TYRO3_HUMAN
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 03-AUG-2022, entry version 207.
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=3; IntAct=EBI-3951628, EBI-401755;
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="http://atlasgeneticsoncology.org/Genes/TYRO3ID42739ch15q15.html";
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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; 35.
DR IntAct; Q06418; 26.
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 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; Q06418; -.
DR PeptideAtlas; Q06418; -.
DR PRIDE; Q06418; -.
DR ProteomicsDB; 58444; -.
DR Antibodypedia; 2066; 742 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 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; VRCTNAL; -.
DR OrthoDB; 263089at2759; -.
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; 43 hits in 1108 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 176 other tissues.
DR ExpressionAtlas; Q06418; baseline and differential.
DR Genevisible; Q06418; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS: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:0014065; P:phosphatidylinositol 3-kinase signaling; NAS:UniProtKB.
DR GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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:0043491; P:protein kinase B signaling; ISS: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 Gene3D; 2.60.40.10; -; 4.
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 Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
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
