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Database: UniProt
Entry: A0A671TP75_SPAAU
LinkDB: A0A671TP75_SPAAU
Original site: A0A671TP75_SPAAU 
ID   A0A671TP75_SPAAU        Unreviewed;       997 AA.
AC   A0A671TP75;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   28-JAN-2026, entry version 27.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=LOC115594263 {ECO:0000313|Ensembl:ENSSAUP00010003065.1};
OS   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Sparus.
OX   NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010003065.1, ECO:0000313|Proteomes:UP000472265};
RN   [1] {ECO:0000313|Ensembl:ENSSAUP00010003065.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Wellcome Sanger Institute Data Sharing;
RL   Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSAUP00010003065.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSSAUP00010003065.1}
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   AlphaFoldDB; A0A671TP75; -.
DR   Ensembl; ENSSAUT00010003287.1; ENSSAUP00010003065.1; ENSSAUG00010001559.1.
DR   GeneTree; ENSGT00940000157138; -.
DR   Proteomes; UP000472265; Chromosome 13.
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:000140; Platelet-derived growth factor receptor beta; 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   InterPro; IPR020635; Tyr_kinase_cat_dom.
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   SMART; SM00219; TyrKc; 1.
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:ARBA00023137};
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:UP000472265};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
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};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..997
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025513542"
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          399..502
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          578..869
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          960..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        733
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         623..629
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         737
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         738
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         751
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   SITE            877
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ   SEQUENCE   997 AA;  110690 MW;  21D90CDB4923611D CRC64;
     MASIRGRTGS LNVLHFLLGA LLVCPEGAVC LELMPSSSEV LKSNANFTVV CSGWSQVTWR
     LPTDTLVDGV VVENQGSSSV LQLSNATWKN SGRYTCEEPS SHQSRDIDIF IPGQGPEEWF
     VPLGPGVVMK EAEEDTIPCV VSDPQLNVSL YERPGRKLIT GTKYEPGRGF TGRLNDTSYV
     CLAARGGEER ESQVYYVFSI IVPKVMEVEL TVSSSVLKQG EALTVNCTVK DTEMVFFSWD
     FPRKQEIEPL TDFLPNRIRS FLNISEATVE DSGVYVCMVK ETMQEQTVTK NITLRVLDQG
     YVYLWSSGET NVSSLLHHTV EFSVEVDAHP APTVLWTKDN QTIATDTTSI TTRHLTGSRY
     LSTLTLVRVQ MDQTGSYTAT ASNDDDVEEV IFKLEVKAPP RITSLSEVGS KAVQCVSEGA
     PPPSITWYTC QSSHRCNNLT GGWRSLSASE GRALLGNITE VEERGVTKVR SVLTLQSLSS
     LSAVRCEAKN SAGRRARDLR IVSSSLLSQV AVLAAVLVLV ILAVIFLIIL ILLWRKKPRY
     EVRWKVIESV SPDGQQYTYL DPAHLPYNST WEVPRDNIVI GQVLGSGAFG RVVEATVSGL
     LHSHSSTKVA IKMVKRPVHL ITEFCRHGDL VNYLQRNKHT FLQRDTHTKS DSDGGYMDMN
     KEESAQYVAM KELSYADIEP AVYETPYTAP DQQEESLLLS DSPLLSLHDL LSFSFQVSKA
     MDFLSTRNCV HRDLAARNVL VCEGKLVKVG DFGLARDLMK DQDYIARGNS FLPVKWMSPE
     SIFQNIYSCQ SDVWSYGVLL WEIFSLGGSP YPDLPMTQEF YSALKRGYRM SRPDHAPHNI
     FDLMKQCWEE KPQSRPSFSS LVVSVGNMLT DDYQKRYLQL TENFLKGENP AVVRSRMSSS
     RAAEDQTNIL ADMNGGPTPQ ENVYLLEVEP VEDGPSHGTY IIPITDITIE TSNGAALDAV
     SPQLSESQDI AGAQEVKTSE EKQEIEAPPA PEEESCL
//
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