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P55144

- TYRO3_MOUSE

UniProt

P55144 - TYRO3_MOUSE

Protein

Tyrosine-protein kinase receptor TYRO3

Gene

Tyro3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3.4 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei540 – 5401ATPPROSITE-ProRule annotation
    Active sitei645 – 6451Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi514 – 5229ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphatidylinositol 3-kinase binding Source: UniProtKB
    3. protein heterodimerization activity Source: MGI
    4. protein tyrosine kinase activity Source: UniProtKB
    5. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. apoptotic cell clearance Source: UniProtKB
    2. forebrain cell migration Source: MGI
    3. natural killer cell differentiation Source: MGI
    4. negative regulation of inflammatory response Source: UniProtKB
    5. negative regulation of innate immune response Source: UniProtKB
    6. negative regulation of lymphocyte activation Source: MGI
    7. negative regulation of neuron apoptotic process Source: MGI
    8. negative regulation of toll-like receptor signaling pathway Source: UniProtKB
    9. neuron cellular homeostasis Source: UniProtKB
    10. ovulation cycle Source: MGI
    11. platelet activation Source: MGI
    12. platelet aggregation Source: UniProtKB
    13. protein autophosphorylation Source: UniProtKB
    14. protein kinase B signaling Source: UniProtKB
    15. secretion by cell Source: MGI
    16. spermatogenesis Source: UniProtKB
    17. substrate adhesion-dependent cell spreading Source: MGI
    18. vagina development Source: MGI

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase receptor TYRO3 (EC:2.7.10.1)
    Alternative name(s):
    Etk2/tyro3
    TK19-2
    Tyrosine-protein kinase DTK
    Tyrosine-protein kinase RSE
    Tyrosine-protein kinase TIF
    Gene namesi
    Name:Tyro3
    Synonyms:Dtk, Rse, Tif
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:104294. Tyro3.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW
    3. nuclear envelope Source: UniProtKB
    4. nucleus Source: UniProtKB
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    knockout mice are fertile, but male animals that lack all three receptors TYRO3, AXL and MERTK produce no mature sperm.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 880850Tyrosine-protein kinase receptor TYRO3PRO_0000024479Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi54 ↔ 107PROSITE-ProRule annotation
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi150 ↔ 193PROSITE-ProRule annotation
    Glycosylationi181 – 1811N-linked (GlcNAc...)1 Publication
    Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
    Modified residuei671 – 6711Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei675 – 6751Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei676 – 6761Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei794 – 7941Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP55144.
    PRIDEiP55144.

    PTM databases

    PhosphoSiteiP55144.

    Expressioni

    Tissue specificityi

    Abundant in the brain and lower levels in other tissues.

    Gene expression databases

    BgeeiP55144.
    CleanExiMM_TYRO3.
    GenevestigatoriP55144.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Interacts (via N-terminus) with extracellular ligands TULP1 and GAS6. Interacts with PIK3R1; this interaction increases PI3-kinase activity By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204395. 1 interaction.
    IntActiP55144. 1 interaction.
    MINTiMINT-4138931.

    Structurei

    Secondary structure

    1
    880
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi509 – 5179
    Beta strandi520 – 5267
    Beta strandi536 – 5416
    Helixi550 – 56213
    Beta strandi575 – 5784
    Beta strandi589 – 5946
    Helixi601 – 6099
    Helixi619 – 63820
    Helixi648 – 6503
    Beta strandi651 – 6533
    Beta strandi659 – 6613
    Helixi686 – 6883
    Helixi691 – 6966
    Helixi701 – 71616
    Turni722 – 7254
    Helixi728 – 7303
    Helixi731 – 7366
    Helixi749 – 7579
    Helixi763 – 7653
    Helixi769 – 78113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QUPX-ray1.90A485-800[»]
    4FEQX-ray2.20A485-800[»]
    4FF8X-ray2.40A485-800[»]
    ProteinModelPortaliP55144.
    SMRiP55144. Positions 37-365, 499-785.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 419389ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini441 – 880440CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei420 – 44021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 11888Ig-like C2-type 1Add
    BLAST
    Domaini129 – 20981Ig-like C2-type 2Add
    BLAST
    Domaini217 – 31094Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini315 – 40692Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini508 – 785278Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily.PROSITE-ProRule annotation
    Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00720000108377.
    HOVERGENiHBG006346.
    KOiK05116.
    OMAiDQVYIPV.
    OrthoDBiEOG77DJ5C.
    TreeFamiTF317402.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF00041. fn3. 2 hits.
    PF07679. I-set. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00060. FN3. 2 hits.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50853. FN3. 2 hits.
    PS50835. IG_LIKE. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 3 (identifier: P55144-1) [UniParc]FASTAAdd to Basket

