TYRO3_CHICK
ID TYRO3_CHICK Reviewed; 873 AA.
AC Q98949;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Tyrosine-protein kinase receptor TYRO3;
DE EC=2.7.10.1;
DE AltName: Full=Retina-expressed kinase;
DE Short=Rek;
DE Flags: Precursor;
GN Name=TYRO3; Synonyms=REK;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic brain;
RX PubMed=8910558; DOI=10.1074/jbc.271.46.29049;
RA Biscardi J.S., Denhez F., Buehler G.F., Chesnutt D.A., Baragona S.C.,
RA O'Bryan J.P., Der C.J., Fiordalisi J.J., Fults D.W., Maness P.F.;
RT "Rek, a gene expressed in retina and brain, encodes a receptor tyrosine
RT kinase of the Axl/Tyro3 family.";
RL J. Biol. Chem. 271:29049-29059(1996).
CC -!- FUNCTION: Receptor tyrosine kinase that transduces signals from the
CC extracellular matrix into the cytoplasm by binding to several ligands.
CC Regulates many physiological processes including cell survival,
CC migration and differentiation. Ligand binding at the cell surface
CC induces dimerization and autophosphorylation of TYRO3 on its
CC intracellular domain that provides docking sites for downstream
CC signaling molecules. Following activation by ligand, enhances PI3-
CC kinase activity and activates the AKT survival pathway, including
CC nuclear translocation of NF-kappa-B and up-regulation of transcription
CC of NF-kappa-B-regulated genes (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic retina (at protein level).
CC detected in brain, retina, kidney and in retinal Mueller glia-like
CC cells. {ECO:0000269|PubMed:8910558}.
CC -!- PTM: Autophosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:8910558}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. AXL/UFO subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U70045; AAC60041.1; -; mRNA.
DR RefSeq; NP_989958.1; NM_204627.2.
DR AlphaFoldDB; Q98949; -.
DR SMR; Q98949; -.
DR BioGRID; 675626; 1.
DR STRING; 9031.ENSGALP00000014051; -.
DR PaxDb; Q98949; -.
DR GeneID; 395336; -.
DR KEGG; gga:395336; -.
DR CTD; 558; -.
DR VEuPathDB; HostDB:geneid_395336; -.
DR eggNOG; ENOG502QRYR; Eukaryota.
DR InParanoid; Q98949; -.
DR OrthoDB; 263089at2759; -.
DR PhylomeDB; Q98949; -.
DR PRO; PR:Q98949; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..873
FT /note="Tyrosine-protein kinase receptor TYRO3"
FT /id="PRO_0000346114"
FT TOPO_DOM 29..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..873
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..116
FT /note="Ig-like C2-type 1"
FT DOMAIN 127..208
FT /note="Ig-like C2-type 2"
FT DOMAIN 215..308
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 310..403
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 505..776
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 845..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 642
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 511..519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 673
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 148..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 873 AA; 96402 MW; 6294E173C5D8104E CRC64;
MELRRSMALP RLLLLGLWAA ALRDGAVAAG MKFTGSPIKL KVSQGQPVKL NCSLEGMEDP
EMLWIKDGAV VQSVDQVYIP VDEDHWIGFL SLKSVERTDS GKYWCQVENG GKKEESQQVW
LIVEGVPYFT VEPEDVSVSP NAPFHMACAA VGPPEPVTIV WWMGDSRVGL PDISPSILNV
SGINQSTMFS CEAHNVKGLS SSRTATVQIK AMPLPPLNVT VSQVTSSNAS VVWVPGFDGR
APLHSCTLQV AESPDGQEVS TEVAPVPPFA YGVQGLKHST NYSVRVQCSN EMGSSPFTER
VYFQTLELAP SSTPQNIHVI QRDPGLVLEW EGVAPDVLKE NVLGYRLEWI QDNVTQGEMI
VQDTKANLTT WNPLKDLIIR VCVLNSAGCG PWSDLFLLEA QEVMGGQRQP PYGTSWVPVA
LGILTALVTA VALALILLRK RRKETRFGHA FGSVVGRGDP AVHFRAARSF NREGPELIEA
TLESVGISDE LKTKLKDVLI QEQQFTLGRM LGKGEFGSVR EALLKLDDGS FQKVAVKMLK
ADIFTSTDIE EFLREAACMK EFDHPHVTKL IGVSLRSRPK GRLPIPMVIL PFMKHGDLHA
FLLMSRIGEN PFNLPLQTLL KFMIDIASGM EYLSSKNFIH RDLAARNCML DENMNVSVAD
FGLSKKIYSG DYYRQGCASK LPVKWLALES LADNLYTTHS DVWAFGVTMW EIVTRGQTPY
AGIENAEIYN YLISGNRLKQ PPECLEDVYD LMCRCWHPEP KLRPSFGVLR SQLEMIRGRM
STLSLSQDPL YVNIGKDKES SVSDPAVHTS FGNTDGDETI AGAAAAAITS DYRYIMSPLC
LGDDVEGERH PEGQEGENKS LLYELETEGE KSC
