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P55144 (TYRO3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Tyro3
Synonyms:Dtk, Rse, Tif
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length880 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.14 Ref.17 Ref.18 Ref.19

Catalytic activity

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

Subunit structure

Monomer and homodimer. Interacts (via N-terminus) with extracellular ligands TULP1 and GAS6. Interacts with PIK3R1; this interaction increases PI3-kinase activity By similarity. Ref.13 Ref.16

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Tissue specificity

Abundant in the brain and lower levels in other tissues.

Post-translational modification

Autophosphorylated By similarity.

Disruption phenotype

knockout mice are fertile, but male animals that lack all three receptors TYRO3, AXL and MERTK produce no mature sperm. Ref.12

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily.

Contains 2 fibronectin type-III domains.

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Sequence caution

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

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

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic cell clearance

Inferred from genetic interaction PubMed 18159085. Source: UniProtKB

forebrain cell migration

Inferred from genetic interaction PubMed 18787040. Source: MGI

natural killer cell differentiation

Inferred from genetic interaction PubMed 16751775. Source: MGI

negative regulation of inflammatory response

Inferred from genetic interaction PubMed 18083102. Source: UniProtKB

negative regulation of innate immune response

Inferred from genetic interaction PubMed 18083102. Source: UniProtKB

negative regulation of lymphocyte activation

Inferred from genetic interaction PubMed 11452127. Source: MGI

negative regulation of neuron apoptotic process

Inferred from genetic interaction PubMed 18787040. Source: MGI

negative regulation of toll-like receptor signaling pathway

Inferred from genetic interaction PubMed 18083102. Source: UniProtKB

neuron cellular homeostasis

Inferred from mutant phenotype Ref.17. Source: UniProtKB

ovulation cycle

Inferred from genetic interaction PubMed 18787040. Source: MGI

platelet activation

Inferred from mutant phenotype Ref.14. Source: MGI

platelet aggregation

Inferred from mutant phenotype PubMed 20546121. Source: UniProtKB

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase B signaling

Inferred from mutant phenotype Ref.17. Source: UniProtKB

secretion by cell

Inferred from mutant phenotype Ref.14. Source: MGI

spermatogenesis

Inferred from genetic interaction Ref.12. Source: UniProtKB

substrate adhesion-dependent cell spreading

Inferred from mutant phenotype Ref.14. Source: MGI

vagina development

Inferred from genetic interaction PubMed 18393392. Source: MGI

   Cellular_componentendoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear envelope

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol 3-kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 18787040. Source: MGI

protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: P55144-1)

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.
Isoform 2 (identifier: P55144-2)

Also known as: II;

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: MALRRSMGWPGLRPLLLAGLASLLLPGSAAA → MGCPAGDWKV...QGAGPAAPSG
Isoform 1 (identifier: P55144-3)

Also known as: I; B;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 880850Tyrosine-protein kinase receptor TYRO3
PRO_0000024479

Regions

Topological domain31 – 419389Extracellular Potential
Transmembrane420 – 44021Helical; Potential
Topological domain441 – 880440Cytoplasmic Potential
Domain31 – 11888Ig-like C2-type 1
Domain129 – 20981Ig-like C2-type 2
Domain217 – 31094Fibronectin type-III 1
Domain315 – 40692Fibronectin type-III 2
Domain508 – 785278Protein kinase
Nucleotide binding514 – 5229ATP By similarity

Sites

Active site6451Proton acceptor By similarity
Binding site5401ATP By similarity

Amino acid modifications

Modified residue6711Phosphotyrosine; by autocatalysis By similarity
Modified residue6751Phosphotyrosine; by autocatalysis By similarity
Modified residue6761Phosphotyrosine; by autocatalysis By similarity
Modified residue7941Phosphotyrosine; by autocatalysis By similarity
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation1811N-linked (GlcNAc...) Ref.15
Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation3561N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 107 By similarity
Disulfide bond150 ↔ 193 By similarity

Natural variations

Alternative sequence1 – 3131MALRR…GSAAA → MDDKLENTLGRWAGENGLSI GEYLAIK in isoform 1.
VSP_012548
Alternative sequence1 – 3131MALRR…GSAAA → MGCPAGDWKVFGEGGAWPGA CPGSEAGPPQRQRSGQGAGP AAPSG in isoform 2.
VSP_012549

Experimental info

Sequence conflict6301A → R in CAA54995. Ref.3
Sequence conflict637 – 6393SSR → AIK in BAA19191. Ref.5
Sequence conflict637 – 6393SSR → AIK in BAA19192. Ref.5
Sequence conflict8111V → L in AAA19237. Ref.1
Sequence conflict8111V → L in AAC52148. Ref.2
Sequence conflict8111V → L in BAA19193. Ref.5
Sequence conflict8111V → L in AAB26942. Ref.6
Sequence conflict8111V → L in AAB26943. Ref.6

Secondary structure

....................................... 880
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 (III) [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 2794316CB0034617

FASTA88096,208
        10         20         30         40         50         60 
MALRRSMGWP GLRPLLLAGL ASLLLPGSAA AGLKLMGAPV KMTVSQGQPV KLNCSVEGME 

