ID TYRO3_HUMAN Reviewed; 890 AA. AC Q06418; O14953; Q86VR3; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 216. DE RecName: Full=Tyrosine-protein kinase receptor TYRO3; DE EC=2.7.10.1; DE AltName: Full=Tyrosine-protein kinase BYK; DE AltName: Full=Tyrosine-protein kinase DTK; DE AltName: Full=Tyrosine-protein kinase RSE; DE AltName: Full=Tyrosine-protein kinase SKY; DE AltName: Full=Tyrosine-protein kinase TIF; DE Flags: Precursor; GN Name=TYRO3; Synonyms=BYK, DTK, RSE, SKY, TIF; 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; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7511603; DOI=10.1016/s0021-9258(17)34118-2; RA Mark M.R., Scadden D.T., Wang Z., Gu Q., Goddard A., Godowski P.J.; RT "RSE, a novel receptor-type tyrosine kinase with homology to Axl/Ufo, is RT expressed at high levels in the brain."; RL J. Biol. Chem. 269:10720-10728(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8108112; RA Ohashi K., Mizuno K., Kuma K., Miyata T., Nakamura T.; RT "Cloning of the cDNA for a novel receptor tyrosine kinase, Sky, RT predominantly expressed in brain."; RL Oncogene 9:699-705(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-815. RC TISSUE=Brain; RX PubMed=7857658; DOI=10.3109/08977199409001055; RA Crosier K.E., Hall L.R., Lewis P.M., Morris C.M., Wood C.R., Morris J.C., RA Crosier P.S.; RT "Isolation and characterization of the human DTK receptor tyrosine RT kinase."; RL Growth Factors 11:137-144(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=9175267; DOI=10.1016/s0248-4900(97)86830-x; RA Kajii Y., Ninomiya D., Kato M., Mizuguchi M., Saji M., Katsumoto T., RA Ohno K., Takashima S., Onodera K.; RT "A tyrosine kinase-like molecule is localized in the nuclear membrane of RT neurons: hippocampal behavior under stress."; RL Biol. Cell 88:45-54(1996). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-21; SER-542; RP MET-819 AND GLY-824. RC TISSUE=Skin, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 519-720. RX PubMed=8262388; DOI=10.1016/0378-1119(93)90109-g; RA Polvi A., Armstrong E., Lai C., Lemke G., Huebner K., Spritz R.A., RA Giuda L.C., Nicholls R.D., Alitalo K.; RT "The human TYRO3 gene and pseudogene are located in chromosome 15q14-q25."; RL Gene 134:289-293(1993). RN [7] RP AUTOPHOSPHORYLATION. RX PubMed=7537495; DOI=10.1006/bbrc.1995.1549; RA Toshima J., Ohashi K., Iwashita S., Mizuno K.; RT "Autophosphorylation activity and association with Src family kinase of Sky RT receptor tyrosine kinase."; RL Biochem. Biophys. Res. Commun. 209:656-663(1995). RN [8] RP INTERACTION WITH GAS6. RX PubMed=7634325; DOI=10.1016/0092-8674(95)90424-7; RA Godowski P.J., Mark M.R., Chen J., Sadick M.D., Raab H., Hammonds R.G.; RT "Reevaluation of the roles of protein S and Gas6 as ligands for the RT receptor tyrosine kinase Rse/Tyro 3."; RL Cell 82:355-358(1995). RN [9] RP REVIEW ON FUNCTION. RX PubMed=16737840; DOI=10.1016/j.cytogfr.2006.04.004; RA Hafizi S., Dahlback B.; RT "Signalling and functional diversity within the Axl subfamily of receptor RT tyrosine kinases."; RL Cytokine Growth Factor Rev. 17:295-304(2006). RN [10] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=17005688; DOI=10.1128/jvi.01157-06; RA Shimojima M., Takada A., Ebihara H., Neumann G., Fujioka K., Irimura T., RA Jones S., Feldmann H., Kawaoka Y.; RT "Tyro3 family-mediated cell entry of Ebola and Marburg viruses."; RL J. Virol. 80:10109-10116(2006). RN [11] RP REVIEW ON FUNCTION. RX PubMed=18421305; DOI=10.1038/nri2303; RA Lemke G., Rothlin C.V.; RT "Immunobiology of the TAM receptors."; RL Nat. Rev. Immunol. 