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Database: UniProt
Entry: A0A8C1BHJ6_CYPCA
LinkDB: A0A8C1BHJ6_CYPCA
Original site: A0A8C1BHJ6_CYPCA 
ID   A0A8C1BHJ6_CYPCA        Unreviewed;       875 AA.
AC   A0A8C1BHJ6;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2023, sequence version 2.
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};
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:ENSCCRP00000031557.2, ECO:0000313|Proteomes:UP001108240};
RN   [1] {ECO:0000313|Ensembl:ENSCCRP00000031557.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSCCRP00000031557.2}
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; A0A8C1BHJ6; -.
DR   Ensembl; ENSCCRT00000034223.2; ENSCCRP00000031557.2; ENSCCRG00000016989.2.
DR   GeneTree; ENSGT00940000155626; -.
DR   Proteomes; UP001108240; Unplaced.
DR   GO; GO:1990682; C:CSF1-CSF1R complex; IEA:TreeGrafter.
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:0019955; F:cytokine binding; IEA:InterPro.
DR   GO; GO:0019838; F:growth factor binding; IEA:TreeGrafter.
DR   GO; GO:0005011; F:macrophage colony-stimulating factor receptor activity; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001667; P:ameboidal-type cell migration; IEA:UniProtKB-ARBA.
DR   GO; GO:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   GO; GO:0030316; P:osteoclast differentiation; IEA:TreeGrafter.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:TreeGrafter.
DR   GO; GO:0043408; P:regulation of MAPK cascade; IEA:TreeGrafter.
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; IPR030658; CSF-1_receptor.
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; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR   PANTHER; PTHR24416:SF47; MACROPHAGE COLONY-STIMULATING FACTOR 1 RECEPTOR; 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   PIRSF; PIRSF500947; CSF-1_receptor; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 2.
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.
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   ECO:0000256|PIRSR:PIRSR500947-52};
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:UP001108240};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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   TRANSMEM        470..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          99..182
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          190..266
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          533..847
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        711
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         512
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         539..547
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT   BINDING         540..547
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         567
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         615..621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         715
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         716
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         729
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   DISULFID        34..73
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        116..165
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        212..254
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        384..451
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ   SEQUENCE   875 AA;  98574 MW;  38AD1D5450DDBD04 CRC64;
     MAKELPAPVI KLNFSPLSQS EVVWSADKPF ILSCDGQADI IWKTRIRKYQ KHVSQKTLNV
     KKPTTEYTGT YRCSYKNQTD LYSEIHIYVK DSVKAFTTPQ NTIIIQKEGS NYLLDCLVTN
     PASTEYSLQM VNGSAVPSEM NYTADPKRGI LVRNLQPSYS GDYVCTVKIN GVQKKSDVFQ
     ITVIEKTQQP PAVSLPANRY VRIVGETLQI PCHTKNQDHS YNITWSSSGK VNIGNYLLLT
     IHQVKMSDAG NLTCTGQNQA GKNSVTAVLK VVDKPYIHLK PVLSSEYKVN GTDIEVMQGD
     KVELAVQTEA YPEVKWTRWK TPKSNHTHEE AFNRINNRKV GAMDNGHYIY TARSASVNAS
     IIFTVHVYQK PNTLITWENG VASCVASGYP VPRIQWFQCE DARDMCSSNQ TAAVELMATQ
     STLGDVREYE PVRVKSVLPV TNMTTTLTFE CVATNIAGED RDTFTYKISF WITVVLIAAL
     VLAILGMLIL FYKHRKYEIH WKIIEANEGN NYTFIDPTQL PYDKKLEFPR NKLKLGQVLG
     AGAFGKVVQA TAYGLVKDES FTRVAVKMLK PSAHFEEKEA LMSELKILNY IGPHENIVNL
     LGACTQGGPM LLITEYCCQG DLLNFLRQRA ETFVNNVLGV QSFPENSNLY KNVAVQKEII
     SLFQIWSVST ESCNEGGKDA WSLDNMDLLK FSYQVAKGME FLASKNCIHR DLAARNVLVA
     DCRVVKICDF GLARDIMNDL NYVVKGNARL PVKWMSPESI FECLYTVQSD VWSYGVLLWE
     IFSLGMSPYP NVVIDAQFYK MIKDGYHMPQ PDFAPHEMYT IMKMCWSLEP TLRPTFANIT
     ELIAKLLPNQ PSEVRHTVRA IPSVVKATSL DSLHN
//
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