ID A0A667ZS06_9TELE Unreviewed; 940 AA.
AC A0A667ZS06;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=csf1ra {ECO:0000313|Ensembl:ENSMMDP00005045705.1};
OS Myripristis murdjan (pinecone soldierfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Holocentriformes; Holocentridae; Myripristis.
OX NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005045705.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005045705.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMMDP00005045705.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSMMDP00005045705.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC for CSF1 and plays an essential role in the regulation of survival,
CC proliferation and differentiation of hematopoietic precursor cells,
CC especially mononuclear phagocytes, such as macrophages and monocytes.
CC Plays an important role in innate immunity and in inflammatory
CC processes. Plays an important role in the regulation of osteoclast
CC proliferation and differentiation, the regulation of bone resorption,
CC and is required for normal bone development. Promotes reorganization of
CC the actin cytoskeleton, regulates formation of membrane ruffles, cell
CC adhesion and cell migration. Activates several signaling pathways in
CC response to ligand binding. {ECO:0000256|ARBA:ARBA00058066}.
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 -!- SUBUNIT: Monomer. Homodimer. Interacts with CSF1.
CC {ECO:0000256|ARBA:ARBA00062014}.
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; A0A667ZS06; -.
DR Ensembl; ENSMMDT00005046603.1; ENSMMDP00005045705.1; ENSMMDG00005020516.1.
DR GeneTree; ENSGT00940000155506; -.
DR Proteomes; UP000472263; Chromosome 10.
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: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:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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:0022603; P:regulation of anatomical structure morphogenesis; IEA:UniProtKB-ARBA.
DR GO; GO:1905521; P:regulation of macrophage migration; IEA:UniProtKB-ARBA.
DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:TreeGrafter.
DR FunFam; 2.60.40.10:FF:002103; Colony-stimulating factor 1 receptor, a; 1.
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; 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; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
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 Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW ECO:0000256|RuleBase:RU000311};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
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 Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP000472263};
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 Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 204..297
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 308..399
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 553..884
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 748
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 559..567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT BINDING 560..567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 635..641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 752
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 753
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 766
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 895
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT DISULFID 37..81
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 129..178
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 225..281
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 422..491
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ SEQUENCE 940 AA; 106319 MW; 46A3389326DFECBE CRC64;
CYVCLTQWRR PVIKFNSKVV EGPEVVVTAG TRLRLTCEGN GPVNWQTRLA KHRRYVLKGT
GNIRTLNVER PAAEFTGTYK CSYTSGPQRV RDLVSSVHVY VKDPDRLFWT SSTSLRVVKK
EGEDYLLPCL LTDPAATNLG LRMDNGTSLP PGMNFTAYPH KGILIHSLHP SFNADYVCTA
KINGVEKSSR AFSINVIQKL RFPPYVFLEK DEYVRIVGEE LKIRCNTHNP NFNYNVTWRY
TTKMKSTVEE KVRSSGENRL DIESILTISA VDLADTGNIS CIGTNEAGVN SSTTYLLVVD
KPYIRLSPQL SPKLAHQGLS VEVNEGEDLE LSVLVEAYPH IIEQGWDTPT SPNTSTQEKK
FIKYNNRYHA SLLLKRMNPQ EQGQYTFHAK SHMANASITF QVQMYQRPVA VVRWENVTTL
TCTSFGYPAP RIIWYQCFGI RPTCSENTTG MQMPVPLQAP TVEVQREEYG AVEVESVLTV
GPSNRRMTVE CVAFNLVGVS SDTFAMDVTV TVAKPRYEIR WKIIEARDGN NYTFVDPTQL
PYNEKWEFPR DKLKLGKILG AGAFGKVVEA TAFGLGKEDN TLRVAVKMLK ASAHSDEREA
LMSELKILSH LGHHKNIVNL LGACTYGGPV LVITEYCSHG DLLNFLRQRA EPFLNFIMSV
PEITEEPGDY KNICNQKQFI RSDSGISSVS SGSYLEMRPS QQPIKSSLDS VCEEGGDWPL
DIDDLLRFSH QVSQGLDFLA AKNCIHRDVA ARNVLLTDHR VAKICDFGLA RDIMNDSNYV
VKGNARLPVK WMAPESIFDC VYTVQSDVWS YGILLWEIFS LGKSPYPSMA VDSRFYKMVK
CGYQMSRPDF APPEMYLIMK ACWNLEPTER PTFSKISQMI ERLLGDHHNQ EQLMYQNVQQ
QVTESEACDE PKCSEGPCDR SCDYEEEEQP LMKTNHYQFC
//