    Also known as: III

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALRRSMGWP GLRPLLLAGL ASLLLPGSAA AGLKLMGAPV KMTVSQGQPV    50
    KLNCSVEGME DPDIHWMKDG TVVQNASQVS ISISEHSWIG LLSLKSVERS 100
    DAGLYWCQVK DGEETKISQS VWLTVEGVPF FTVEPKDLAV PPNAPFQLSC 150
    EAVGPPEPVT IYWWRGLTKV GGPAPSPSVL NVTGVTQRTE FSCEARNIKG 200
    LATSRPAIVR LQAPPAAPFN TTVTTISSYN ASVAWVPGAD GLALLHSCTV 250
    QVAHAPGEWE ALAVVVPVPP FTCLLRNLAP ATNYSLRVRC ANALGPSPYG 300
    DWVPFQTKGL APARAPQNFH AIRTDSGLIL EWEEVIPEDP GEGPLGPYKL 350
    SWVQENGTQD ELMVEGTRAN LTDWDPQKDL ILRVCASNAI GDGPWSQPLV 400
    VSSHDHAGRQ GPPHSRTSWV PVVLGVLTAL ITAAALALIL LRKRRKETRF 450
    GQAFDSVMAR GEPAVHFRAA RSFNRERPER IEATLDSLGI SDELKEKLED 500
    VLIPEQQFTL GRMLGKGEFG SVREAQLKQE DGSFVKVAVK MLKADIIASS 550
    DIEEFLREAA CMKEFDHPHV AKLVGVSLRS RAKGRLPIPM VILPFMKHGD 600
    LHAFLLASRI GENPFNLPLQ TLVRFMVDIA CGMEYLSSRN FIHRDLAARN 650
    CMLAEDMTVC VADFGLSRKI YSGDYYRQGC ASKLPVKWLA LESLADNLYT 700
    VHSDVWAFGV TMWEIMTRGQ TPYAGIENAE IYNYLIGGNR LKQPPECMEE 750
    VYDLMYQCWS ADPKQRPSFT CLRMELENIL GHLSVLSTSQ DPLYINIERA 800
    EQPTESGSPE VHCGERSSSE AGDGSGVGAV GGIPSDSRYI FSPGGLSESP 850
    GQLEQQPESP LNENQRLLLL QQGLLPHSSC 880
    Length:880
    Mass (Da):96,208
    Last modified:July 27, 2011 - v2
    Checksum:i2794316CB0034617
    GO
    Isoform 2 (identifier: P55144-2) [UniParc]FASTAAdd to Basket

    Also known as: II

    The sequence of this isoform differs from the canonical sequence as follows:
         1-31: MALRRSMGWPGLRPLLLAGLASLLLPGSAAA → MGCPAGDWKV...QGAGPAAPSG

    Show »
    Length:894
    Mass (Da):97,343
    Checksum:i4F45E58F5B466FEA
    GO
    Isoform 1 (identifier: P55144-3) [UniParc]FASTAAdd to Basket

    Also known as: I, B

    The sequence of this isoform differs from the canonical sequence as follows:
         1-31: MALRRSMGWPGLRPLLLAGLASLLLPGSAAA → MDDKLENTLGRWAGENGLSIGEYLAIK

    Show »
    Length:876
    Mass (Da):96,042
    Checksum:i5C7813084CC59D56
    GO

    Sequence cautioni

    The sequence AAB26942.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA54995.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti630 – 6301A → R in CAA54995. (PubMed:8058320)Curated
    Sequence conflicti637 – 6393SSR → AIK in BAA19191. (PubMed:8108112)Curated
    Sequence conflicti637 – 6393SSR → AIK in BAA19192. (PubMed:8108112)Curated
    Sequence conflicti811 – 8111V → L in AAA19237. (PubMed:7511603)Curated
    Sequence conflicti811 – 8111V → L in AAC52148. (PubMed:7857657)Curated
    Sequence conflicti811 – 8111V → L in BAA19193. (PubMed:8108112)Curated
    Sequence conflicti811 – 8111V → L in AAB26942. (PubMed:7723626)Curated
    Sequence conflicti811 – 8111V → L in AAB26943. (PubMed:7723626)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3131MALRR…GSAAA → MDDKLENTLGRWAGENGLSI GEYLAIK in isoform 1. 3 PublicationsVSP_012548Add
    BLAST
    Alternative sequencei1 – 3131MALRR…GSAAA → MGCPAGDWKVFGEGGAWPGA CPGSEAGPPQRQRSGQGAGP AAPSG in isoform 2. 1 PublicationVSP_012549Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05683 mRNA. Translation: AAA19237.1.
    U18933 mRNA. Translation: AAC52148.1.
    X78103 mRNA. Translation: CAA54995.1. Different initiation.
    U18342 mRNA. Translation: AAB26942.1. Different initiation.
    U18343 mRNA. Translation: AAB26943.1.
    AB000826 Genomic DNA. Translation: BAA19191.1.
    AB000827 mRNA. Translation: BAA19192.1.
    AB000828 mRNA. Translation: BAA19193.1.
    AK141198 mRNA. Translation: BAE24581.1.
    AL844896 Genomic DNA. Translation: CAM22049.1.
    BC066058 mRNA. Translation: AAH66058.1.
    BC082325 mRNA. Translation: AAH82325.1.
    U23721, U23718 Genomic DNA. Translation: AAC52215.1.
    U23721, U23719 Genomic DNA. Translation: AAC52216.1.
    U23721, U23720 Genomic DNA. Translation: AAC52217.1.
    CCDSiCCDS16611.1. [P55144-1]
    CCDS71119.1. [P55144-3]
    PIRiB53743.
    I48862.
    I49152.
    RefSeqiNP_001277729.1. NM_001290800.1. [P55144-3]
    NP_062265.2. NM_019392.2. [P55144-1]
    UniGeneiMm.2901.
    Mm.424496.