        70         80         90        100        110        120 
DPDIHWMKDG TVVQNASQVS ISISEHSWIG LLSLKSVERS DAGLYWCQVK DGEETKISQS 

       130        140        150        160        170        180 
VWLTVEGVPF FTVEPKDLAV PPNAPFQLSC EAVGPPEPVT IYWWRGLTKV GGPAPSPSVL 

       190        200        210        220        230        240 
NVTGVTQRTE FSCEARNIKG LATSRPAIVR LQAPPAAPFN TTVTTISSYN ASVAWVPGAD 

       250        260        270        280        290        300 
GLALLHSCTV QVAHAPGEWE ALAVVVPVPP FTCLLRNLAP ATNYSLRVRC ANALGPSPYG 

       310        320        330        340        350        360 
DWVPFQTKGL APARAPQNFH AIRTDSGLIL EWEEVIPEDP GEGPLGPYKL SWVQENGTQD 

       370        380        390        400        410        420 
ELMVEGTRAN LTDWDPQKDL ILRVCASNAI GDGPWSQPLV VSSHDHAGRQ GPPHSRTSWV 

       430        440        450        460        470        480 
PVVLGVLTAL ITAAALALIL LRKRRKETRF GQAFDSVMAR GEPAVHFRAA RSFNRERPER 

       490        500        510        520        530        540 
IEATLDSLGI SDELKEKLED VLIPEQQFTL GRMLGKGEFG SVREAQLKQE DGSFVKVAVK 

       550        560        570        580        590        600 
MLKADIIASS DIEEFLREAA CMKEFDHPHV AKLVGVSLRS RAKGRLPIPM VILPFMKHGD 

       610        620        630        640        650        660 
LHAFLLASRI GENPFNLPLQ TLVRFMVDIA CGMEYLSSRN FIHRDLAARN CMLAEDMTVC 

       670        680        690        700        710        720 
VADFGLSRKI YSGDYYRQGC ASKLPVKWLA LESLADNLYT VHSDVWAFGV TMWEIMTRGQ 

       730        740        750        760        770        780 
TPYAGIENAE IYNYLIGGNR LKQPPECMEE VYDLMYQCWS ADPKQRPSFT CLRMELENIL 

       790        800        810        820        830        840 
GHLSVLSTSQ DPLYINIERA EQPTESGSPE VHCGERSSSE AGDGSGVGAV GGIPSDSRYI 

       850        860        870        880 
FSPGGLSESP GQLEQQPESP LNENQRLLLL QQGLLPHSSC 

« Hide

Isoform 2 (II) [UniParc].

Checksum: 4F45E58F5B466FEA
Show »

FASTA89497,343
Isoform 1 (I) (B) [UniParc].

Checksum: 5C7813084CC59D56
Show »

FASTA87696,042

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Role of Gas6 receptors in platelet signaling during thrombus stabilization and implications for antithrombotic therapy."
Angelillo-Scherrer A., Burnier L., Flores N., Savi P., DeMol M., Schaeffer P., Herbert J.M., Lemke G., Goff S.P., Matsushima G.K., Earp H.S., Vesin C., Hoylaerts M.F., Plaisance S., Collen D., Conway E.M., Wehrle-Haller B., Carmeliet P.
J. Clin. Invest. 115:237-246(2005) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS16611.1. [P55144-1]
PIRB53743.
I48862.
I49152.
RefSeqNP_001277729.1. NM_001290800.1. [P55144-3]
NP_062265.2. NM_019392.2. [P55144-1]
UniGeneMm.2901.
Mm.424496.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QUPX-ray1.90A485-800[»]
4FEQX-ray2.20A485-800[»]
4FF8X-ray2.40A485-800[»]
ProteinModelPortalP55144.
SMRP55144. Positions 37-365, 499-785.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204395. 1 interaction.
IntActP55144. 1 interaction.
MINTMINT-4138931.

PTM databases

PhosphoSiteP55144.

Proteomic databases

PaxDbP55144.
PRIDEP55144.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028763; ENSMUSP00000028763; ENSMUSG00000027298. [P55144-1]
ENSMUST00000110783; ENSMUSP00000106410; ENSMUSG00000027298. [P55144-3]
GeneID22174.
KEGGmmu:22174.
UCSCuc008luq.1. mouse. [P55144-1]

Organism-specific databases

CTD7301.
MGIMGI:104294. Tyro3.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108377.
HOVERGENHBG006346.
KOK05116.
OMADQVYIPV.
OrthoDBEOG77DJ5C.
TreeFamTF317402.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

BgeeP55144.
CleanExMM_TYRO3.
GenevestigatorP55144.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR003961. 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]
PfamPF00041. fn3. 2 hits.
PF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00060. FN3. 2 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50853. 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]
ProtoNetSearch...

Other

ChiTaRSTYRO3. mouse.
NextBio302127.
PROP55144.
SOURCESearch...

Entry information

Entry nameTYRO3_MOUSE
AccessionPrimary (citable) accession number: P55144
Secondary accession number(s): O09070 expand/collapse secondary AC list , O09080, P70285, Q60752, Q62482, Q62483, Q62484, Q6NZM6, Q78E85, Q78E87
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot