ID A0A7J7FFV4_DICBM Unreviewed; 1242 AA. AC A0A7J7FFV4; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 02-OCT-2024, entry version 18. DE RecName: Full=Vascular endothelial growth factor receptor 2 {ECO:0000256|ARBA:ARBA00022256}; DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902}; GN ORFNames=HPG69_001520 {ECO:0000313|EMBL:KAF5926889.1}; OS Diceros bicornis minor (South-central black rhinoceros). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Rhinocerotidae; Diceros. OX NCBI_TaxID=77932 {ECO:0000313|EMBL:KAF5926889.1, ECO:0000313|Proteomes:UP000551758}; RN [1] {ECO:0000313|EMBL:KAF5926889.1, ECO:0000313|Proteomes:UP000551758} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBR-YM {ECO:0000313|EMBL:KAF5926889.1}; RC TISSUE=Skin {ECO:0000313|EMBL:KAF5926889.1}; RX PubMed=32585004; RA Moodley Y., Westbury M.V., Russo I.M., Gopalakrishnan S., Rakotoarivelo A., RA Olsen R.A., Prost S., Tunstall T., Ryder O.A., Dalen L., Bruford M.W.; RT "Interspecific Gene Flow and the Evolution of Specialization in Black and RT White Rhinoceros."; RL Mol. Biol. Evol. 37:3105-3117(2020). 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:0000256|ARBA:ARBA00001171}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. CC Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Early endosome CC {ECO:0000256|ARBA:ARBA00004412}. Endoplasmic reticulum CC {ECO:0000256|ARBA:ARBA00004240}. Endosome CC {ECO:0000256|ARBA:ARBA00004177}. Membrane CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, CC ECO:0000256|RuleBase:RU000311}. Vesicle CC {ECO:0000256|ARBA:ARBA00004373}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. CSF-1/PDGF receptor subfamily. CC {ECO:0000256|RuleBase:RU000311}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAF5926889.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JACDTQ010000745; KAF5926889.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7J7FFV4; -. DR Proteomes; UP000551758; Unassembled WGS sequence. DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0019838; F:growth factor binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IEA:InterPro. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter. DR GO; GO:0045446; P:endothelial cell differentiation; IEA:TreeGrafter. DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:TreeGrafter. DR GO; GO:0030335; P:positive regulation of cell migration; IEA:TreeGrafter. DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:TreeGrafter. DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:InterPro. DR CDD; cd00096; Ig; 1. DR CDD; cd05862; IgI_VEGFR; 1. DR CDD; cd05864; IgI_VEGFR-2; 1. DR CDD; cd05103; PTKc_VEGFR2; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 6. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR050122; RTK. 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 InterPro; IPR009136; VEGFR2_rcpt. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR PANTHER; PTHR24416:SF45; VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2; 1. DR Pfam; PF07679; I-set; 2. DR Pfam; PF00047; ig; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF22971; VEGFR-1-like_5th; 1. DR Pfam; PF21339; VEGFR-1-like_Ig-like; 1. DR Pfam; PF17988; VEGFR-2_TMD; 1. DR Pfam; PF22854; VEGFR1-3_N_Ig-like; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 3. DR PRINTS; PR01832; VEGFRECEPTOR. DR PRINTS; PR01834; VEGFRECEPTR2. DR SMART; SM00409; IG; 6. DR SMART; SM00408; IGc2; 4. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF48726; Immunoglobulin; 6. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50835; IG_LIKE; 4. 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 3: Inferred from homology; KW Angiogenesis {ECO:0000256|ARBA:ARBA00022657}; KW ATP-binding {ECO:0000256|PIRSR:PIRSR000615-2, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Developmental protein {ECO:0000256|ARBA:ARBA00022473}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Endosome {ECO:0000256|ARBA:ARBA00022753}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319, KW ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00023137}; KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000615-2, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311}; KW Reference proteome {ECO:0000313|Proteomes:UP000551758}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|ARBA:ARBA00023137}; KW Transmembrane {ECO:0000256|RuleBase:RU000311}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..1242 FT /note="Vascular endothelial growth factor receptor 2" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5029458201" FT DOMAIN 224..323 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 328..414 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 421..544 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 553..625 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 720..1048 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1166..1242 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1172..1201 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1223..1242 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 914 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1" FT BINDING 727..734 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2" FT BINDING 754 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2, FT ECO:0000256|PROSITE-ProRule:PRU10141" FT BINDING 918 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2" FT BINDING 919 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3" FT BINDING 932 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3" SQ SEQUENCE 1242 AA; 138520 MW; C3D79963769741A3 CRC64; MEGKALLAIA LWLCVETRAA SVGLSSVSVD PPRLSIQKDI LTIMANTTLQ ITCRGERDLD WLWPNNQSGS ENRVGVTECS DGFFCKTLTI PEVIGNDTGA YKCFYRDTDT ASVVYVYVQD YRSPFIASVS DQHGVVYITE NKNKTVVIPC LGSISNLNVS LCARYPEKRF VPDGNRISWD SKKGFTIPSY MISYAGMVFC EAKINDETYQ SIMYIVVVVG YKIYDVVLSP PDGIELSVGE KLVLNCTART ELNVGIDFNW EYPSLKHQHK KLVNRDLKTQ SGSEMKKFLS TLTIDRVTRS DRGQYTCAAS SGLMTKRNST LVTVHEKPFV AFGSGMESLV EVTVGDHVKV PVKYLGYPPP EIKWYKNGRP IESNHTIKVG HALTIMEVSE KDAGNYTIIL TNPISKEKQS HVVSLVVNVP PQIGEKSLIS PVDSYQYGTT QVLTCTVYAV PPPLHIRWYW QLEEECTYKP TQAVLMTNPY TCKEWRNMED FQGGNKIEVN KNQFALIEGK NKTVSTLVIQ VANVSALYKC EAVNKAGRGE RVISFHVTKR MAPMITGNLE NQTTSIGETI EVACTVSGNP SPQITWFKDN ETLVEDSGIV LKDGNRNLTI RRVRKEDEGL YTCQACSVLG CAKVEAFFIV EGAQEKTNLE VIILVGTAVI AMFFWLLLVI VLRTVKRANG GELKTGYLSI VMDPDELPLD EHCERLPYDA SKWEFPRDRL KLGKPLGRGA FGQVIEADAF GIDKTATCKT VAVKMLKEGA THSEHRALMS ELKILIHIGH HLNVVNLLGA CTKPGGPLMV IVEFCKFGNL STYLRSKRNE FVPYKSKGAR FRPGKEYVGE ITVDPKRRLD SITSSQSSAS SGFVEEKSLS DVEEEEVSED LYKNFLTLEH LICYSFQVAK GMEFLASRKC IHRDLAARNI LLSEKNVVKI CDFGLARDIY KDPDYVRKGD ARLPLKWMAP ETIFDRVYTI QSDVWSFGVL LWEIFSLGAS PYPGVKIDEE FCRRLKEGTR MRAPDYTTPE MYQTMLDCWH GEPSQRPTFS ELVEHLGNLL QANAQQDGKD YIVLPISETL SMEEDSGLSL PTSPVSCMEE EEVCDPKFHY DNTAGISQYL QNSKRKSRPV SVKTFEDIPL EEPEVKVIPD DNQTDSGMVL ASEELKTLED RTKLAPSFSG LMPSKSKESV ASEGSNQTSG YQSGYHSDDT DTTVYSSEEA ELLKLMEMGQ QAGSAAQILQ PGSGTTLSSP PV //