P52583

PR
Gene name
KDR
Protein name
Vascular endothelial growth factor receptor 2
Names
VEGFR-2, Endothelial kinase receptor EK1, Quek 1, Quek1
Species
Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
KEGG Pathway
EC number
2.7.10.1: Protein-tyrosine kinases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

186-257 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

1038-1063 (Activation loop from InterPro)

Target domain

825-1155 (Protein kinase domain)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for P52583

Entry ID Method Resolution Chain Position Source
AF-P52583-F1 Predicted AlphaFoldDB

No variants for P52583

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P52583

No associated diseases with P52583

25 regional properties for P52583

Type Name Position InterPro Accession
domain Protein kinase domain 825 - 1155 IPR000719
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 825 - 1153 IPR001245
conserved_site Tyrosine-protein kinase, receptor class III, conserved site 884 - 897 IPR001824
domain Immunoglobulin subtype 2 232 - 306 IPR003598-1
domain Immunoglobulin subtype 2 334 - 396 IPR003598-2
domain Immunoglobulin subtype 2 552 - 640 IPR003598-3
domain Immunoglobulin subtype 2 670 - 735 IPR003598-4
domain Immunoglobulin subtype 35 - 116 IPR003599-1
domain Immunoglobulin subtype 130 - 214 IPR003599-2
domain Immunoglobulin subtype 226 - 318 IPR003599-3
domain Immunoglobulin subtype 328 - 409 IPR003599-4
domain Immunoglobulin subtype 421 - 538 IPR003599-5
domain Immunoglobulin subtype 546 - 653 IPR003599-6
domain Immunoglobulin subtype 664 - 746 IPR003599-7
domain Immunoglobulin-like domain 234 - 312 IPR007110-1
domain Immunoglobulin-like domain 320 - 405 IPR007110-2
domain Immunoglobulin-like domain 412 - 534 IPR007110-3
domain Immunoglobulin-like domain 553 - 651 IPR007110-4
domain Immunoglobulin-like domain 658 - 744 IPR007110-5
active_site Tyrosine-protein kinase, active site 1017 - 1029 IPR008266
domain Immunoglobulin I-set 329 - 403 IPR013098-1
domain Immunoglobulin I-set 659 - 745 IPR013098-2
binding_site Protein kinase, ATP binding site 831 - 859 IPR017441
domain Tyrosine-protein kinase, catalytic domain 825 - 1153 IPR020635
domain VEGFR-2, transmembrane domain 750 - 784 IPR041348

Functions

Description
EC Number 2.7.10.1 Protein-tyrosine kinases
Subcellular Localization
  • Cell membrane ; Single-pass type I membrane protein
  • Cytoplasmic vesicle
  • Early endosome
  • Cell junction
  • Endoplasmic reticulum
  • Detected on caveolae-enriched lipid rafts at the cell surface
  • Is recycled from the plasma membrane to endosomes and back again
  • Phosphorylation triggered by VEGFA binding promotes internalization and subsequent degradation
  • Localized with RAP1A at cell-cell junctions (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
anchoring junction A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix.
early endosome A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
growth factor binding Binding to a growth factor, proteins or polypeptides that stimulate a cell or organism to grow or proliferate.
vascular endothelial growth factor receptor activity Combining with a vascular endothelial growth factor (VEGF) receptor ligand and transmitting the signal across the plasma membrane to initiate a change in cell activity.

