ID A0A8C1PAC5_CYPCA Unreviewed; 1062 AA.
AC A0A8C1PAC5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=LOC109046274 {ECO:0000313|Ensembl:ENSCCRP00010102313.1};
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962 {ECO:0000313|Ensembl:ENSCCRP00010102313.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010102313.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00010102313.1}
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; A0A8C1PAC5; -.
DR Ensembl; ENSCCRT00010113657.1; ENSCCRP00010102313.1; ENSCCRG00010044796.1.
DR Proteomes; UP000694427; 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: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 CDD; cd00096; Ig; 1.
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; 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; 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 PRINTS; PR00109; TYRKINASE.
DR PRINTS; PR01832; VEGFRECEPTOR.
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; 4.
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:UP000694427};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1062
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034433354"
FT TRANSMEM 507..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..105
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 202..290
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 314..384
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 393..499
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 575..937
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 963..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 801
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 554
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 582..589
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 609
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 657..663
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 805
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 806
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 819
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 945
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 1062 AA; 119646 MW; 4063C6BB5F7D913D CRC64;
MKSFSRSQLT AMTTGLLLLC LGSSGLELNP SVTQVVLSIN SSFSITCSGR SYVSWRFKRE
ENVPEFHTEK RSPSSSVLSL EQVTWRHTGV YVCSENSTNE TREVAVFVPD PEVWFLENDH
FMVTKMGVEG TIPCLVTDPL INVALYEKDS EIKVEGTYNP STGYTAALED RIYKCKGKLN
KVEKESKEFY VFSIFALEAL DPYINASKTV LKQGETLNIN CTVHGVELVF FVWDIPNKDA
EDIEPFTDIP SSRSMRSYLS ITDVSLARSG QYVCNVYEGV QNQKASASIN ITVLEKGFVA
LSSHLDRNVS AQLGENVELT VEIQAYPKPT VHWTKDGTAI RGHNTRQENE TRFVSTLTLV
RIRLEQMGLY TVSVQNEDDF KDLTFDLEVK VPPQITELSD HQLPGKKHAV TCVAEGVPSP
SIQWFSCDSM PKCSNKSVAW SPLVEDPEKV TIQTNFTYNI TRKIHQVHSQ VTLLRPQLLT
IRCEARNERG ARARDIRLVN STLFSQVAVL AAVLALVVIA IISIIILIAV WRKKPRYEIR
WKVIESVSLD GHEYIYVDPI HLPYDLAWEM PRDSLVLGRT LGSGAFGRVV EATAYGFGRS
QSATKVAVKM LKSTARRSET QALMSELKIM SHLGPHLNIV NLLGACTKHG PLYLVTEYCR
YGDLVDYLHR NKHSFLQHYA DKNHIANGNQ ICNDSDVSTR KEYVSFGSEC DGGYMDMTKD
EQTEYVPMQE LSDSIKYADI QPSPYESPYQ QDIYQEQGHR VDQSLVISDS PVLSYTDLVG
FSYQVAKGME FLASKNCVHR DLAARNVLIC EGKLAKICDF GLARDIMHDN NYISKGSTFL
PLKWMAPESI FHNLYTTLSD VWSYGILLWE IFTLGGTPYP DLPMNELFYS ALKRGYRMAK
PSYACDDIYE VMRKCWDEKF EKRPEFSFLV HTLGDMLSDG YKKRYSQVSD SFLKSDHPAV
ARVKPRVPSP FPGTLDLSPN PTPRPQVNRD IADAPHNEYI IPIPDPKPGE ETQDGPVLTE
IPSSLLSSDE ETVSMETPST EPEHEELLPD HSGSPEVEES FL
//
