ID TYRO3_MOUSE Reviewed; 880 AA.
AC P55144; O09070; O09080; P70285; Q60752; Q62482; Q62483; Q62484; Q6NZM6;
AC Q78E85; Q78E87;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 201.
DE RecName: Full=Tyrosine-protein kinase receptor TYRO3;
DE EC=2.7.10.1;
DE AltName: Full=Etk2/tyro3;
DE AltName: Full=TK19-2;
DE AltName: Full=Tyrosine-protein kinase DTK;
DE AltName: Full=Tyrosine-protein kinase RSE;
DE AltName: Full=Tyrosine-protein kinase TIF;
DE Flags: Precursor;
GN Name=Tyro3; Synonyms=Dtk, Rse, Tif;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=7857657; DOI=10.3109/08977199409001054;
RA Crosier P.S., Lewis P.M., Hall L.R., Vitas M.R., Morris C.M., Beier D.R.,
RA Wood C.R., Crosier K.E.;
RT "Isolation of a receptor tyrosine kinase (DTK) from embryonic stem cells:
RT structure, genetic mapping and analysis of expression.";
RL Growth Factors 11:125-136(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J;
RX PubMed=8058320;
RA Lai C., Gore M., Lemke G.;
RT "Structure, expression, and activity of Tyro 3, a neural adhesion-related
RT receptor tyrosine kinase.";
RL Oncogene 9:2567-2578(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Brain, and Liver;
RX PubMed=8108111;
RA Fujimoto J., Yamamoto T.;
RT "brt, a mouse gene encoding a novel receptor-type protein-tyrosine kinase,
RT is preferentially expressed in the brain.";
RL Oncogene 9:693-698(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7723626; DOI=10.1016/0169-328x(94)00216-2;
RA Schulz N., Paulhiac C., Lee L., Zhou R.;
RT "Isolation and expression analysis of tyro3, a murine growth factor
RT receptor tyrosine kinase preferentially expressed in adult brain.";
RL Brain Res. Mol. Brain Res. 28:273-280(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8889809; DOI=10.1093/oxfordjournals.jbchem.a021408;
RA Sasaki M., Enami J.;
RT "Structure and expression of a murine homologue of sky receptor tyrosine
RT kinase.";
RL J. Biochem. 120:264-270(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92 (ISOFORMS 1; 2 AND 3).
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=7784069;
RA Biesecker L.G., Giannola D.M., Emerson S.G.;
RT "Identification of alternative exons, including a novel exon, in the
RT tyrosine kinase receptor gene Etk2/tyro3 that explain differences in 5'
RT cDNA sequences.";
RL Oncogene 10:2239-2242(1995).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=10227296; DOI=10.1038/19554;
RA Lu Q., Gore M., Zhang Q., Camenisch T., Boast S., Casagranda F., Lai C.,
RA Skinner M.K., Klein R., Matsushima G.K., Earp H.S., Goff S.P., Lemke G.;
RT "Tyro-3 family receptors are essential regulators of mammalian
RT spermatogenesis.";
RL Nature 398:723-728(1999).
RN [13]
RP INTERACTION WITH PIK3R1.
RX PubMed=10627473;
RA Lan Z., Wu H., Li W., Wu S., Lu L., Xu M., Dai W.;
RT "Transforming activity of receptor tyrosine kinase tyro3 is mediated, at
RT least in part, by the PI3 kinase-signaling pathway.";
RL Blood 95:633-638(2000).
RN [14]
RP FUNCTION IN PLATELET ACTIVATION.
RX PubMed=15650770; DOI=10.1172/jci22079;
RA Angelillo-Scherrer A., Burnier L., Flores N., Savi P., DeMol M.,
RA Schaeffer P., Herbert J.M., Lemke G., Goff S.P., Matsushima G.K.,
RA Earp H.S., Vesin C., Hoylaerts M.F., Plaisance S., Collen D., Conway E.M.,
RA Wehrle-Haller B., Carmeliet P.;
RT "Role of Gas6 receptors in platelet signaling during thrombus stabilization
RT and implications for antithrombotic therapy.";
RL J. Clin. Invest. 115:237-246(2005).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-181.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [17]
RP INTERACTION WITH TULP1.
