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Database: UniProt
Entry: A0A8C8G7B8_ONCTS
LinkDB: A0A8C8G7B8_ONCTS
Original site: A0A8C8G7B8_ONCTS 
ID   A0A8C8G7B8_ONCTS        Unreviewed;       980 AA.
AC   A0A8C8G7B8;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
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};
GN   Name=CSF1R {ECO:0000313|Ensembl:ENSOTSP00005045560.1};
OS   Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=74940 {ECO:0000313|Ensembl:ENSOTSP00005045560.1, ECO:0000313|Proteomes:UP000694402};
RN   [1] {ECO:0000313|Ensembl:ENSOTSP00005045560.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSOTSP00005045560.1}
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; A0A8C8G7B8; -.
DR   Ensembl; ENSOTST00005049542.2; ENSOTSP00005045560.1; ENSOTSG00005019218.2.
DR   GeneTree; ENSGT00940000155506; -.
DR   Proteomes; UP000694402; 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-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:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   GO; GO:0030318; P:melanocyte differentiation; IEA:UniProtKB-ARBA.
DR   GO; GO:0097324; P:melanocyte migration; IEA:UniProtKB-ARBA.
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   CDD; cd05106; PTKc_CSF-1R; 1.
DR   FunFam; 2.60.40.10:FF:002322; macrophage colony-stimulating factor 1 receptor; 1.
DR   FunFam; 1.10.510.10:FF:000177; Mast/stem cell growth factor receptor; 1.
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   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; 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   PRINTS; PR01832; VEGFRECEPTOR.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00219; TyrKc; 1.
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; 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:UP000694402};
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}.
FT   TRANSMEM        524..549
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..117
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          228..312
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          323..412
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          593..923
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        787
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         572
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         599..607
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT   BINDING         600..607
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         672..678
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         791
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         792
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         805
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   DISULFID        63..107
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        153..202
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        249..296
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        435..504
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ   SEQUENCE   980 AA;  110741 MW;  65B4CA857906731C CRC64;
     MTSVIFWSDV YKDARVSDLE FRIGCLLKTH FPKWRRPVIK LNSEVVVGSE VVLNPGTPLV
     LRCEGDGPVN WLTRLSKHKS LISKGNGRVR TFRVDRPSAE HTGTYKCEYT SVNVKVRDLF
     STVHVYVKDS LFWTSSASLR VVRKEGEDHL LPCLLTDPEA TDLGLRMDNC TSVPPGMNYT
     ADPRRGILIR NLHPSYNADY VCSAKLHGVE RTSKTFNLNI IQRLRFPPYV FLEKDEYVHI
     VGEKLSIHCT THNPNFNYNV TWNYTSKKAI DSNRLDIESI LTIPVVDQSD TGNITCIGTN
     EAGVNKSTTS LMVVEEAYIR LSPQLSSKPA HQGLSIDVNE GEDLKLSVLI EAYPQITGQH
     WDTPTASSTQ EQTFTRYNNR YSATLLLKRM IAQEQGQYTF YANSSMANAS ITFQIQMYRK
     PVAVVRWENI TTLTCTSFGY PAPIILWYQC SGIRTTCNEN ATGHQISAPL LAQTVEVQRE
     EYGAVEVQSV LTVEPSSHRM TVECVAFNLV GVGKDTFAMD VSNIMFTSTL LGAAVVLALL
     LLLLMVLLYK YKQKPRYEIR WKIIQASEGN NYTFIDPTQM PYNEKWEFPR DKLKLGKILG
     AGAFGKVVEA TAYGLGEDDN AMRVAVKMLK ELIKREALMS ELKILSHLGQ HKNIVNLLGA
     CTQAGPVLVI TEYCSHGDLL NFLRHKQETF LNFVMNIPAV PEETSDYKNL CEGKQFIRSD
     SGISSVCSDS YLEMRPGPQP VNSSLDSVCE DGGPDSWPLD MEDLLRFSYQ VAQGLDFLAA
     KNCIHRDVAA RNVLLTDLRV AKICDFGLAR DIMNDSNYVV KGNARLPVKW MAPESIFDCL
     YTVQSDVWSY GILLWEIFSL GKSPYPSVLV DTKFYNMIKC GYQMSRPDFA PPEMYTIMKM
     CWNLEPTERP TFSKISQLIE RLLGEEPERP DQLQQDMTVE ELEPCDDNDE PKCCDGSCDQ
     SCEHEEEEQP LVKTNNYQFC
//
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