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Database: UniProt
Entry: A0A8C5DN55_GOUWI
LinkDB: A0A8C5DN55_GOUWI
Original site: A0A8C5DN55_GOUWI 
ID   A0A8C5DN55_GOUWI        Unreviewed;       975 AA.
AC   A0A8C5DN55;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 20.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=LOC114475476 {ECO:0000313|Ensembl:ENSGWIP00000008365.1};
OS   Gouania willdenowi (Blunt-snouted clingfish) (Lepadogaster willdenowi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Blenniimorphae; Blenniiformes; Gobiesocoidei; Gobiesocidae;
OC   Gobiesocinae; Gouania.
OX   NCBI_TaxID=441366 {ECO:0000313|Ensembl:ENSGWIP00000008365.1, ECO:0000313|Proteomes:UP000694680};
RN   [1] {ECO:0000313|Ensembl:ENSGWIP00000008365.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Wellcome Sanger Institute Data Sharing;
RL   Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGWIP00000008365.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSGWIP00000008365.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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}.
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DR   RefSeq; XP_028322118.1; XM_028466317.1.
DR   AlphaFoldDB; A0A8C5DN55; -.
DR   Ensembl; ENSGWIT00000009338.1; ENSGWIP00000008365.1; ENSGWIG00000004945.1.
DR   GeneID; 114475476; -.
DR   OrthoDB; 9936425at2759; -.
DR   Proteomes; UP000694680; Chromosome 14.
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: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   CDD; cd00096; Ig; 1.
DR   FunFam; 1.10.510.10:FF:000554; Predicted protein; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
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; IPR013151; Immunoglobulin_dom.
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   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; PF00047; ig; 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; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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   4: Predicted;
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694680};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..975
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5034990474"
FT   TRANSMEM        510..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          203..293
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          314..391
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          578..887
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        751
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         557
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         585..592
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         612
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         658..664
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         755
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         756
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         769
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   SITE            895
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ   SEQUENCE   975 AA;  108214 MW;  4D1DFC78AD25AE6B CRC64;
     MAPAGEHLHL IHFLFGVLLV GPEDTMSLEV VPSATEVLLD VNSNYTVVCS GWSPVTWEFP
     GDSLSDSVIM ETQGSVSVLQ FVNVTWKNSG RYTCEEKSSK ESKDIDIFIP GQGPEEWFVP
     LGPGVVMKEA EEETIPCVVS DPHLNVSLFE RGEQTAVVGM KFEPGRGFTG RLNDTSYICV
     ATRGQMERQS QVYYVFSVIV SVPKQIDVEL SVSSTVVKKG EVLTVNCTVT NTEMVFFTWD
     FPRKQEVEPV TDFLPNQIRS FVNITSVTME DSGVYLCVVQ ETTEGPTMEK NITVRVLDQG
     FVSVWPSGET NTVCLLHHSV EFTVEVEAHP EPSVVWTKDN LTIPMETIST NTKHLTGTRY
     SSTLSLVRVL MDQRGRYTVT ASNEDMEAEV TFTLEVQVPP KITSLSELST NTILCASEGA
     PPPSVKWYIC PSSLRCSDLS GGWMNLSATT VGITQQDTVT VVEMDVAKVR SVLALQAFSL
     VSAVRCEVNN SAGRGSRDLR MESVSLLSQV SVLAVVLVLF IIALIFLIIL IVLWRKKPGY
     EVHWKLIESA SPDGQSYVYV DPAKLPYSSD WEIPRDQLVL GQVLGSGAFG RVVEGTVSGL
     MESQAFTKVA VKMVKGKGDA VQSLMSELRM LVHVGPHLNL VNVLGASTTG GPVYLITEFC
     CHGDLLKYLQ RNKNSFLLLE THSVSDGDGG YMDMKNIHDV EPHADEMLEQ RELPLPDSDS
     SHLSLHDLLW FSYQVCHAMD FLSVRQCVHT DLAARNVLVC EKKLVKVCDY GLARDLLKHE
     DYDTHGNAVL PLRWMSPESI FQKVYSSHSQ VWSFGVLLWE IFSMGCRPYA ELMGTRDLFN
     FLRKGHRMSR PEHASQNMYE LMMQCWKDTP QSRPSFSSLV DSLASMLSDD YKQRYCQLTQ
     DFHRGQNPAI ARSQVTQSKT EGNSVSMVTV DPLPLESVET GPSHSTQVID VAIETISTAA
     LDAVSVQDKE EESSL
//
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