RX PubMed=20978472; DOI=10.1038/emboj.2010.265;
RA Caberoy N.B., Zhou Y., Li W.;
RT "Tubby and tubby-like protein 1 are new MerTK ligands for phagocytosis.";
RL EMBO J. 29:3898-3910(2010).
RN [18]
RP FUNCTION IN NEURON PROTECTION.
RX PubMed=21084607; DOI=10.1523/jneurosci.4437-10.2010;
RA Zhong Z., Wang Y., Guo H., Sagare A., Fernandez J.A., Bell R.D.,
RA Barrett T.M., Griffin J.H., Freeman R.S., Zlokovic B.V.;
RT "Protein S protects neurons from excitotoxic injury by activating the TAM
RT receptor Tyro3-phosphatidylinositol 3-kinase-Akt pathway through its sex
RT hormone-binding globulin-like region.";
RL J. Neurosci. 30:15521-15534(2010).
RN [19]
RP FUNCTION IN IMMUNE RESPONSE INHIBITION.
RX PubMed=20363878; DOI=10.1210/en.2009-1498;
RA Sun B., Qi N., Shang T., Wu H., Deng T., Han D.;
RT "Sertoli cell-initiated testicular innate immune response through toll-like
RT receptor-3 activation is negatively regulated by Tyro3, Axl, and mer
RT receptors.";
RL Endocrinology 151:2886-2897(2010).
RN [20]
RP FUNCTION.
RX PubMed=21291561; DOI=10.1186/1750-1326-6-13;
RA Guo H., Barrett T.M., Zhong Z., Fernandez J.A., Griffin J.H., Freeman R.S.,
RA Zlokovic B.V.;
RT "Protein S blocks the extrinsic apoptotic cascade in tissue plasminogen
RT activator/N-methyl D-aspartate-treated neurons via Tyro3-Akt-FKHRL1
RT signaling pathway.";
RL Mol. Neurodegener. 6:13-13(2011).
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:15650770,
CC ECO:0000269|PubMed:20363878, ECO:0000269|PubMed:21084607,
CC ECO:0000269|PubMed:21291561}.
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. Interacts with PIK3R1; this
CC interaction increases PI3-kinase activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3; Synonyms=III;
CC IsoId=P55144-1; Sequence=Displayed;
CC Name=2; Synonyms=II;
CC IsoId=P55144-2; Sequence=VSP_012549;
CC Name=1; Synonyms=I, B;
CC IsoId=P55144-3; Sequence=VSP_012548;
CC -!- TISSUE SPECIFICITY: Abundant in the brain and lower levels in other
CC tissues.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: knockout mice are fertile, but male animals that
CC lack all three receptors TYRO3, AXL and MERTK produce no mature sperm.
CC {ECO:0000269|PubMed:10227296}.
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=AAB26942.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA54995.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U05683; AAA19237.1; -; mRNA.
DR EMBL; U18933; AAC52148.1; -; mRNA.
DR EMBL; X78103; CAA54995.1; ALT_INIT; mRNA.
DR EMBL; U18342; AAB26942.1; ALT_INIT; mRNA.
DR EMBL; U18343; AAB26943.1; -; mRNA.
DR EMBL; AB000826; BAA19191.1; -; Genomic_DNA.
DR EMBL; AB000827; BAA19192.1; -; mRNA.
DR EMBL; AB000828; BAA19193.1; -; mRNA.
DR EMBL; AK141198; BAE24581.1; -; mRNA.
DR EMBL; AL844896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066058; AAH66058.1; -; mRNA.
DR EMBL; BC082325; AAH82325.1; -; mRNA.
DR EMBL; U23721; AAC52215.1; -; Genomic_DNA.
DR EMBL; U23718; AAC52215.1; JOINED; Genomic_DNA.
DR EMBL; U23721; AAC52216.1; -; Genomic_DNA.
DR EMBL; U23719; AAC52216.1; JOINED; Genomic_DNA.
DR EMBL; U23721; AAC52217.1; -; Genomic_DNA.
DR EMBL; U23720; AAC52217.1; JOINED; Genomic_DNA.
