ID A0A8C6MD33_NOTFU Unreviewed; 971 AA.
AC A0A8C6MD33;
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=CSF1R {ECO:0000313|Ensembl:ENSNFUP00015033276.1};
GN Synonyms=csf1ra {ECO:0000313|Ensembl:ENSNFUP00015033276.1};
OS Nothobranchius furzeri (Turquoise killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Nothobranchiidae;
OC Nothobranchius.
OX NCBI_TaxID=105023 {ECO:0000313|Ensembl:ENSNFUP00015033276.1, ECO:0000313|Proteomes:UP000694548};
RN [1] {ECO:0000313|Ensembl:ENSNFUP00015033276.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GRZ {ECO:0000313|Ensembl:ENSNFUP00015033276.1};
RA Senf B., Petzold A., Downie B.R., Koch P., Platzer M.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNFUP00015033276.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSNFUP00015033276.1}
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; A0A8C6MD33; -.
DR Ensembl; ENSNFUT00015034773.1; ENSNFUP00015033276.1; ENSNFUG00015013427.1.
DR GeneTree; ENSGT00940000155506; -.
DR Proteomes; UP000694548; Chromosome sgr01.
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:0048513; P:animal organ development; 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:0050793; P:regulation of developmental process; IEA:UniProtKB-ARBA.
DR GO; GO:0002682; P:regulation of immune system process; IEA:UniProtKB-ARBA.
DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:TreeGrafter.
DR FunFam; 2.60.40.10:FF:001029; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:002322; macrophage colony-stimulating factor 1 receptor; 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; 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; 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; PF07679; I-set; 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; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 1.
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:UP000694548};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 522..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..303
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 590..912
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 776
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 569
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 596..604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT BINDING 597..604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 624
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 780
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 781
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 794
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT DISULFID 48..92
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 139..188
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 235..291
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 432..501
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ SEQUENCE 971 AA; 110137 MW; 63C95ADCF53ABB3F CRC64;
VQKYLSVLLT DMFLFSVEWR RPVITFKSRE VGGSEVVVRV GSPLDLSCEG DGPVNWHPRL
PKHKRFVSKS SGNICTLKVP RPTAEFTGTY TCVYAAESKD SNLTSSVHVF VKDPQRVFWT
SSTSLRVVKK EGEAYMLPCL LTDPSATNLS LRMDNGTSVP AGMNFTINRH RGVFIHSLNP
SFNADYVCTA RVNGVERTSK AFSINVIQKL RSPPYVYLET EEYVRIVGEK LKVVCKTHNP
NFNYNVTWKY STKSKPTIEE MVRSSGENRL DIQSILTIPA VDLADTGNIS CVGTNEAGEN
STTTYLLVVD KPYIRLSPQL SPRLAQQGSL IEVNVGEDLE LNVLIEAYPQ IVEHRWFTPT
SPNTSTQEHK FIRYNNRYRA SLQLKRMNIQ EQGQYTFYAR SNLVNASIKF QVQMYQRPVA
VVRWENVTTL TCTSFGYPAP RIIWYQCLGI RPTCNESTSG LQLAVPLQAL TVEVQREENG
AVEVESVLRV GPSTQRMTVE CVAFNLVGIS RDTFSMEVSD ELLTTTLSGV AAIMAILLVL
LVFLLYKYKQ KPRYEIRWKI IEMSSGNNYT FIDPTQLPYN EKWEFPRDKL KLGKILGAGA
FGKVVEATAY GLGKEDNAVR VAVKMLKASA HSDEREALMS ELKILSHLGH HKNIVNLLGA
CTYGGPVLVI TEYCSLGDLL NFLRQKAETF VNSVMNLPDV RKNSDYKNIC SQRQFIRSDS
GISSAASSTY LEMRPSQCDY EETGDWLLDI EDLLRFSLQV AQGLDFLAAR NCIHRDVAAR
NVLLTSQREA KICDFGLARD IMNDSNYVVK GNARLPVKWM APESIFDCIY TVQSDVWSYG
ILLWEIFSLG QSPYPSMAVD TRFYKMIKHG YQMSQPGFAS LEMYTIMRMC WNLEPTKRPT
FQKISQMIEK LLGDQLEEEQ VDYCIQLKQT SLYQNVQQEL TEEDVHDQSK CCDQAEEQQL
LMKTNNKYQF C
//