8:327-336(2008). RN [12] RP FUNCTION IN PLATELET ACTIVATION. RX PubMed=20546121; DOI=10.1111/j.1538-7836.2010.03935.x; RA Cosemans J.M., Van Kruchten R., Olieslagers S., Schurgers L.J., RA Verheyen F.K., Munnix I.C., Waltenberger J., Angelillo-Scherrer A., RA Hoylaerts M.F., Carmeliet P., Heemskerk J.W.; RT "Potentiating role of Gas6 and Tyro3, Axl and Mer (TAM) receptors in human RT and murine platelet activation and thrombus stabilization."; RL J. Thromb. Haemost. 8:1797-1808(2010). RN [13] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=22156524; DOI=10.1128/jvi.06451-11; RA Shimojima M., Stroher U., Ebihara H., Feldmann H., Kawaoka Y.; RT "Identification of cell surface molecules involved in dystroglycan- RT independent Lassa virus cell entry."; RL J. Virol. 86:2067-2078(2012). RN [14] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=22673088; DOI=10.1292/jvms.12-0176; RA Shimojima M., Kawaoka Y.; RT "Cell surface molecules involved in infection mediated by lymphocytic RT choriomeningitis virus glycoprotein."; RL J. Vet. Med. Sci. 74:1363-1366(2012). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466 AND SER-818, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP FUNCTION (MICROBIAL INFECTION), AND REVIEW. RX PubMed=25277499; DOI=10.1016/j.virol.2014.09.009; RA Moller-Tank S., Maury W.; RT "Phosphatidylserine receptors: enhancers of enveloped virus entry and RT infection."; RL Virology 468:565-580(2014). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 41-222, SUBUNIT, INTERACTION WITH RP GAS6, MUTAGENESIS OF ILE-99, AND DISULFIDE BONDS. RX PubMed=14623883; DOI=10.1074/jbc.m311750200; RA Heiring C., Dahlbaeck B., Muller Y.A.; RT "Ligand recognition and homophilic interactions in Tyro3: structural RT insights into the Axl/Tyro3 receptor tyrosine kinase family."; RL J. Biol. Chem. 279:6952-6958(2004). RN [18] RP VARIANT [LARGE SCALE ANALYSIS] THR-831. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Receptor tyrosine kinase that transduces signals from the CC extracellular matrix into the cytoplasm by binding to several ligands CC including TULP1 or GAS6. Regulates many physiological processes CC including cell survival, migration and differentiation. Ligand binding CC at the cell surface induces dimerization and autophosphorylation of CC TYRO3 on its intracellular domain that provides docking sites for CC downstream signaling molecules. Following activation by ligand, CC interacts with PIK3R1 and thereby enhances PI3-kinase activity. CC Activates the AKT survival pathway, including nuclear translocation of CC NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated CC genes. TYRO3 signaling plays a role in various processes such as neuron CC protection from excitotoxic injury, platelet aggregation and CC cytoskeleton reorganization. Also plays an important role in inhibition CC of Toll-like receptors (TLRs)-mediated innate immune response by CC activating STAT1, which selectively induces production of suppressors CC of cytokine signaling SOCS1 and SOCS3. {ECO:0000269|PubMed:20546121}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for lassa virus and CC lymphocytic choriomeningitis virus, possibly through GAS6 binding to CC phosphatidyl-serine at the surface of virion envelope. CC {ECO:0000269|PubMed:22156524, ECO:0000269|PubMed:22673088, CC ECO:0000269|PubMed:25277499}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Ebolavirus, CC possibly through GAS6 binding to phosphatidyl-serine at the surface of CC virion envelope. {ECO:0000269|PubMed:17005688}. 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:0000255|PROSITE-ProRule:PRU10028}; CC -!- SUBUNIT: Monomer and homodimer. Interacts (via N-terminus) with CC extracellular ligands TULP1 and GAS6 (By similarity). Interacts with CC PIK3R1; this interaction increases PI3-kinase activity (By similarity). CC {ECO:0000250}. CC -!