DR CCDS; CCDS16611.1; -. [P55144-1]
DR CCDS; CCDS71119.1; -. [P55144-3]
DR PIR; B53743; B53743.
DR PIR; I48862; I48862.
DR PIR; I49152; I49152.
DR RefSeq; NP_001277729.1; NM_001290800.1. [P55144-3]
DR RefSeq; NP_062265.2; NM_019392.2. [P55144-1]
DR RefSeq; XP_017172636.1; XM_017317147.1.
DR PDB; 3QUP; X-ray; 1.90 A; A=485-800.
DR PDB; 4FEQ; X-ray; 2.20 A; A=485-800.
DR PDB; 4FF8; X-ray; 2.40 A; A=485-800.
DR PDBsum; 3QUP; -.
DR PDBsum; 4FEQ; -.
DR PDBsum; 4FF8; -.
DR AlphaFoldDB; P55144; -.
DR SMR; P55144; -.
DR BioGRID; 204395; 1.
DR STRING; 10090.ENSMUSP00000028763; -.
DR GlyCosmos; P55144; 8 sites, No reported glycans.
DR GlyGen; P55144; 8 sites.
DR iPTMnet; P55144; -.
DR PhosphoSitePlus; P55144; -.
DR SwissPalm; P55144; -.
DR MaxQB; P55144; -.
DR PaxDb; 10090-ENSMUSP00000028763; -.
DR ProteomicsDB; 298047; -. [P55144-1]
DR ProteomicsDB; 298048; -. [P55144-2]
DR ProteomicsDB; 298049; -. [P55144-3]
DR Antibodypedia; 2066; 882 antibodies from 35 providers.
DR DNASU; 22174; -.
DR Ensembl; ENSMUST00000028763.10; ENSMUSP00000028763.10; ENSMUSG00000027298.18. [P55144-1]
DR Ensembl; ENSMUST00000110783.8; ENSMUSP00000106410.2; ENSMUSG00000027298.18. [P55144-3]
DR GeneID; 22174; -.
DR KEGG; mmu:22174; -.
DR UCSC; uc008lup.2; mouse. [P55144-3]
DR UCSC; uc008luq.1; mouse. [P55144-1]
DR AGR; MGI:104294; -.
DR CTD; 7301; -.
DR MGI; MGI:104294; Tyro3.
DR VEuPathDB; HostDB:ENSMUSG00000027298; -.
DR eggNOG; ENOG502QRYR; Eukaryota.
DR GeneTree; ENSGT00940000155879; -.
DR HOGENOM; CLU_015796_0_0_1; -.
DR InParanoid; P55144; -.
DR OMA; DCREDIY; -.
DR OrthoDB; 1614410at2759; -.
DR PhylomeDB; P55144; -.
DR TreeFam; TF317402; -.
DR BRENDA; 2.7.10.1; 3474.
DR BioGRID-ORCS; 22174; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Tyro3; mouse.
DR PRO; PR:P55144; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P55144; Protein.
DR Bgee; ENSMUSG00000027298; Expressed in primary motor cortex and 213 other cell types or tissues.
DR Genevisible; P55144; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
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; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR GO; GO:0043277; P:apoptotic cell clearance; IGI:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0021885; P:forebrain cell migration; IGI:MGI.
DR GO; GO:0046649; P:lymphocyte activation; IGI:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IGI:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IGI:UniProtKB.
DR GO; GO:0045824; P:negative regulation of innate immune response; IGI:UniProtKB.
DR GO; GO:0051250; P:negative regulation of lymphocyte activation; IGI:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IGI:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IGI:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IMP:MGI.
DR GO; GO:0042698; P:ovulation cycle; IGI:MGI.
DR GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:UniProtKB.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
DR GO; GO:1903902; P:positive regulation of viral life cycle; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0032940; P:secretion by cell; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IGI:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0060068; P:vagina development; IGI:MGI.
DR CDD; cd00063; FN3; 2.
