ID X5D991_HUMAN Unreviewed; 608 AA. AC X5D991; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 29-MAY-2024, entry version 47. DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312}; DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312}; DE Flags: Fragment; GN Name=NTRK1 {ECO:0000313|EMBL:AHW56543.1}; 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:AHW56543.1}; RN [1] {ECO:0000313|EMBL:AHW56543.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Fetal whole brain {ECO:0000313|EMBL:AHW56543.1}; RX PubMed=24722188; RA Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., RA Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., RA Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A., RA Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., RA Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.; RT "Protein interaction network of alternatively spliced isoforms from brain RT links genetic risk factors for autism."; RL Nat. Commun. 5:3650-3650(2014). 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. 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; KJ534903; AHW56543.1; -; mRNA. DR AlphaFoldDB; X5D991; -. DR PeptideAtlas; X5D991; -. DR ChiTaRS; NTRK1; human. DR GO; GO:0030424; C:axon; IEA:TreeGrafter. DR GO; GO:0005886; C:plasma membrane; IEA:InterPro. DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043121; F:neurotrophin binding; IEA:TreeGrafter. DR GO; GO:0005030; F:neurotrophin receptor activity; IEA:InterPro. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0038180; P:nerve growth factor signaling pathway; IEA:TreeGrafter. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:TreeGrafter. DR GO; GO:0051896; P:regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:TreeGrafter. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro. DR CDD; cd04971; IgI_TrKABC_d5; 1. DR CDD; cd05092; PTKc_TrkA; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR020777; NTRK. DR InterPro; IPR020461; NTRK1. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR040665; TrkA_TMD. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS. DR PANTHER; PTHR24416:SF370; HIGH AFFINITY NERVE GROWTH FACTOR RECEPTOR; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF18613; TrkA_TMD; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 3. DR PRINTS; PR01939; NTKRECEPTOR. DR PRINTS; PR01940; NTKRECEPTOR1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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|PIRSR:PIRSR000615-2, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Kinase {ECO:0000313|EMBL:AHW56543.1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000615-2, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, KW ECO:0000256|RuleBase:RU000312}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Transferase {ECO:0000256|ARBA:ARBA00023137}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000312}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}. FT TRANSMEM 228..251 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 322..593 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT ACT_SITE 462 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1" FT BINDING 328..336 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR620777-51" FT BINDING 329..336 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2" FT BINDING 356 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2, FT ECO:0000256|PROSITE-ProRule:PRU10141" FT BINDING 402..408 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2" FT BINDING 466 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2" FT BINDING 467 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3" FT BINDING 480 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3" FT SITE 308 FT /note="Interaction with SHC1" FT /evidence="ECO:0000256|PIRSR:PIRSR620777-52" FT SITE 603 FT /note="Interaction with PLCG1" FT /evidence="ECO:0000256|PIRSR:PIRSR620777-52" FT NON_TER 608 FT /evidence="ECO:0000313|EMBL:AHW56543.1" SQ SEQUENCE 608 AA; 67035 MW; AA2005064FA94550 CRC64; MLRGGRRGQL GWHSWAAGPG SLLAWLILAS GRGLEQAGWI LTELEQSATV MKSGGLPSLG LTLANVTSDL NRKNVTCWAE NDVGRAEVSV QVNVSFPASV QLHTAVEMHH WCIPFSVDGQ PAPSLRWLFN GSVLNETSFI FTEFLEPAAN ETVRHGCLRL NQPTHVNNGN YTLLAANPFG QASASIMAAF MDNPFEFNPE DPIPVSFSPV DTNSTSGDPV EKKDETPFGV SVAVGLAVFA CLFLSTLLLV LNKCGRRNKF GINRPAVLAP EDGLAMSLHF MTLGGSSLSP TEGKGSGLQG HIIENPQYFS DACVHHIKRR DIVLKWELGE GAFGKVFLAE CHNLLPEQDK MLVAVKALKE ASESARQDFQ REAELLTMLQ HQHIVRFFGV CTEGRPLLMV FEYMRHGDLN RFLRSHGPDA KLLAGGEDVA PGPLGLGQLL AVASQVAAGM VYLAGLHFVH RDLATRNCLV GQGLVVKIGD FGMSRDIYST DYYRVGGRTM LPIRWMPPES ILYRKFTTES DVWSFGVVLW EIFTYGKQPW YQLSNTEAID CITQGRELER PRACPPEVYA IMRGCWQREP QQRHSIKDVH ARLQALAQAP PVYLDVLG //