6 GO annotations of biological process

Name Definition
angiogenesis Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.
cell differentiation The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state.
cellular response to vascular endothelial growth factor stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vascular endothelial growth factor stimulus.
positive regulation of protein phosphorylation Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein.
protein autophosphorylation The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
vascular endothelial growth factor receptor signaling pathway The series of molecular signals initiated by a ligand binding to a vascular endothelial growth factor receptor (VEGFR) on the surface of the target cell, and ending with the regulation of a downstream cellular process, e.g. transcription.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MELGPLRVLT VLLCLAPVFA GLFISMDQPT LSIQKSVLTI TTNDTLNITC SGQRAVYWSW
70 80 90 100 110 120
PNNQSSVEKR LAVTGCSEGP FCKTLTLLRV IGNDTGDYRC LYGDSQAATT IYVYVQDYRS
130 140 150 160 170 180
PFVTSVGDQL GIVYITKNKT VVVPCLGTVS NLNVSLHAKY PEKVFVPDGK SISWDNKKGF
190 200 210 220 230 240
TIPSHLINYA GMVFCEAKID NESYQSVIYI VAVVGYRIYD LTMNPHYQVE LAVGEKLVLN
250 260 270 280 290 300
CTVRTELNVG IDFRWDYPSI KERRATIRDL KTTAGEIKTF VSTLTIESVN LSDKGRYTCA
310 320 330 340 350 360
ASSGRMNMKN SSYFIIHESP FIHLEKMENV VEMKLGDTVS IPVKFKGYPP PEAKWYKNGK
370 380 390 400 410 420
VINANHTVKL GYALVITEAT EKDAGNYTVV LTNPTNKMQK RHTFTLLVNV PPQIGENALM
430 440 450 460 470 480
APVDSYKYGS TQALTCTIYA VPPPAAVLWY WQLEEECTFS PQKVRLGANP YACRKWKVIS
490 500 510 520 530 540
ERKGGNQVEI KQRVVTIAGK TKTVSTLVIQ AANVSALYRC MATNRAGSSE RVISFHVTRG
550 560 570 580 590 600
LEINLQPRSQ LTEKDNTSLQ CTADKFTFEK LSWYKLSTHV SQTPFGGLPM PVCKNLDALQ
610 620 630 640 650 660
KLNATVSNVN GENVTLELIL RNISLQDGGD YVCIAQDKKA KTQHCLVKHL TVQEPLHPRL
670 680 690 700 710 720
VGNLENQTTN IGETIEVLCT VNGVPPPNIT WFKNSETLFE DSGIVLKDGN KTLTIRRVRK
730 740 750 760 770 780
EDGGLYTCLA CNILGCKKAE AFFSVQGAEE KTNLELIILV GTAVIAMFFW LLLVIILRTV
790 800 810 820 830 840
KRANGGDMKT GYLSIIMDPD EVPIDEHCER LPYDASKWEF PRDRLKLGKP LGRGAFGQVI
850 860 870 880 890 900
EADAFGIDKT ATCRTVAVKM LKEGATHSEH RALMSELKIL IHIGHHLNVV NLLGACTKPG
910 920 930 940 950 960
GPLMVIVEYC KFGNLSAYLR SKRSEFIPYK MKSARFRQGK ENYTGDISTD LKQRLDSITS
970 980 990 1000 1010 1020
SQSSTSSGFV EERSLSDVEE EDAGSEDLCK NPLTMEDLIC YSFQVARGME FLASRKCIHR
1030 1040 1050 1060 1070 1080
DLAARNILLS DNNVVKICDF GLARDIYKDP DYVRKGDARL PLKWMAPETI FDRVYTIQSD
1090 1100 1110 1120 1130 1140
VWSFGVLLWE IFSLGASPYP GVKIDEEFCR RLKEGTRMRA PDYTTPEMYQ TMLDCWHGDP
1150 1160 1170 1180 1190 1200
KQRPTFSELV EHLGNLLQAN VRQDGKDYVV LPLSVSLNME EDSGLSLPTS PASCKEEEEV
1210 1220 1230 1240 1250 1260
CDPKFHYDNT AGISQYRQGS KRKSRPVSVK TFEDIPLVTT VKVVQEENQT DSGMVLASEE
1270 1280 1290 1300 1310 1320
LKTLEEQDKQ VKIPFSTLAP SKSNESVMSE ASNQTSGYQS GYHSDDMDNM VCSSEDTELL
1330 1340
CAQEASPTLP RCAWPGIYSP APVASLPL