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Database: UniProt
Entry: A0A8C5BX81_GADMO
LinkDB: A0A8C5BX81_GADMO
Original site: A0A8C5BX81_GADMO 
ID   A0A8C5BX81_GADMO        Unreviewed;       983 AA.
AC   A0A8C5BX81;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   08-OCT-2025, sequence version 3.
DT   28-JAN-2026, entry version 21.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8049 {ECO:0000313|Ensembl:ENSGMOP00000052322.1, ECO:0000313|Proteomes:UP000694546};
RN   [1] {ECO:0000313|Ensembl:ENSGMOP00000052322.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSGMOP00000052322.1}
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}.
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}.
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DR   AlphaFoldDB; A0A8C5BX81; -.
DR   Ensembl; ENSGMOT00000037302.1; ENSGMOP00000052322.1; ENSGMOG00000010289.2.
DR   GeneTree; ENSGT00940000156021; -.
DR   Proteomes; UP000694546; Chromosome 12.
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; 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:SF52; PLATELET-DERIVED GROWTH FACTOR RECEPTOR ALPHA; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07679; I-set; 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; 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|PROSITE-
KW   ProRule:PRU10141}; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694546};
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}.
FT   TRANSMEM        414..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          206..304
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          482..845
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          909..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..951
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         516
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   983 AA;  110400 MW;  1E325602162224F1 CRC64;
     MAQLNFMSPL NEKYMILDMI IPLHTSFSLT CRGHSPLYWS MPFDLPEQTQ ADSSGLFVSA
     VTVEAAIVHH TGRYSCHYVN GQEDDEPASI YIYVPDPEVP FLPLSLLSFG NHMVSEPKDM
     AIQCMVSNPE ANVTLFDVYT QQPVASTYDS QRGAMGVFPA GTYACRALIN GQEHISQEYI
     VHGFPPGTGV CVSHGPNLLE DHWKYPGKLV RQRTFGSVES AELDEVKEFR AVVDSFPSVR
     VTWLKDGQPL DYVVAEISTN LRQLRETRYE SVLTLIRAKE EDSGNYTIRV ENGNQSHSHS
     FTLQVKVIVE LMDIHHGSAT GQSVVCIAGG RPTPEVEWFV CKNIKHCANE SSQWEPLQTN
     STTVSVESHL DQDNNLESQV MFGHLEGNLA VRCLARNHLA TVSREVKLVA TSELSVAAAV
     LVLLVIVIIS LIVLVIIWKQ KPRYEIRWRV IESVSPDGHE YIYVDPMQLP YDSRWEFPRD
     RLVLGRILGS GAFGKVVEGT AYGLSRSQPV MKVAVKMLKP TARSSEKQAL MSELKIMTHL
     GPHINIVNLL GACTKSGPIY IITEYCLYGD LVNYLHKNRE NFISLQPEKS RKNLDIFGIN
     PVDESSRSYV ILSFEGKGGD YMDMKQADNT QYVPMLEMNS SKYSDIMRSN YDHPPSQKEF
     DGEMDNLLSE DGKDGLSTTD LLSFTYQVAK GMEFLASKNC VHRDLAARNV LLSQGKIVKI
     CDFGLARDIM HDNNYVSKGS TFLPVKWMAP ESIFDNLYTT LSDVWSYGIL LWEIFSLGYG
     NICGTPYPGM VVDSSFYNKI KSGYRMAKPE HAPSDMYEVM MRCWNSEPEK RPSFMELTEA
     VASLLPSSYK RCYDRVNQDF LKSDHPAVTR VCVDTDLPVD DNAYIGIAYK NHGKLKERES
     GFDEQRLSSD SGYIIPLPDL EPLSDDEYGK RNRHSSQTSD ESAIETGSSI STLAKREGET
     LEDITMLDDM CLDSSDLVED SFL
//
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