ID A0A673LYD6_9TELE Unreviewed; 893 AA.
AC A0A673LYD6;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 26.
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:ENSSRHP00000080983.1, ECO:0000313|Proteomes:UP000472270};
RN [1] {ECO:0000313|Ensembl:ENSSRHP00000080983.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSRHP00000080983.1}
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; A0A673LYD6; -.
DR Ensembl; ENSSRHT00000083175.1; ENSSRHP00000080983.1; 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; 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; 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; 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; PF07679; I-set; 2.
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; 4.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 2.
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|ARBA:ARBA00023157,
KW 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 216..304
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 313..408
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 544..853
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 717
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 578
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 626..632
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 722
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 735
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 238..292
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 432..495
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ SEQUENCE 893 AA; 101297 MW; 7AEE1FF6B25F22C6 CRC64;
MFCVTLSYIT SHLKVLLSGM IYVMVHLTSS EFPAPVIKLN SSPLSRSEVV RSAYKPFILS
CEGQADIIWK TRLRKHQKHV SQNTVSVQKP TTEYTGTYRC SYKNQKDLYS EIHIYVRDSV
KAFTTPQSPI IIQKEGSNLL DCLVTNPESI EFSLQMANGS AVPSEMNYTA DPKRDILIRN
LQPSYNGDYV CTVKMNGVQK KSDIFQLTVI RKTQQPPAVS LPANQYVRIV GEMLHIPCHT
KNQDHSYNIT WSSSEKVLNY ETKKDKGCEQ VCIISLLSIH QVNISNAGNL TCTGQNEAGK
NSVTAVLKVV DKPYIKLKLI LSSEYKVNGT DIEVMQGDTV ELAVQIEAYP EVKRTSWKTP
KSNHTHEETF NRINNSDNYT STIMLEKVGE QDYGNYIFTA RSASVNASLI FTVHVYQKPN
TLIKWENGSA TCVATGYPIP RIQWFQCEDA RAMCSYNQTS AVELMATQST LEYEPVLVKS
VLPVTNANTT LTFECVATNI AGEDHDIFTF KSSSQKGMFF SCTHKGRSKS LFNTISFFKA
HKYEIQWKII EREVFGKVVQ ATAYGLVKDE SVTRVAVKML KPSARFGEKE ALMSELKILN
YIGPHENIVN LLGACTQGGP MLMITEYCCH GDLLNFLRQR AETFVNNVFG VQSFPEDSNL
YKNVAVQKNN WTGYVNVRST INTDDAWSLD NIDLLKFSYQ VAKGMDFLAS KNFIFLDLAA
RNILVADCRV VKICDFGLAR DIMNDLNYVV KGNARLPVKW MSPESIFECL YTVQSDVWSY
GVLLWEIFSL GVSPYPNVVI DAQFYKMIKD GYHMPQPDFA PQEMYTIMKM CWSLEPTLRP
TFANIRELIA KLLPKQSSQV RHTDNHLRCC NSKDRPSSEK NNLFKVNNYF YYC
//
