genom FLT1.[5]

Aminokiselinska sekvenca

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Dužina polipeptidnog lanca je 1.338 aminokiselina, a molekulska težina 150 769 Da .[6]

Simboli
1020304050
MVSYWDTGVLLCALLSCLLLTGSSSGSKLKDPELSLKGTQHIMQAGQTLH
LQCRGEAAHKWSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQAN
HTGFYSCKYLAVPTSKKKETESAIYIFISDTGRPFVEMYSEIPEIIHMTE
GRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKGFIISNATYK
EIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPVKLLRGHTLVL
NCTATTPLNTRVQMTWSYPDEKNKRASVRRRIDQSNSHANIFYSVLTIDK
MQNKDKGLYTCRVRSGPSFKSVNTSVHIYDKAFITVKHRKQQVLETVAGK
RSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDA
GNYTILLSIKQSNVFKNLTATLIVNVKPQIYEKAVSSFPDPALYPLGSRQ
ILTCTAYGIPQPTIKWFWHPCNHNHSEARCDFCSNNEESFILDADSNMGN
RIESITQRMAIIEGKNKMASTLVVADSRISGIYICIASNKVGTVGRNISF
YITDVPNGFHVNLEKMPTEGEDLKLSCTVNKFLYRDVTWILLRTVNNRTM
HYSISKQKMAITKEHSITLNLTIMNVSLQDSGTYACRARNVYTGEEILQK
KEITIRDQEAPYLLRNLSDHTVAISSSTTLDCHANGVPEPQITWFKNNHK
IQQEPGIILGPGSSTLFIERVTEEDEGVYHCKATNQKGSVESSAYLTVQG
TSDKSNLELITLTCTCVAATLFWLLLTLFIRKMKRSSSEIKTDYLSIIMD
PDEVPLDEQCERLPYDASKWEFARERLKLGKSLGRGAFGKVVQASAFGIK
KSPTCRTVAVKMLKEGATASEYKALMTELKILTHIGHHLNVVNLLGACTK
QGGPLMVIVEYCKYGNLSNYLKSKRDLFFLNKDAALHMEPKKEKMEPGLE
QGKKPRLDSVTSSESFASSGFQEDKSLSDVEEEEDSDGFYKEPITMEDLI
SYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKN
PDYVRKGDTRLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGGSPY
PGVQMDEDFCSRLREGMRMRAPEYSTPEIYQIMLDCWHRDPKERPRFAEL
VEKLGDLLQANVQQDGKDYIPINAILTGNSGFTYSTPAFSEDFFKESISA
PKFNSGSSDDVRYVNAFKFMSLERIKTFEELLPNATSMFDDYQGDSSTLL
ASPMLKRFTWTDSKPKASLKIDLRVTSKSKESGLSDVSRPSFCHSSCGHV
SEGKRRFTYDHAELERKIACCSPPPDYNSVVLYSTPPI

Funkcija

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Onkogen FLT pripada porodici src gena i srodan je onkogenu ROS (MIM 165020). Kao i drugi članovi ove porodice, pokazuje aktivnost tirozinske protein-kinaze, koja je važna za kontrolu proliferacije i diferencijacije ćelija. Struktura sekvence gena FLT nalikuje strukturi gena FMS (MIM 164770); stoga, Yoshida et al. (1987) predložili su naziv FLT kao akronim za FMS-sličnu tirozin-kinazu.[7]

Nedavno je otkriveno da je ablacija VEGFR1 hemijskim i genetičkim putem povećala pretvorbu bijelog masnog tkiva u tamno masno tkivo, kao i povećala smeđu masnu angiogenezu kod miševa.[8]

Utvrđeno je da funkcionalne genetičke varijacije u FLT1 (rs9582036) utiču na preživljavanje karcinom pluća ne-malih ćelija.[9]

Interakcije

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Pokazano je da FLT1 stupa u interakcije sa PLCG1 [10] i VEGF-B.[11][12]

Također pogledajte

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Reference

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000102755 - Ensembl, maj 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029648 - 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. ^ Shibuya M, Yamaguchi S, Yamane A, Ikeda T, Tojo A, Matsushime H, Sato M (april 1990). "Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase gene (flt) closely related to the fms family". Oncogene. 5 (4): 519–24. PMID 2158038.
  6. ^ "UniProt, P17948". Pristupljeno 11. 9. 2017.
  7. ^ "Entrez Gene: FLT1 fms-related tyrosine kinase 1 (vascular endothelial growth factor/vascular permeability factor receptor)".
  8. ^ Seki T, Hosaka K, Fischer C, Lim S, Andersson P, Abe M, Iwamoto H, Gao Y, Wang X, Fong GH, Cao Y (februar 2018). "Ablation of endothelial VEGFR1 improves metabolic dysfunction by inducing adipose tissue browning". The Journal of Experimental Medicine. 215 (2): 611–626. doi:10.1084/jem.20171012. PMC 5789413. PMID 29305395.
  9. ^ Glubb DM, Paré-Brunet L, Jantus-Lewintre E, Jiang C, Crona D, Etheridge AS, Mirza O, Zhang W, Seiser EL, Rzyman W, Jassem J, Auman T, Hirsch FR, Owzar K, Camps C, Dziadziuszko R, Innocenti F (juli 2015). "Functional FLT1 Genetic Variation is a Prognostic Factor for Recurrence in Stage I-III Non-Small-Cell Lung Cancer". Journal of Thoracic Oncology. 10 (7): 1067–75. doi:10.1097/JTO.0000000000000549. PMC 4494119. PMID 26134224.
  10. ^ Cunningham SA, Arrate MP, Brock TA, Waxham MN (novembar 1997). "Interactions of FLT-1 and KDR with phospholipase C gamma: identification of the phosphotyrosine binding sites". Biochemical and Biophysical Research Communications. 240 (3): 635–9. doi:10.1006/bbrc.1997.7719. PMID 9398617.
  11. ^ Olofsson B, Korpelainen E, Pepper MS, Mandriota SJ, Aase K, Kumar V, Gunji Y, Jeltsch MM, Shibuya M, Alitalo K, Eriksson U (septembar 1998). "Vascular endothelial growth factor B (VEGF-B) binds to VEGF receptor-1 and regulates plasminogen activator activity in endothelial cells". Proceedings of the National Academy of Sciences of the United States of America. 95 (20): 11709–14. doi:10.1073/pnas.95.20.11709. PMC 21705. PMID 9751730.
  12. ^ Makinen T, Olofsson B, Karpanen T, Hellman U, Soker S, Klagsbrun M, Eriksson U, Alitalo K (juli 1999). "Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1". The Journal of Biological Chemistry. 274 (30): 21217–22. doi:10.1074/jbc.274.30.21217. PMID 10409677.

Dopunska literatura

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Vanjski linkovi

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