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; 1.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell adhesion;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..880
FT /note="Tyrosine-protein kinase receptor TYRO3"
FT /id="PRO_0000024479"
FT TOPO_DOM 31..419
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..118
FT /note="Ig-like C2-type 1"
FT DOMAIN 129..209
FT /note="Ig-like C2-type 2"
FT DOMAIN 217..310
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 315..406
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 508..785
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 800..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 645
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 514..522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 540
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 671
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 675
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 676
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 794
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06418"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55146"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 220
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 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 150..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..31
FT /note="MALRRSMGWPGLRPLLLAGLASLLLPGSAAA -> MDDKLENTLGRWAGENG
FT LSIGEYLAIK (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:7723626,
FT ECO:0000303|PubMed:8108111, ECO:0000303|PubMed:8889809"
FT /id="VSP_012548"
FT VAR_SEQ 1..31
FT /note="MALRRSMGWPGLRPLLLAGLASLLLPGSAAA -> MGCPAGDWKVFGEGGAW
FT PGACPGSEAGPPQRQRSGQGAGPAAPSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8889809"
FT /id="VSP_012549"
FT CONFLICT 630
FT /note="A -> R (in Ref. 3; CAA54995)"
FT /evidence="ECO:0000305"
FT CONFLICT 637..639
FT /note="SSR -> AIK (in Ref. 5; BAA19191/BAA19192)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="V -> L (in Ref. 1; AAA19237, 2; AAC52148, 5;
FT BAA19193 and 6; AAB26942/AAB26943)"
FT /evidence="ECO:0000305"
FT STRAND 509..517
FT /evidence="ECO:0007829|PDB:3QUP"
FT STRAND 520..526
FT /evidence="ECO:0007829|PDB:3QUP"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 550..562
FT /evidence="ECO:0007829|PDB:3QUP"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:3QUP"
FT STRAND 589..594
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 601..609
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 619..638
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:3QUP"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:3QUP"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 686..688
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 691..696
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 701..716
FT /evidence="ECO:0007829|PDB:3QUP"
FT TURN 722..725
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 728..730
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 731..736
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 749..757
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 763..765
FT /evidence="ECO:0007829|PDB:3QUP"
FT HELIX 769..781
FT /evidence="ECO:0007829|PDB:3QUP"
SQ SEQUENCE 880 AA; 96208 MW; 2794316CB0034617 CRC64;
MALRRSMGWP GLRPLLLAGL ASLLLPGSAA AGLKLMGAPV KMTVSQGQPV KLNCSVEGME
DPDIHWMKDG TVVQNASQVS ISISEHSWIG LLSLKSVERS DAGLYWCQVK DGEETKISQS
VWLTVEGVPF FTVEPKDLAV PPNAPFQLSC EAVGPPEPVT IYWWRGLTKV GGPAPSPSVL
NVTGVTQRTE FSCEARNIKG LATSRPAIVR LQAPPAAPFN TTVTTISSYN ASVAWVPGAD
GLALLHSCTV QVAHAPGEWE ALAVVVPVPP FTCLLRNLAP ATNYSLRVRC ANALGPSPYG
DWVPFQTKGL APARAPQNFH AIRTDSGLIL EWEEVIPEDP GEGPLGPYKL SWVQENGTQD
ELMVEGTRAN LTDWDPQKDL ILRVCASNAI GDGPWSQPLV VSSHDHAGRQ GPPHSRTSWV
PVVLGVLTAL ITAAALALIL LRKRRKETRF GQAFDSVMAR GEPAVHFRAA RSFNRERPER
IEATLDSLGI SDELKEKLED VLIPEQQFTL GRMLGKGEFG SVREAQLKQE DGSFVKVAVK
MLKADIIASS DIEEFLREAA CMKEFDHPHV AKLVGVSLRS RAKGRLPIPM VILPFMKHGD
LHAFLLASRI GENPFNLPLQ TLVRFMVDIA CGMEYLSSRN FIHRDLAARN CMLAEDMTVC
VADFGLSRKI YSGDYYRQGC ASKLPVKWLA LESLADNLYT VHSDVWAFGV TMWEIMTRGQ
TPYAGIENAE IYNYLIGGNR LKQPPECMEE VYDLMYQCWS ADPKQRPSFT CLRMELENIL
GHLSVLSTSQ DPLYINIERA EQPTESGSPE VHCGERSSSE AGDGSGVGAV GGIPSDSRYI
FSPGGLSESP GQLEQQPESP LNENQRLLLL QQGLLPHSSC
//