- INTERACTION: CC Q06418; P62993: GRB2; NbExp=4; IntAct=EBI-3951628, EBI-401755; CC Q06418; P08238: HSP90AB1; NbExp=2; IntAct=EBI-3951628, EBI-352572; CC Q06418; Q9Y5K2: KLK4; NbExp=3; IntAct=EBI-3951628, EBI-10224152; CC Q06418; Q6A162: KRT40; NbExp=3; IntAct=EBI-3951628, EBI-10171697; CC Q06418; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-3951628, EBI-10172290; CC Q06418; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-3951628, EBI-10171774; CC Q06418; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-3951628, EBI-10172052; CC Q06418; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-3951628, EBI-10172511; CC Q06418; P26371: KRTAP5-9; NbExp=5; IntAct=EBI-3951628, EBI-3958099; CC Q06418; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-3951628, EBI-1044640; CC Q06418; Q99750: MDFI; NbExp=3; IntAct=EBI-3951628, EBI-724076; CC Q06418; B2RUY7: VWC2L; NbExp=3; IntAct=EBI-3951628, EBI-11747707; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. CC -!- TISSUE SPECIFICITY: Abundant in the brain and lower levels in other CC tissues. CC -!- PTM: Autophosphorylated. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. AXL/UFO subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA21781.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42739/TYRO3"; 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; U05682; AAA19236.1; -; mRNA. DR EMBL; D17517; BAA04467.1; -; mRNA. DR EMBL; U18934; AAC50070.1; -; mRNA. DR EMBL; D50479; BAA21781.1; ALT_INIT; mRNA. DR EMBL; BC049368; AAH49368.1; -; mRNA. DR EMBL; BC051756; AAH51756.1; -; mRNA. DR EMBL; X72886; CAA51396.1; -; mRNA. DR CCDS; CCDS10080.1; -. DR PIR; A53743; A53743. DR PIR; I38912; I38912. DR RefSeq; NP_001317193.1; NM_001330264.1. DR RefSeq; NP_006284.2; NM_006293.3. DR PDB; 1RHF; X-ray; 1.96 A; A/B=41-222. DR PDBsum; 1RHF; -. DR AlphaFoldDB; Q06418; -. DR SMR; Q06418; -. DR BioGRID; 113152; 158. DR IntAct; Q06418; 121. DR MINT; Q06418; -. DR STRING; 9606.ENSP00000263798; -. DR BindingDB; Q06418; -. DR ChEMBL; CHEMBL5314; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q06418; -. DR GuidetoPHARMACOLOGY; 1836; -. DR GlyConnect; 1982; 8 N-Linked glycans (5 sites). DR GlyCosmos; Q06418; 7 sites, 8 glycans. DR GlyGen; Q06418; 7 sites, 8 N-linked glycans (5 sites). DR iPTMnet; Q06418; -. DR PhosphoSitePlus; Q06418; -. DR BioMuta; TYRO3; -. DR DMDM; 1717829; -. DR EPD; Q06418; -. DR jPOST; Q06418; -. DR MassIVE; Q06418; -. DR MaxQB; Q06418; -. DR PaxDb; 9606-ENSP00000263798; -. DR PeptideAtlas; Q06418; -. DR ProteomicsDB; 58444; -. DR Pumba; Q06418; -. DR Antibodypedia; 2066; 882 antibodies from 35 providers. DR DNASU; 7301; -. DR Ensembl; ENST00000263798.8; ENSP00000263798.3; ENSG00000092445.12. DR GeneID; 7301; -. DR KEGG; hsa:7301; -. DR MANE-Select; ENST00000263798.8; ENSP00000263798.3; NM_006293.4; NP_006284.2. DR UCSC; uc001zof.3; human. DR AGR; HGNC:12446; -. DR CTD; 7301; -. DR DisGeNET; 7301; -. DR GeneCards; TYRO3; -. DR HGNC; HGNC:12446; TYRO3. DR HPA; ENSG00000092445; Tissue enhanced (brain, ovary). DR MIM; 600341; gene. DR neXtProt; NX_Q06418; -. DR OpenTargets; ENSG00000092445; -. DR PharmGKB; PA37097; -. DR VEuPathDB; HostDB:ENSG00000092445; -. DR eggNOG; ENOG502QRYR; Eukaryota. DR GeneTree; ENSGT00940000155879; -. DR InParanoid; Q06418; -. DR OMA; DCREDIY; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; Q06418; -. DR TreeFam; TF317402; -. DR BRENDA; 2.7.10.1; 2681. DR PathwayCommons; Q06418; -. DR SignaLink; Q06418; -. DR SIGNOR; Q06418; -. DR BioGRID-ORCS; 7301; 48 hits in 1189 CRISPR screens. DR ChiTaRS; TYRO3; human. DR EvolutionaryTrace; Q06418; -. DR GeneWiki; TYRO3; -. DR GenomeRNAi; 7301; -. DR Pharos; Q06418; Tchem. DR PRO; PR:Q06418; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q06418; Protein. DR Bgee; ENSG00000092445; Expressed in frontal pole and 178 other cell types or tissues. DR ExpressionAtlas; Q06418; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; NAS:UniProtKB. