TYRO3_DANRE
ID TYRO3_DANRE Reviewed; 874 AA.
AC Q9YI66;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Tyrosine-protein kinase receptor TYRO3;
DE EC=2.7.10.1;
DE AltName: Full=Tyrosine-protein kinase DTK;
DE Flags: Precursor;
GN Name=tyro3; Synonyms=dtk;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Walshe J.A., Jansa-Perez M., Crosier K.E., Evans C.W., Crosier P.S.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=9087716;
RA Jansa Perez M., Walshe J.A., Crosier K.E., Crosier P.S.;
RT "Expression of the DTK receptor tyrosine kinase during zebrafish
RT development.";
RL Int. J. Dev. Biol. 40:101S-102S(1996).
CC -!- FUNCTION: May be involved in cell adhesion processes, particularly in
CC the central nervous system. {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 -!- DEVELOPMENTAL STAGE: First detected in gastrula. Detected throughout
CC the embryo. Detected in adult. {ECO:0000269|PubMed:9087716}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. AXL/UFO subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AF021344; AAD01694.1; -; mRNA.
DR AlphaFoldDB; Q9YI66; -.
DR SMR; Q9YI66; -.
DR STRING; 7955.ENSDARP00000116623; -.
DR PaxDb; Q9YI66; -.
DR ZFIN; ZDB-GENE-990714-13; tyro3.
DR eggNOG; ENOG502QRYR; Eukaryota.
DR InParanoid; Q9YI66; -.
DR PhylomeDB; Q9YI66; -.
DR PRO; PR:Q9YI66; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:0003094; P:glomerular filtration; IMP:ZFIN.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR GO; GO:0072015; P:podocyte development; IMP:ZFIN.
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; 1.
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; 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; 2.
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 2: Evidence at transcript 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..874
FT /note="Tyrosine-protein kinase receptor TYRO3"
FT /id="PRO_0000346115"
FT TOPO_DOM 21..411
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..874
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..106
FT /note="Ig-like C2-type 1"
FT DOMAIN 117..198
FT /note="Ig-like C2-type 2"
FT DOMAIN 202..297
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 299..403
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 497..768
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 634
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 503..511
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 665
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 138..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 874 AA; 97599 MW; 1B538628272F5CE7 CRC64;
MEVSLCILLF LLHFNEGIHG VRFTQKPFHQ TVTQGNMVRL GCAFEGLSEP EIIWMKDGEK
LFSTDQMYIT LDPYHWETFH SVKSVQQQDA GKYWCEVEYH GAIISSEPAW ITVAGVPHFG
VEPEDVAAFA GESFNLTCAA SGPPEPVEVL WWLGGEQNGD FTPSPSVLFV KGVNESIKFH
CEPRNARGIS VSRTGTVHIK ARPDSLGRTG HHVSDFNITL TWSPGFTGHS QLSTCTIQLS
RGPGEVKLPD VVVEVPPFQH VFEGLRSYSN YSVRVRCDNE VGSSPFSPWV DFHTPQAAPS
AAPKNFTFDL SEQQLTLSWA TLEQEELRGR LQEELRGRLL AYKLQWNQGG ESQDPLLFKE
NVAHLSGAGR FFNATFQVAA CTMAGCGPWS QPVLVMPVSA MQAQTQRGHM WVGLLFGLLV
ATMVGLLLIV LIRNRGKETQ FGSAFAAQGA EVPVSFTAAR SFNRQFPELP ESTLDSLGIN
SDLKAKLQDV LIFERLLTLG RMLGKGEFGS VREAFLKSEN NSGQKVAVKV LKTDINSSSD
IEQCLKEAAY MKDFHHPNVI QLIGVSLHRR AQQRLPIPMV ILPFMKHGDL HTFLLMSRLG
DEPFTVSQQI LIQFMLDIAR GMEYLSNKNI IHRDLAARNC MLNENMSVCV ADFGLSKKIY
SGDYYRQGSV SKLPVKWIAL ESLADNVYTT QSDVWAFGVT MWEIMTRGQT PYPGVENSEI
YEYLIKGERL KQPPDCPADI YEIMHSCWSP VPKCRPSFQH LIDQLELLWA KLNPAPVKEP
LLYVNLEEED GEQANSGTRS SEEPSWGVPW QCAGIEEDEK DWLMVSSGAA LAIGGDYRYI
IGPSVSAIDE ESRHSEDGLS EDIREEEEDV IINV
