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Q98949 (TYRO3_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase receptor TYRO3

EC=2.7.10.1
Alternative name(s):
Retina-expressed kinase
Short name=Rek
Gene names
Name:TYRO3
Synonyms:REK
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length873 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. 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, enhances PI3-kinase activity and activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes By similarity.

Catalytic activity

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

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

Detected in embryonic retina (at protein level). detected in brain, retina, kidney and in retinal Mueller glia-like cells. Ref.1

Post-translational modification

Autophosphorylated on tyrosine residues. Ref.1

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 873845Tyrosine-protein kinase receptor TYRO3
PRO_0000346114

Regions

Topological domain29 – 416388Extracellular Potential
Transmembrane417 – 43721Helical; Potential
Topological domain438 – 873436Cytoplasmic Potential
Domain29 – 11688Ig-like C2-type 1
Domain127 – 20882Ig-like C2-type 2
Domain213 – 30593Fibronectin type-III 1
Domain310 – 40495Fibronectin type-III 2
Domain505 – 776272Protein kinase
Nucleotide binding511 – 5199ATP By similarity

Sites

Active site6421Proton acceptor By similarity
Binding site5371ATP By similarity

Amino acid modifications

Modified residue6731Phosphotyrosine; by autocatalysis By similarity
Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation2811N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential
Disulfide bond52 ↔ 105 By similarity
Disulfide bond148 ↔ 191 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q98949 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 6294E173C5D8104E

FASTA87396,402
        10         20         30         40         50         60 
MELRRSMALP RLLLLGLWAA ALRDGAVAAG MKFTGSPIKL KVSQGQPVKL NCSLEGMEDP 

        70         80         90        100        110        120 
EMLWIKDGAV VQSVDQVYIP VDEDHWIGFL SLKSVERTDS GKYWCQVENG GKKEESQQVW 

       130        140        150        160        170        180 
LIVEGVPYFT VEPEDVSVSP NAPFHMACAA VGPPEPVTIV WWMGDSRVGL PDISPSILNV 

       190        200        210        220        230        240 
SGINQSTMFS CEAHNVKGLS SSRTATVQIK AMPLPPLNVT VSQVTSSNAS VVWVPGFDGR 

       250        260        270        280        290        300 
APLHSCTLQV AESPDGQEVS TEVAPVPPFA YGVQGLKHST NYSVRVQCSN EMGSSPFTER 

       310        320        330        340        350        360 
VYFQTLELAP SSTPQNIHVI QRDPGLVLEW EGVAPDVLKE NVLGYRLEWI QDNVTQGEMI 

       370        380        390        400        410        420 
VQDTKANLTT WNPLKDLIIR VCVLNSAGCG PWSDLFLLEA QEVMGGQRQP PYGTSWVPVA 

       430        440        450        460        470        480 
LGILTALVTA VALALILLRK RRKETRFGHA FGSVVGRGDP AVHFRAARSF NREGPELIEA 

       490        500        510        520        530        540 
TLESVGISDE LKTKLKDVLI QEQQFTLGRM LGKGEFGSVR EALLKLDDGS FQKVAVKMLK 

       550        560        570        580        590        600 
ADIFTSTDIE EFLREAACMK EFDHPHVTKL IGVSLRSRPK GRLPIPMVIL PFMKHGDLHA 

       610        620        630        640        650        660 
FLLMSRIGEN PFNLPLQTLL KFMIDIASGM EYLSSKNFIH RDLAARNCML DENMNVSVAD 

       670        680        690        700        710        720 
FGLSKKIYSG DYYRQGCASK LPVKWLALES LADNLYTTHS DVWAFGVTMW EIVTRGQTPY 

       730        740        750        760        770        780 
AGIENAEIYN YLISGNRLKQ PPECLEDVYD LMCRCWHPEP KLRPSFGVLR SQLEMIRGRM 

       790        800        810        820        830        840 
STLSLSQDPL YVNIGKDKES SVSDPAVHTS FGNTDGDETI AGAAAAAITS DYRYIMSPLC 

       850        860        870 
LGDDVEGERH PEGQEGENKS LLYELETEGE KSC 

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References

[1]"Rek, a gene expressed in retina and brain, encodes a receptor tyrosine kinase of the Axl/Tyro3 family."
Biscardi J.S., Denhez F., Buehler G.F., Chesnutt D.A., Baragona S.C., O'Bryan J.P., Der C.J., Fiordalisi J.J., Fults D.W., Maness P.F.
J. Biol. Chem. 271:29049-29059(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, TISSUE SPECIFICITY.
Tissue: Embryonic brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U70045 mRNA. Translation: AAC60041.1.
IPIIPI00575698.
RefSeqNP_989958.1. NM_204627.2.
UniGeneGga.4266.

3D structure databases

ProteinModelPortalQ98949.
SMRQ98949. Positions 35-210.
ModBaseSearch...

Proteomic databases

PaxDbQ98949.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID395336.
KEGGgga:395336.

Organism-specific databases

CTD7301.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000231685.
HOVERGENHBG006346.
InParanoidQ98949.
KOK05116.
OrthoDBEOG4H4639.

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_cat_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. 1 hit.
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. FN_III-like. 2 hits.
SSF56112. Kinase_like. 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

NextBio20815421.

Entry information

Entry nameTYRO3_CHICK
AccessionPrimary (citable) accession number: Q98949
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 1, 1997
Last modified: May 29, 2013
This is version 96 of the entry and version 1 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