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:UniProtKB. DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central. DR GO; GO:0001618; F:virus receptor activity; IDA:FlyBase. DR GO; GO:0043277; P:apoptotic cell clearance; ISS:UniProtKB. DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB. DR GO; GO:0016477; P:cell migration; IBA:GO_Central. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0021885; P:forebrain cell migration; ISS:UniProtKB. DR GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl. DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB. DR GO; GO:0045824; P:negative regulation of innate immune response; ISS:UniProtKB. DR GO; GO:0051250; P:negative regulation of lymphocyte activation; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:0070050; P:neuron cellular homeostasis; ISS:UniProtKB. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:Ensembl. DR GO; GO:0042698; P:ovulation cycle; ISS:UniProtKB. DR GO; GO:0006909; P:phagocytosis; IBA:GO_Central. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB. DR GO; GO:0030168; P:platelet activation; ISS:UniProtKB. DR GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB. DR GO; GO:1903902; P:positive regulation of viral life cycle; IMP:FlyBase. DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB. DR GO; GO:0032940; P:secretion by cell; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR GO; GO:0060068; P:vagina development; IEA:Ensembl. DR CDD; cd00063; FN3; 2. DR CDD; cd20961; Ig1_Tyro3_like; 1. DR CDD; cd05749; IgI_2_Axl_Tyro3_like; 1. DR CDD; cd05074; PTKc_Tyro3; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 4. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. 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 PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR PANTHER; PTHR24416:SF279; TYROSINE-PROTEIN KINASE RECEPTOR TYRO3; 1. DR Pfam; PF00041; fn3; 2. DR Pfam; PF07679; I-set; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00060; FN3; 2. DR SMART; SM00409; IG; 2. DR SMART; SM00408; IGc2; 2. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50853; FN3; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR Genevisible; Q06418; HS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell adhesion; Cell membrane; Disulfide bond; KW Glycoprotein; Host cell receptor for virus entry; Host-virus interaction; KW Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase; KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase. FT SIGNAL 1..40 FT /evidence="ECO:0000255" FT CHAIN 41..890 FT /note="Tyrosine-protein kinase receptor TYRO3" FT /id="PRO_0000024478" FT TOPO_DOM 41..429 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 430..450 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 451..890 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 41..128 FT /note="Ig-like C2-type 1" FT DOMAIN 139..220 FT /note="Ig-like C2-type 2" FT DOMAIN 227..320 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 325..416 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 518..790 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 815..837 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 851..871 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 655 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 524..532 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 550 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 466 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 681 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 685 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 686 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 804 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 818 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 869 