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Database: UniProt
Entry: A0A673LYE1_9TELE
LinkDB: A0A673LYE1_9TELE
Original site: A0A673LYE1_9TELE 
ID   A0A673LYE1_9TELE        Unreviewed;       852 AA.
AC   A0A673LYE1;
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};
OS   Sinocyclocheilus rhinocerous.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Sinocyclocheilus.
OX   NCBI_TaxID=307959 {ECO:0000313|Ensembl:ENSSRHP00000080988.1, ECO:0000313|Proteomes:UP000472270};
RN   [1] {ECO:0000313|Ensembl:ENSSRHP00000080988.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSSRHP00000080988.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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; A0A673LYE1; -.
DR   Ensembl; ENSSRHT00000083180.1; ENSSRHP00000080988.1; ENSSRHG00000040087.1.
DR   Proteomes; UP000472270; Unassembled WGS sequence.
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-KW.
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: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:000619; macrophage colony-stimulating factor 1 receptor isoform X2; 1.
DR   FunFam; 1.10.510.10:FF:000140; Platelet-derived growth factor receptor beta; 1.
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; 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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR050122; RTK.
DR   InterPro; IPR001245; Ser-Thr/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; 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; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 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|PIRSR:PIRSR000615-
KW   2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR500947-52};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
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   Reference proteome {ECO:0000313|Proteomes:UP000472270};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          209..292
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          510..820
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        684
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         544
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         592..598
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         688
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         689
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         702
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   DISULFID        61..100
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        142..191
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        231..280
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        398..461
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ   SEQUENCE   852 AA;  96389 MW;  E5B2E4CD9008BECD CRC64;
     MFCVTLSYIT SHLKVLLSGM IYVMVHLTSS EFPAPVIKLN SSPLSRSEVV RSAYKPFILS
     CEGQADIIWK TRLRKHQKHV SQNTVSVQKP TTEYTGTYRC SYKNQKDLYS EIHIYVRDSV
     KAFTTPQSPI IIQKEGSNLL DCLVTNPESI EFSLQMANGS AVPSEMNYTA DPKRDILIRN
     LQPSYNGDYV CTVKMNGVQK KSDIFQLTPP AVSLPANQYV RIVGEMLHIP CHTKNQDHSY
     NITWSSSEKV NTVSGCEQVC IISLLSIHQV NISNAGNLTC TGQNEAGKNS VTAVLKVVDK
     PYIKLKLILS SEYKVNGTDI EVMQGDTVEL AVQIEAYPEV KRTSWKTPKS NHTHEETFNR
     INNRLVHLFL VNASLIFTVH VYQKPNTLIK WENGSATCVA TGYPIPRIQW FQCEDARAMC
     SYNQTSAVEL MATQSTLEYE PVLVKSVLPV TNANTTLTFE CVATNIAGED HDIFTFKSSC
     KENANVPAAE HVFVHLKWSG HLIHFQCYEI QWKIIEEREV FGKVVQATAY GLVKDESVTR
     VAVKMLKPSA RFGEKEALMS ELKILNYIGP HENIVNLLGA CTQGGPMLMI TEYCCHGDLL
     NFLRQRAETF VNNVFGVQSF PEDSNLYKNV AVQKNNWTGY VNVKSCNEGG KDAWSLDNID
     LLKFSYQVAK GMDFLASKNF IFLDLAARNI LVADCRVVKI CDFGLARDIM NDLNYVVKGN
     ARLPVKWMSP ESIFECLYTV QSDVWSYGVL LWEIFSLGVS PYPNVVIDAQ FYKMIKDGYH
     MPQPDFAPQE MYTIMKMCWS LEPTLRPTFA NIRELIAKLL PKQSSQTNPS QRDRPSSEKN
     NLFKVNNYFY YC
//
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