    Genome annotation databases

    EnsembliENSMUST00000028763; ENSMUSP00000028763; ENSMUSG00000027298. [P55144-1]
    ENSMUST00000110783; ENSMUSP00000106410; ENSMUSG00000027298. [P55144-3]
    GeneIDi22174.
    KEGGimmu:22174.
    UCSCiuc008luq.1. mouse. [P55144-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05683 mRNA. Translation: AAA19237.1 .
    U18933 mRNA. Translation: AAC52148.1 .
    X78103 mRNA. Translation: CAA54995.1 . Different initiation.
    U18342 mRNA. Translation: AAB26942.1 . Different initiation.
    U18343 mRNA. Translation: AAB26943.1 .
    AB000826 Genomic DNA. Translation: BAA19191.1 .
    AB000827 mRNA. Translation: BAA19192.1 .
    AB000828 mRNA. Translation: BAA19193.1 .
    AK141198 mRNA. Translation: BAE24581.1 .
    AL844896 Genomic DNA. Translation: CAM22049.1 .
    BC066058 mRNA. Translation: AAH66058.1 .
    BC082325 mRNA. Translation: AAH82325.1 .
    U23721 , U23718 Genomic DNA. Translation: AAC52215.1 .
    U23721 , U23719 Genomic DNA. Translation: AAC52216.1 .
    U23721 , U23720 Genomic DNA. Translation: AAC52217.1 .
    CCDSi CCDS16611.1. [P55144-1 ]
    CCDS71119.1. [P55144-3 ]
    PIRi B53743.
    I48862.
    I49152.
    RefSeqi NP_001277729.1. NM_001290800.1. [P55144-3 ]
    NP_062265.2. NM_019392.2. [P55144-1 ]
    UniGenei Mm.2901.
    Mm.424496.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QUP X-ray 1.90 A 485-800 [» ]
    4FEQ X-ray 2.20 A 485-800 [» ]
    4FF8 X-ray 2.40 A 485-800 [» ]
    ProteinModelPortali P55144.
    SMRi P55144. Positions 37-365, 499-785.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204395. 1 interaction.
    IntActi P55144. 1 interaction.
    MINTi MINT-4138931.

    PTM databases

    PhosphoSitei P55144.

    Proteomic databases

    PaxDbi P55144.
    PRIDEi P55144.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028763 ; ENSMUSP00000028763 ; ENSMUSG00000027298 . [P55144-1 ]
    ENSMUST00000110783 ; ENSMUSP00000106410 ; ENSMUSG00000027298 . [P55144-3 ]
    GeneIDi 22174.
    KEGGi mmu:22174.
    UCSCi uc008luq.1. mouse. [P55144-1 ]

    Organism-specific databases

    CTDi 7301.
    MGIi MGI:104294. Tyro3.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00720000108377.
    HOVERGENi HBG006346.
    KOi K05116.
    OMAi DQVYIPV.
    OrthoDBi EOG77DJ5C.
    TreeFami TF317402.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.

    Miscellaneous databases

    ChiTaRSi TYRO3. mouse.
    NextBioi 302127.
    PROi P55144.
    SOURCEi Search...

    Gene expression databases

    Bgeei P55144.
    CleanExi MM_TYRO3.
    Genevestigatori P55144.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF00041. fn3. 2 hits.
    PF07679. I-set. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00060. FN3. 2 hits.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50853. FN3. 2 hits.
    PS50835. IG_LIKE. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RSE, a novel receptor-type tyrosine kinase with homology to Axl/Ufo, is expressed at high levels in the brain."
      Mark M.R., Scadden D.T., Wang Z., Gu Q., Goddard A., Godowski P.J.
      J. Biol. Chem. 269:10720-10728(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Brain.
    2. "Isolation of a receptor tyrosine kinase (DTK) from embryonic stem cells: structure, genetic mapping and analysis of expression."
      Crosier P.S., Lewis P.M., Hall L.R., Vitas M.R., Morris C.M., Beier D.R., Wood C.R., Crosier K.E.
      Growth Factors 11:125-136(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Brain.
    3. "Structure, expression, and activity of Tyro 3, a neural adhesion-related receptor tyrosine kinase."
      Lai C., Gore M., Lemke G.
      Oncogene 9:2567-2578(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Strain: C57BL/6.
    4. "brt, a mouse gene encoding a novel receptor-type protein-tyrosine kinase, is preferentially expressed in the brain."
      Fujimoto J., Yamamoto T.
      Oncogene 9:693-698(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
      Tissue: Brain and Liver.
    5. "Cloning of the cDNA for a novel receptor tyrosine kinase, Sky, predominantly expressed in brain."
      Ohashi K., Mizuno K., Kuma K., Miyata T., Nakamura T.
      Oncogene 9:699-705(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
      Strain: BALB/c.
      Tissue: Brain.
    6. "Isolation and expression analysis of tyro3, a murine growth factor receptor tyrosine kinase preferentially expressed in adult brain."
      Schulz N., Paulhiac C., Lee L., Zhou R.
      Brain Res. Mol. Brain Res. 28:273-280(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
      Strain: BALB/c.
      Tissue: Brain.
    7. "Structure and expression of a murine homologue of sky receptor tyrosine kinase."
      Sasaki M., Enami J.
      J. Biochem. 120:264-270(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
      Strain: BALB/c.
      Tissue: Brain.
    8. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Cerebellum.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    11. "Identification of alternative exons, including a novel exon, in the tyrosine kinase receptor gene Etk2/tyro3 that explain differences in 5' cDNA sequences."
      Biesecker L.G., Giannola D.M., Emerson S.G.
      Oncogene 10:2239-2242(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92 (ISOFORMS 1; 2 AND 3).
      Strain: 129/Sv.
      Tissue: Liver.
    12. "Tyro-3 family receptors are essential regulators of mammalian spermatogenesis."
      Lu Q., Gore M., Zhang Q., Camenisch T., Boast S., Casagranda F., Lai C., Skinner M.K., Klein R., Matsushima G.K., Earp H.S., Goff S.P., Lemke G.
      Nature 398:723-728(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    13. "Transforming activity of receptor tyrosine kinase tyro3 is mediated, at least in part, by the PI3 kinase-signaling pathway."
      Lan Z., Wu H., Li W., Wu S., Lu L., Xu M., Dai W.
      Blood 95:633-638(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIK3R1.
    14. Cited for: FUNCTION IN PLATELET ACTIVATION.
    15. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-181.
    16. "Tubby and tubby-like protein 1 are new MerTK ligands for phagocytosis."
      Caberoy N.B., Zhou Y., Li W.
      EMBO J. 29:3898-3910(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TULP1.
    17. "Protein S protects neurons from excitotoxic injury by activating the TAM receptor Tyro3-phosphatidylinositol 3-kinase-Akt pathway through its sex hormone-binding globulin-like region."
      Zhong Z., Wang Y., Guo H., Sagare A., Fernandez J.A., Bell R.D., Barrett T.M., Griffin J.H., Freeman R.S., Zlokovic B.V.
      J. Neurosci. 30:15521-15534(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NEURON PROTECTION.
    18. "Sertoli cell-initiated testicular innate immune response through toll-like receptor-3 activation is negatively regulated by Tyro3, Axl, and mer receptors."
      Sun B., Qi N., Shang T., Wu H., Deng T., Han D.
      Endocrinology 151:2886-2897(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN IMMUNE RESPONSE INHIBITION.
    19. "Protein S blocks the extrinsic apoptotic cascade in tissue plasminogen activator/N-methyl D-aspartate-treated neurons via Tyro3-Akt-FKHRL1 signaling pathway."
      Guo H., Barrett T.M., Zhong Z., Fernandez J.A., Griffin J.H., Freeman R.S., Zlokovic B.V.
      Mol. Neurodegener. 6:13-13(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiTYRO3_MOUSE
    AccessioniPrimary (citable) accession number: P55144
    Secondary accession number(s): O09070
    , O09080, P70285, Q60752, Q62482, Q62483, Q62484, Q6NZM6, Q78E85, Q78E87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3