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55146" FT CARBOHYD 63 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 191 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 230 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 240 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 293 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 366 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 380 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 64..117 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:14623883" FT DISULFID 160..203 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:14623883" FT VARIANT 21 FT /note="P -> L (in dbSNP:rs17854578)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_045886" FT VARIANT 346 FT /note="I -> N (in dbSNP:rs12148316)" FT /id="VAR_045887" FT VARIANT 542 FT /note="G -> S (in dbSNP:rs17857363)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_045888" FT VARIANT 815 FT /note="A -> V (in dbSNP:rs1042057)" FT /evidence="ECO:0000269|PubMed:7857658" FT /id="VAR_045889" FT VARIANT 819 FT /note="L -> M (in dbSNP:rs17854579)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_045890" FT VARIANT 824 FT /note="R -> G (in dbSNP:rs17857364)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_045891" FT VARIANT 831 FT /note="A -> T" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041876" FT MUTAGEN 99 FT /note="I->R: Abolishes dimerization." FT /evidence="ECO:0000269|PubMed:14623883" FT CONFLICT 29..36 FT /note="Missing (in Ref. 3; AAC50070)" FT /evidence="ECO:0000305" FT CONFLICT 285 FT /note="L -> F (in Ref. 4; BAA21781)" FT /evidence="ECO:0000305" FT CONFLICT 293 FT /note="N -> I (in Ref. 4; BAA21781)" FT /evidence="ECO:0000305" FT CONFLICT 341 FT /note="E -> V (in Ref. 4; BAA21781)" FT /evidence="ECO:0000305" FT CONFLICT 812 FT /note="E -> D (in Ref. 4; BAA21781)" FT /evidence="ECO:0000305" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 60..68 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 74..78 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 85..94 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 97..106 FT /evidence="ECO:0007829|PDB:1RHF" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 113..121 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 131..136 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 140..143 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 156..163 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 170..175 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 183..192 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 199..207 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 210..213 FT /evidence="ECO:0007829|PDB:1RHF" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:1RHF" SQ SEQUENCE 890 AA; 96905 MW; F9EC675077C4E8F1 CRC64; MALRRSMGRP GLPPLPLPPP PRLGLLLAAL ASLLLPESAA AGLKLMGAPV KLTVSQGQPV KLNCSVEGME EPDIQWVKDG AVVQNLDQLY IPVSEQHWIG FLSLKSVERS DAGRYWCQVE DGGETEISQP VWLTVEGVPF FTVEPKDLAV PPNAPFQLSC EAVGPPEPVT IVWWRGTTKI GGPAPSPSVL NVTGVTQSTM FSCEAHNLKG LASSRTATVH LQALPAAPFN ITVTKLSSSN ASVAWMPGAD GRALLQSCTV QVTQAPGGWE VLAVVVPVPP FTCLLRDLVP ATNYSLRVRC ANALGPSPYA DWVPFQTKGL APASAPQNLH AIRTDSGLIL EWEEVIPEAP LEGPLGPYKL SWVQDNGTQD ELTVEGTRAN LTGWDPQKDL IVRVCVSNAV GCGPWSQPLV VSSHDRAGQQ GPPHSRTSWV PVVLGVLTAL VTAAALALIL LRKRRKETRF GQAFDSVMAR GEPAVHFRAA RSFNRERPER IEATLDSLGI SDELKEKLED VLIPEQQFTL GRMLGKGEFG SVREAQLKQE DGSFVKVAVK MLKADIIASS DIEEFLREAA CMKEFDHPHV AKLVGVSLRS RAKGRLPIPM VILPFMKHGD LHAFLLASRI GENPFNLPLQ TLIRFMVDIA CGMEYLSSRN FIHRDLAARN CMLAEDMTVC VADFGLSRKI YSGDYYRQGC ASKLPVKWLA LESLADNLYT VQSDVWAFGV TMWEIMTRGQ TPYAGIENAE IYNYLIGGNR LKQPPECMED VYDLMYQCWS ADPKQRPSFT CLRMELENIL GQLSVLSASQ DPLYINIERA EEPTAGGSLE LPGRDQPYSG AGDGSGMGAV GGTPSDCRYI LTPGGLAEQP GQAEHQPESP LNETQRLLLL QQGLLPHSSC //