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P55144

- TYRO3_MOUSE

UniProt

P55144 - TYRO3_MOUSE

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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

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. peptidyl-tyrosine phosphorylation Source: GOC
  12. platelet activation Source: MGI
  13. platelet aggregation Source: UniProtKB
  14. protein autophosphorylation Source: UniProtKB
  15. protein kinase B signaling Source: UniProtKB
  16. secretion by cell Source: MGI
  17. spermatogenesis Source: UniProtKB
  18. substrate adhesion-dependent cell spreading Source: MGI
  19. vagina development Source: MGI
Complete GO annotation...

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-KW
Complete GO annotation...

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

MaxQBiP55144.
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 – 5179Combined sources
Beta strandi520 – 5267Combined sources
Beta strandi536 – 5416Combined sources
Helixi550 – 56213Combined sources
Beta strandi575 – 5784Combined sources
Beta strandi589 – 5946Combined sources
Helixi601 – 6099Combined sources
Helixi619 – 63820Combined sources
Helixi648 – 6503Combined sources
Beta strandi651 – 6533Combined sources
Beta strandi659 – 6613Combined sources
Helixi686 – 6883Combined sources
Helixi691 – 6966Combined sources
Helixi701 – 71616Combined sources
Turni722 – 7254Combined sources
Helixi728 – 7303Combined sources
Helixi731 – 7366Combined sources
Helixi749 – 7579Combined sources
Helixi763 – 7653Combined sources
Helixi769 – 78113Combined sources

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.
GeneTreeiENSGT00760000119065.
HOVERGENiHBG006346.
InParanoidiP55144.
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

        10         20         30         40         50
MALRRSMGWP GLRPLLLAGL ASLLLPGSAA AGLKLMGAPV KMTVSQGQPV
60 70 80 90 100
KLNCSVEGME DPDIHWMKDG TVVQNASQVS ISISEHSWIG LLSLKSVERS
110 120 130 140 150
DAGLYWCQVK DGEETKISQS VWLTVEGVPF FTVEPKDLAV PPNAPFQLSC
160 170 180 190 200
EAVGPPEPVT IYWWRGLTKV GGPAPSPSVL NVTGVTQRTE FSCEARNIKG
210 220 230 240 250
LATSRPAIVR LQAPPAAPFN TTVTTISSYN ASVAWVPGAD GLALLHSCTV
260 270 280 290 300
QVAHAPGEWE ALAVVVPVPP FTCLLRNLAP ATNYSLRVRC ANALGPSPYG
310 320 330 340 350
DWVPFQTKGL APARAPQNFH AIRTDSGLIL EWEEVIPEDP GEGPLGPYKL
360 370 380 390 400
SWVQENGTQD ELMVEGTRAN LTDWDPQKDL ILRVCASNAI GDGPWSQPLV
410 420 430 440 450
VSSHDHAGRQ GPPHSRTSWV PVVLGVLTAL ITAAALALIL LRKRRKETRF
460 470 480 490 500
GQAFDSVMAR GEPAVHFRAA RSFNRERPER IEATLDSLGI SDELKEKLED
510 520 530 540 550
VLIPEQQFTL GRMLGKGEFG SVREAQLKQE DGSFVKVAVK MLKADIIASS
560 570 580 590 600
DIEEFLREAA CMKEFDHPHV AKLVGVSLRS RAKGRLPIPM VILPFMKHGD
610 620 630 640 650
LHAFLLASRI GENPFNLPLQ TLVRFMVDIA CGMEYLSSRN FIHRDLAARN
660 670 680 690 700
CMLAEDMTVC VADFGLSRKI YSGDYYRQGC ASKLPVKWLA LESLADNLYT
710 720 730 740 750
VHSDVWAFGV TMWEIMTRGQ TPYAGIENAE IYNYLIGGNR LKQPPECMEE
760 770 780 790 800
VYDLMYQCWS ADPKQRPSFT CLRMELENIL GHLSVLSTSQ DPLYINIERA
810 820 830 840 850
EQPTESGSPE VHCGERSSSE AGDGSGVGAV GGIPSDSRYI FSPGGLSESP
860 870 880
GQLEQQPESP LNENQRLLLL QQGLLPHSSC
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

MaxQBi P55144.
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 ENSGT00760000119065.
HOVERGENi HBG006346.
InParanoidi P55144.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 143 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