ID A0A7J7FFV4_DICBM Unreviewed; 1242 AA. AC A0A7J7FFV4; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 22-FEB-2023, entry version 9. DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902}; 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 Membrane {ECO:0000256|ARBA:ARBA00004479, CC ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}. 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0019838; F:growth factor binding; IEA:InterPro. 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:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:InterPro. DR CDD; cd00096; Ig; 1. DR CDD; cd05862; Ig_VEGFR; 1. DR CDD; cd05864; Ig_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; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. 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; PF13927; Ig_3; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF17988; VEGFR-2_TMD; 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|PROSITE-ProRule:PRU10141}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319, KW ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00023137}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW 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}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|ARBA:ARBA00023137}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000311}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..1242 FT /note="receptor protein-tyrosine kinase" 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 BINDING 754 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" 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 //