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Protein

Tyrosine-protein kinase receptor TYRO3

Gene

Tyro3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

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

GO - Biological processi

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. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase receptor TYRO3 (EC:2.7.10.1)
Alternative name(s):
Tyrosine-protein kinase SKY
Gene namesi
Name:Tyro3
Synonyms:Sky
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3923. Tyro3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 419389ExtracellularSequence analysisAdd
BLAST
Transmembranei420 – 44021HelicalSequence analysisAdd
BLAST
Topological domaini441 – 880440CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • nuclear envelope Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Chaini31 – 880850Tyrosine-protein kinase receptor TYRO3PRO_0000024480Add
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...)Sequence analysis
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 residuei456 – 4561PhosphoserineBy similarity
Modified residuei671 – 6711Phosphotyrosine; by autocatalysisBy similarity
Modified residuei675 – 6751Phosphotyrosine; by autocatalysisBy similarity
Modified residuei676 – 6761Phosphotyrosine; by autocatalysisBy similarity
Modified residuei794 – 7941Phosphotyrosine; by autocatalysisBy similarity
Modified residuei808 – 8081PhosphoserineBy similarity
Modified residuei859 – 8591PhosphoserineCombined sources

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP55146.
PRIDEiP55146.

PTM databases

iPTMnetiP55146.
PhosphoSiteiP55146.

Expressioni

Tissue specificityi

Abundant in the brain and lower levels in other tissues.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • phosphatidylinositol 3-kinase binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007656.

Structurei

3D structure databases

ProteinModelPortaliP55146.
SMRiP55146. Positions 37-212, 496-781.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 11888Ig-like C2-type 1Add
BLAST
Domaini129 – 21082Ig-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

eggNOGiENOG410IG6I. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000231685.
HOVERGENiHBG006346.
InParanoidiP55146.
KOiK05116.
PhylomeDBiP55146.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR003961. FN3_dom.
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. 2 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
SSF49265. 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]

Sequencei

Sequence statusi: Complete.

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

P55146-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRRSMGRP GLRPLLLAGL ASLLLPGSAA AGLKLMGAPV KMTVSQGQPV
60 70 80 90 100
KLNCSVEGMD DPDIHWMKDG AVVQNASQVS ISISEQNWIG LLSLKSAERS
110 120 130 140 150
DAGLYWCQVK DGEETKISQS VWLTVEGVPF FTVEPKDLAV PPNVPFQLSC
160 170 180 190 200
EAVGPPEPVT IFWWRGPTKV GGPASSPSVL NVTGVTQRTE FSCEAHNIKG
210 220 230 240 250
LATSRPAIIR LQAPPAAPFN ITVTTISSSN 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 ELMVEGTTAN LTDWDPQKDL VLRVCASNAI 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 IYNYLISGNR LKQPPECMEE
760 770 780 790 800
VYDLMYQCWS ADPKQRPSFT CLRMELENIL GHLSVLSTSQ DPLYINIERA
810 820 830 840 850
GQPAENGSPE LPCGEQSSSE AGDGSGMGAI GGIPSDCRYI FSPGGLAESP
860 870 880
GQLEQQPESP LNENQRLLLL QQGLLPHSSC
Length:880
Mass (Da):95,919
Last modified:October 1, 1996 - v1
Checksum:iC3751E86AAE5FA5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37880 mRNA. Translation: BAA07119.1.
PIRiJC4166.
RefSeqiNP_058788.1. NM_017092.1.
UniGeneiRn.8883.

Genome annotation databases

GeneIDi25232.
KEGGirno:25232.
UCSCiRGD:3923. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37880 mRNA. Translation: BAA07119.1.
PIRiJC4166.
RefSeqiNP_058788.1. NM_017092.1.
UniGeneiRn.8883.

3D structure databases

ProteinModelPortaliP55146.
SMRiP55146. Positions 37-212, 496-781.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007656.

PTM databases

iPTMnetiP55146.
PhosphoSiteiP55146.

Proteomic databases

PaxDbiP55146.
PRIDEiP55146.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25232.
KEGGirno:25232.
UCSCiRGD:3923. rat.

Organism-specific databases

CTDi7301.
RGDi3923. Tyro3.

Phylogenomic databases

eggNOGiENOG410IG6I. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000231685.
HOVERGENiHBG006346.
InParanoidiP55146.
KOiK05116.
PhylomeDBiP55146.

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Miscellaneous databases

PROiP55146.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR003961. FN3_dom.
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. 2 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
SSF49265. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiTYRO3_RAT
AccessioniPrimary (citable) accession number: P55146
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.