ID B3XZL9_HUMAN Unreviewed; 785 AA. AC B3XZL9; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 02-JUN-2021, entry version 74. DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312}; DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG55003.1}; RN [1] {ECO:0000313|EMBL:BAG55003.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18593892; DOI=10.1158/0008-5472.CAN-07-6158; RA Choi Y.L., Takeuchi K., Soda M., Inamura K., Togashi Y., Hatano S., RA Enomoto M., Hamada T., Haruta H., Watanabe H., Kurashina K., Hatanaka H., RA Ueno T., Takada S., Yamashita Y., Sugiyama Y., Ishikawa Y., Mano H.; RT "Identification of novel isoforms of the EML4-ALK transforming gene in non- RT small cell lung cancer."; RL Cancer Res. 68:4971-4976(2008). 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 ECO:0000256|RuleBase:RU000312}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Insulin receptor subfamily. CC {ECO:0000256|RuleBase:RU000312}. 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; AB374361; BAG55003.1; -; mRNA. DR SMR; B3XZL9; -. DR PeptideAtlas; B3XZL9; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0000187; P:activation of MAPK activity; IEA:InterPro. DR GO; GO:0048666; P:neuron development; IEA:InterPro. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro. DR InterPro; IPR026830; ALK. 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; IPR002011; Tyr_kinase_rcpt_2_CS. DR PANTHER; PTHR24416:SF276; PTHR24416:SF276; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Kinase {ECO:0000256|ARBA:ARBA00023137}; KW Membrane {ECO:0000256|RuleBase:RU000312}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Phosphoprotein {ECO:0000256|RuleBase:RU000312}; KW Receptor {ECO:0000256|RuleBase:RU000312}; KW Transferase {ECO:0000256|ARBA:ARBA00023137}; KW Transmembrane {ECO:0000256|RuleBase:RU000312}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}. FT DOMAIN 281..557 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 57..205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 573..628 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 679..705 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 64..110 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 111..136 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 137..174 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 175..193 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 683..697 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 315 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 785 AA; 86401 MW; 3C013565BAD771DB CRC64; MDGFAGSLDD SISAASTSDV QDRLSALESR VQQQEDEITV LKAALADVLR RLAISEDHVA SVKKSVSSKG QPSPRAVIPM SCITNGSGAN RKPSHTSAVS IAGKETLSSA AKSGTEKKKE KPQGQREKKE ESHSNDQSPQ IRASPSPQPS SQPLQIHRQT PESKNATPTK SIKRPSPAEK SHNSWENSDD SRNKLSKIPS TPKLIPKVTK TADKHKDVII NQVYRRKHQE LQAMQMELQS PEYKLSKLRT STIMTDYNPN YCFAGKTSSI SDLKEVPRKN ITLIRGLGHG AFGEVYEGQV SGMPNDPSPL QVAVKTLPEV CSEQDELDFL MEALIISKFN HQNIVRCIGV SLQSLPRFIL LELMAGGDLK SFLRETRPRP SQPSSLAMLD LLHVARDIAC GCQYLEENHF IHRDIAARNC LLTCPGPGRV AKIGDFGMAR DIYRASYYRK GGCAMLPVKW MPPEAFMEGI FTSKTDTWSF GVLLWEIFSL GYMPYPSKSN QEVLEFVTSG GRMDPPKNCP GPVYRIMTQC WQHQPEDRPN FAIILERIEY CTQDPDVINT ALPIEYGPLV EEEEKVPVRP KDPEGVPPLL VSQQAKREEE RSPAAPPPLP TTSSGKAAKK PTAAEVSVRV PRGPAVEGGH VNMAFSQSNP PSELHRVHGS RNKPTSLWNP TYGSWFTEKP TKKNNPIAKK EPHERGNLGL EGSCTVPPNV ATGRLPGASL LLEPSSLTAN MKEVPLFRLR HFPCGNVNYG YQQQGLPLEA ATAPGAGHYE DTILKSKNSM NQPGP //