ID A0A9D3S7Z5_ANGAN Unreviewed; 1101 AA.
AC A0A9D3S7Z5;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=ANANG_G00072650 {ECO:0000313|EMBL:KAG5853377.1};
OS Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC Anguilla.
OX NCBI_TaxID=7936 {ECO:0000313|EMBL:KAG5853377.1, ECO:0000313|Proteomes:UP001044222};
RN [1] {ECO:0000313|EMBL:KAG5853377.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tag_6206 {ECO:0000313|EMBL:KAG5853377.1};
RC TISSUE=Liver {ECO:0000313|EMBL:KAG5853377.1};
RA Henkel C., Jong-Raadsen S.A., Dufour S., Weltzien F.-A., Palstra A.P.,
RA Pelster B., Spaink H.P., Van Den Thillart G.E., Jansen H., Zahm M.,
RA Klopp C., Cedric C., Louis A., Berthelot C., Parey E., Roest Crollius H.,
RA Montfort J., Robinson-Rechavi M., Bucao C., Bouchez O., Gislard M.,
RA Lluch J., Milhes M., Lampietro C., Lopez Roques C., Donnadieu C.,
RA Braasch I., Desvignes T., Postlethwait J., Bobe J., Guiguen Y., Dirks R.;
RT "A chromosome-scale assembly of European eel, Anguilla anguilla.";
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00051243};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
CC protein {ECO:0000256|RuleBase:RU000311}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily.
CC {ECO:0000256|RuleBase:RU000311}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG5853377.1}.
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; JAFIRN010000003; KAG5853377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9D3S7Z5; -.
DR Proteomes; UP001044222; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; IEA:TreeGrafter.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IEA:TreeGrafter.
DR GO; GO:0001667; P:ameboidal-type cell migration; IEA:UniProtKB-ARBA.
DR GO; GO:0001525; P:angiogenesis; IEA:TreeGrafter.
DR GO; GO:0060326; P:cell chemotaxis; IEA:TreeGrafter.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:TreeGrafter.
DR FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 1.10.510.10:FF:000140; Platelet-derived growth factor receptor beta; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR050122; RTK.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR PANTHER; PTHR24416:SF53; PLATELET-DERIVED GROWTH FACTOR RECEPTOR BETA; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000615-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000615-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP001044222};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000311};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 524..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..304
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 592..953
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 66..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1085
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 817
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 571
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 599..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 674..680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 821
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 822
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 835
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 961
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 1101 AA; 123129 MW; 73AEC24DEC82C4DE CRC64;
MLRISSHFGL FYHEEKKHKG GSVSGCHFCS PSALRGRPRP GALARRRRRG PERGRQLLRR
LPGAGRGVLE ARPPGRDGVR VTSGPAHSNL ALENATWAHT GMYTCVDPDA GETRNVSVFV
PDDKVWFLPV EYNIVTRTSH QATVPCVVTN PQIKVSLYEA TGNTSLDGEY HPLKGFTAHL
EDKSYFCRGE LDGQRSNSVE FYVFTILVPE NLEPHVNASK TVMKQGEPLS VHCTIEGVEL
VLFSWEYPRM ESLELEPLTD VLSSTSMRSS LFIPNVTLDN SGWYVCNVKE DMQNQNASDA
ILVTVLERGF VNISYAGRRN ISAQLHESIE IRVQIEAYPK PTMRWTMDRG DLHGDTISIE
TKQMDETRYV STLTLIRVKK EQRGLYAITV SNEDAVKKLT FHLKVKVPPQ IVNLSDHPLA
DRRHSVICVA EGVPPPRIQW FSCDSRQKCS NGTMPWQPLV AEPESVDIQT NVSYDDVLKI
SQARSVVTFQ GLQRVISVRC QATNKRGQRE RDIKLVSHML FSQVAVLAAI LSLVVLAVIF
TIILIALWRK KPRYEIRWKV IESVSSDGHE YIYVDPIHLP YDSAWEVPRD SLILGRTLGS
GAFGRVVEAT AYGLGHSQST TKVAVKMLKS TARRSETQAL MSELKIMSHL GPHLNIVNLL
GACTKQGPIY LVTEYCRYGD LVDYLHRNKH TFLQHYADKS RRDAIMCSNG VADGQSKGYV
SFAGGCDGNY MDMSKEDSAQ YMAMKELSDI KYADIQPSVY ETPYHQDLYG GQGEERSETA
LVISDSPLLS YSDLVGFSYQ VAKGMDFLAS KNCVHRDLAA RNVLICEGKL VKICDFGLAR
DIMHDSNYIS KGNTFLPLKW MAPESIFHNL YTTLSDVWSF GVLLWEIFTL GGTPYPDLPM
NELFYSALKR GYRMAKPAHA SDEIYDVMRK CWEEKFEKRP EFSYLVHAVG NMLTDSYKKK
YTQVNDGFLK SDHPAVVRTK PRLSVPLASP QNGSPVGIRW EGDGEEALAS YNEYIIPIPD
PKPEEGWDEA PTLTDGSSSD RSRDPDEESD SVSLEAPAAV PEEEKTQLIQ KEERGGGGGG
SGASGMPGNS GRRRQLPLET P
//
