TYRO3_XENLA
ID TYRO3_XENLA Reviewed; 880 AA.
AC Q8QFP9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Tyrosine-protein kinase receptor TYRO3;
DE EC=2.7.10.1;
DE AltName: Full=Xenopus kinase of Sky family;
DE Short=Xksy;
DE Flags: Precursor;
GN Name=tyro3; Synonyms=ksy;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Tail bud;
RX PubMed=12034491; DOI=10.1016/s0378-1119(02)00483-3;
RA Kishi Y.A., Funakoshi H., Matsumoto K., Nakamura T.;
RT "Molecular cloning, expression and partial characterization of Xksy,
RT Xenopus member of the Sky family of receptor tyrosine kinases.";
RL Gene 288:29-40(2002).
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:0000269|PubMed:12034491};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:12034491}.
CC -!- TISSUE SPECIFICITY: Detected in brain, spinal cord, intestine, lung,
CC stomach, ovary, testis, skin and eye. {ECO:0000269|PubMed:12034491}.
CC -!- DEVELOPMENTAL STAGE: Levels are high at cleavage and blastula stage,
CC and low at gastrulation stage. Subsequently, levels increase from mid-
CC neurulation to the tail bud stage. Detected in embryonic brain at the
CC tail bud stage. {ECO:0000269|PubMed:12034491}.
CC -!- PTM: Tyrosine phosphorylated upon receptor stimulation.
CC {ECO:0000269|PubMed:12034491}.
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; AB022787; BAB87808.1; -; mRNA.
DR RefSeq; NP_001082223.1; NM_001088754.2.
DR AlphaFoldDB; Q8QFP9; -.
DR SMR; Q8QFP9; -.
DR GeneID; 398301; -.
DR KEGG; xla:398301; -.
DR CTD; 398301; -.
DR Xenbase; XB-GENE-922154; tyro3.L.
DR OMA; VRCTNAL; -.
DR OrthoDB; 263089at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 398301; Expressed in brain and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 2.
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 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..880
FT /note="Tyrosine-protein kinase receptor TYRO3"
FT /id="PRO_0000346116"
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..880
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..880
FT /note="Disordered"
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 880 AA; 97934 MW; A36D29C2ED2C8832 CRC64;
MVYPGPPGLI AGLLLAALSL SCVDGAKALG FVGHGYNLTV SQGHEAKLNC SLQGIEEPEI
QWLKDGVPVQ SADQMYIPVD EDHWISFLSL KNVERPDAGK YWCEAEHSGR KSVSDAIWIM
VEGVPYFTLE PKDLSVTPNS PFNMTCAAVG PPEPLVIIWW VGDSPLGKSE SSPSVLQMSG
IHERTAFSCE AHNAKGVSSS RTAIVEVKGL PYPPFNVTIS KVTGSTATVT WFPGFNSFSL
IKSCTIQVQS LHGNREMYSR LISAPPFAVL LDELQPLTNH SVRVQCTNEM GASPFTEWRT
FHTKETVPQL LPQNVHMTKT ETSLLLDWEE VEPDREGYNI LGFKVQWEQE NATQGELFVQ
ENQANLTKWN PEKDLTIRIC IANAAGCGPW SEFLLAGSKE EAGKQRHPHT RMSWVPMVLG
ILTALVTVVA MTLIFLRKGR KETRFGNMLG SMLGRGGPVI QFTAARSFNR RGPEMMEATL
DSIGISEELK SKLKDVLIQQ QQFTLGRTLG KGEFGSVREA QLKMEDDTMQ KVAVKMLKAE
IFCSSDIEEF LREAAFMKEF DHPNVCKLIG VSLRSRTKGR LPVPMVILPF MKHGDLHTFL
LMSRIGEEPI TLPVQTLVRF MIDICSGMEY LSSKNFIHRD LATRNCMLNE DMTVCVADFG
LSKKIYSGDY YRQGCASKLP VKWLALESLA DNVYTVHSDV WAFGVTLWEI ATLGQTPYAG
VENSEIYSYL IAGNRLKQPL DCLDELYEMM CQCWITEPKR RPSFVDLKQR LEAIWGRLSI
LSASQDQLYV NLGETCGAAA AVSGLHSAFC SEEDYCAGPS QTCGTSAITS DYRYIVNPGC
LREGNEWSSS AQNGEARGLL HEEEEEEEEE MQEEQVVITL
