ID A0A9J8BTX8_CYPCA Unreviewed; 1247 AA.
AC A0A9J8BTX8;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS Cyprinus carpio carpio.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000156615.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000156615.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000156615.1}
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; A0A9J8BTX8; -.
DR Ensembl; ENSCCRT00000123477.1; ENSCCRP00000156615.1; ENSCCRG00000038896.2.
DR GeneTree; ENSGT00940000155626; -.
DR Proteomes; UP001108240; Unplaced.
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:0019838; F:growth factor binding; IEA:TreeGrafter.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0001667; P:ameboidal-type cell migration; IEA:UniProtKB-ARBA.
DR GO; GO:0030183; P:B cell differentiation; IEA:TreeGrafter.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:TreeGrafter.
DR GO; GO:0038109; P:Kit signaling pathway; IEA:TreeGrafter.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:TreeGrafter.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IEA:TreeGrafter.
DR FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; IPR001824; Tyr_kinase_rcpt_3_CS.
DR PANTHER; PTHR24416:SF46; MAST_STEM CELL GROWTH FACTOR RECEPTOR KIT; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 4: Predicted;
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP001108240};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1247
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039944815"
FT TRANSMEM 516..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 758..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 786..813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 819..840
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 847..868
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 880..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 914..935
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 941..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 979..1006
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1018..1037
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1049..1075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1102..1123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..100
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 209..305
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 411..508
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 584..883
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1247 AA; 139855 MW; 10D699F7985680A4 CRC64;
MEYHCVLFTV LLQLIVQPAR SRPTITPEGP HLTVPLNSDF SLHCRSDNSV RWLREDRPTR
TLNVQRQGQV TVLKVSKAGP QHMGKYSCRE EASGEKSSIY VYVKAFLSAD PENPFRRNIV
FDFVAGEGEM TTLPCLATDP RITDLHLQKC DGQPLPNSLR YSASIETGIT LEDVRKDFEG
CYVCVGTLEG NTVKSGQYQL NVRLVPDAPP VITLGRPQRV LLIQGEELSL SCSTSNVNSD
ITIRWKAPQG VQPSVQQFSR ILTEPISHLR NATLNLGSVT KQDAGSYNCE ARNERGTSAK
TVWVEIYDKG FINLTSVNNS TKRMRAGESL SLRVVMDAYP KPHTFSWSYS GVKLTNTTDH
VITTRSHGNS YTSELKLVRL KVLESGVYTF SCSNRDATVH QMFEVHVTSK PQIVSYEGPI
GGQVRCVAEG YPTPQIKWYY CDQPYSRCSN LLNATQEEED VVTVTMTNPP FGKGTVESRL
NITKNSYSTL ECVASANGEI VYTLFSISEN TVPHELFTPL LIGFVAAAVI LVLILIVLSY
KYIQKPKYQI QWKVIEGIHG NSYVYIDPTQ LPYDHQWEFP RDKLRFGKTL GSGAFGKVVE
ATAYGMSKAD TVMTVAVKML KPSAHATEKE ALMSELKVLS YLGNHINIVN LLGACTIGGP
TLVITEYCCF GDLLNFLRRR RESFYFTTLG EDSYYRNVML QPEPNESRNG YMTMKPSVMG
LLSSENRRSL KKGWINVSSV LIISFPVILS LLVTQSLFVS SCLVPAFLIS SLLTLSYLFS
CLHFSYLLLM SLLSHLISFV LFCLSCVSCL ISSHLTLSHL FSCFPFIFLS CVFSFFHLVL
SLFVSYCLVL LFFYVVFFSC LLVSSYLFSY PGSSLLISTH LFLLCAFSSS LFCPCLSCSH
LFSPCLFSYH IVSFLIFSSF LFCLIFYLIL FFLFLSHHFS FHLFSCLLFF IFSSLLMPSL
YLLIFVFSVS CLISFSSHIV FSFIPFSLLV CCLILKSPCL FSSVLLSRIF SSHFISSLLV
LSSLVVLSLL FSCLLSLSHL LSCLLFPYLL IYPFCLTSSL LAYLVFTVLI PSLLFSHPVS
SVSFFSCPSC LLSSCLIYSP SLFFLCLCLS VGFLSYCVFI IIFNKFVIPL GDSYSDSDAV
SEILQEDGMT MDTEDLLSFS YQVAKGMDFL ASKNVSVFLI YLNSVSLTDT EFYIPSGCSN
PILQIFSLFL YNATGSHSIT SVQSRIRLHK VTHERIHIVK HMHTLIH
//
