TYRO3_XENTR
ID TYRO3_XENTR Reviewed; 881 AA.
AC A0JM20;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Tyrosine-protein kinase receptor TYRO3;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=tyro3;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: Tyrosine phosphorylated upon receptor stimulation. {ECO:0000250}.
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; BC125706; AAI25707.1; -; mRNA.
DR RefSeq; NP_001072731.1; NM_001079263.1.
DR AlphaFoldDB; A0JM20; -.
DR SMR; A0JM20; -.
DR STRING; 8364.ENSXETP00000060585; -.
DR PaxDb; A0JM20; -.
DR GeneID; 780188; -.
DR KEGG; xtr:780188; -.
DR CTD; 7301; -.
DR Xenbase; XB-GENE-922144; tyro3.
DR eggNOG; ENOG502QRYR; Eukaryota.
DR InParanoid; A0JM20; -.
DR OMA; NRERPEC; -.
DR OrthoDB; 263089at2759; -.
DR TreeFam; TF317402; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000000052; Expressed in brain and 12 other tissues.
DR ExpressionAtlas; A0JM20; baseline.
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; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..881
FT /note="Tyrosine-protein kinase receptor TYRO3"
FT /id="PRO_0000346117"
FT TOPO_DOM 29..414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..881
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..114
FT /note="Ig-like C2-type 1"
FT DOMAIN 125..206
FT /note="Ig-like C2-type 2"
FT DOMAIN 213..306
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 311..401
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 503..774
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 846..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 640
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 509..517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 671
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 146..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 881 AA; 98019 MW; CBB00EDE8FDEF8E3 CRC64;
MVNPGPPGLI AGLLLAALSL SSVDGTKALG FVGHGYNMTV SQGHEAKLNC SLQGMEEPEI
QWLKDGVPVQ SADQMYIPVD EDHWISFLSL KNVERPDAGR YWCEAEHSGR KSVSDAIWVM
VEGVPYFTLE PKDLSVTPNS PFNMTCAAVG PPEPLVIFWW VGDSPLGKSE SSPSVLQIPG
IRERTAFSCE AHNAKGVSSS RTAIVEVKGL PYPPFNVTIS KVTGSTATVT WSPGFNSFSL
IKSCTIQVQS LHGNREMYSR LTSVPPFAVV LDDLQPLTNH SVRVQCTNEM GASPFSEWIT
FNTKEKVPQL IPQNVHMTKT DSCLLLDWED VDPDKEGYNI LGFKVQWEQE NTTQGELFVQ
ENQANLTKWN PEKDLTIRIC IANAAGCGPW SEFLLAGSKE EAGKQRHPHT RMSWVPMVLG
ILTALVTVVA MTLIFLRKGR KETRFGNMLG SMLGRGGPVI QFTAARSFNR RGPEVMEATL
DSIGISDELK SKLKDVLIQQ QQFTLGRTLG KGEFGSVREA QLKMEDDTMQ KVAVKMLKAE
IFCSSDIEEF LREAAFMKEF DHPNVCKLIG VSLRSRTKGR LPVPMVILPF MKHGDLHTFL
LMSRIGEEPI ALPIQTLVRF MIDICSGMEY LSSKNFIHRD LATRNCMLNE DMTVCVADFG
LSKKIYSGDY YRQGCASKLP VKWLALESLA DNVYTVHSDV WAFGVTLWEI VTRGQTPYAG
VENSEIYSYL TAGNRLKQPP DCLDELYEMM CQCWITEPKR RPSFVDLKRR LEAIWGRLSI
LSASHDQLYV NLGETCGAAA AVSGLHSAFC KEEDYCAGPS QTCGTSAITS DYRYIVNPGC
LREGNEWSSS AQNGEARGLL HEEEEEEEEE EMQEEQVVIT L
