ID D4ACA7_RAT Unreviewed; 1022 AA.
AC D4ACA7;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 2.
DT 28-JAN-2026, entry version 122.
DE RecName: Full=Macrophage colony-stimulating factor 1 receptor {ECO:0000256|ARBA:ARBA00073697};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE AltName: Full=CSF-1 receptor {ECO:0000256|ARBA:ARBA00077528};
DE AltName: Full=Proto-oncogene c-Fms {ECO:0000256|ARBA:ARBA00077514};
GN Name=Csf1r {ECO:0000313|Ensembl:ENSRNOP00000040411.4,
GN ECO:0000313|RGD:2425};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000040411.4, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000040411.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000040411.4};
RA Doris P.A., Kalbfleisch T., Li K., Howe K., Wood J.;
RT "GRCr8: a new rat reference genome assembly contstructed from accurate long
RT reads and long range scaffolding.";
RL Submitted (JAN-2024) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000040411.4}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000040411.4};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSRNOP00000040411.4}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000040411.4};
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 -!- SUBUNIT: Monomer. Homodimer. Interacts with CSF1 and IL34. Interaction
CC with dimeric CSF1 or IL34 leads to receptor homodimerization. Interacts
CC with INPPL1/SHIP2 and THOC5. Interacts (tyrosine phosphorylated) with
CC PLCG2 (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1
CC (via SH2 domain). Interacts (tyrosine phosphorylated) with FYN, YES1
CC and SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with CBL,
CC GRB2 and SLA2. {ECO:0000256|ARBA:ARBA00064698}.
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; D4ACA7; -.
DR SMR; D4ACA7; -.
DR PeptideAtlas; D4ACA7; -.
DR Ensembl; ENSRNOT00000049357.6; ENSRNOP00000040411.4; ENSRNOG00000018414.9.
DR GeneID; 307403; -.
DR KEGG; rno:307403; -.
DR CTD; 1436; -.
DR RGD; 2425; Csf1r.
DR GeneTree; ENSGT00940000155506; -.
DR OMA; TIHKAKY; -.
DR OrthoDB; 6077854at2759; -.
DR PhylomeDB; D4ACA7; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000018414; Expressed in spleen and 19 other cell types or tissues.
DR ExpressionAtlas; D4ACA7; baseline and differential.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:1990682; C:CSF1-CSF1R complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019955; F:cytokine binding; IEA:Ensembl.
DR GO; GO:0005011; F:macrophage colony-stimulating factor receptor activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; IEA:Ensembl.
DR GO; GO:0045217; P:cell-cell junction maintenance; IEA:Ensembl.
DR GO; GO:0021879; P:forebrain neuron differentiation; IEA:Ensembl.
DR GO; GO:0044794; P:host-mediated activation of viral process; IEA:Ensembl.
DR GO; GO:0061518; P:microglial cell proliferation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0021772; P:olfactory bulb development; IEA:Ensembl.
DR GO; GO:0035265; P:organ growth; IEA:UniProtKB-ARBA.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl.
DR GO; GO:0120041; P:positive regulation of macrophage proliferation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0070848; P:response to growth factor; IEA:UniProtKB-ARBA.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0031529; P:ruffle organization; IEA:Ensembl.
DR CDD; cd05106; PTKc_CSF-1R; 1.
DR FunFam; 2.60.40.10:FF:001029; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:001088; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:001160; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:001169; 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; IPR013151; Immunoglobulin_dom.
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; PF00047; ig; 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; 5.
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; 4.
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 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000615-
KW 2};
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 Proteomics identification {ECO:0007829|PeptideAtlas:D4ACA7};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1022
FT /note="Macrophage colony-stimulating factor 1 receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003053633"
FT TRANSMEM 555..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..129
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 151..232
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 247..338
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 444..544
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 624..958
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 964..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..980
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 820
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 603
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 630..638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT BINDING 631..638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 658
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 706..712
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 824
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 825
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 838
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 965
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT DISULFID 86..128
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 171..221
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 268..322
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 461..527
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ SEQUENCE 1022 AA; 114164 MW; BBDC0E120E2505A6 CRC64;
MELGAPLVLL LATAWHGVQI LSGEKSRTTI HIYLLAGRRA VTTEIVLMGQ RSTDVQRVND
CQGAPVIEPS GPELVVEPGA TVTLRCVSNG SVEWDGPISP YWTLDSESPG SILITKNATF
KNTGTYRCTE LEDPMRGSTA IHLYVKDPVR PWNLLAQEVT VFEGQEAVLP CLITDPTLKD
SVSLVREWGR PVSRKTVYSF LPWRGFIIHK AKFLDSHTYM CKAVVNARES TSIGIRLKVN
RAHPGPPHII LEPTKLVRIR GEAAQIVCSA THSEVEFNVI LKRGDTKLEI PINSDFQDNA
YKKVLTLNLN AVDFQDAGIY SCVANNAAGS NTATMNFQVV ESAYLNLTSE QSLLQEVSVG
ENLDLTVIAD AYPGLQRYNW TYLGPFFEDP HNLEFRTQWT TYSYSFKLHL NRVKPLEAGR
YSLMAQNKAG WNNLTFELTL RYPPEVSVTW IPVNGSDVLL CDVSGYPQPN VTWMECRGHT
DRCDEAQASQ VWDDTQPEVL SQKPFHRVIL QSQLPIGTLK HNMTYVCRAH NNVGNSSQFF
RAISLGQSKQ LPDEYLFTPV VVACISVMSL LVLLLLLLLY KYKQKPKYQV RWKIIESYEG
NNYTFIDPTQ LPYNEKWEFP RNNLQFGKTL GAGAFGKVVE ATAFGLGKED AVLKVAVKML
KSTAHADEKE ALMSELKIMS HLGQHENIVN LLGACTHGGP VLVITEYCCY GDLLNFLRRK
AEAMLGPSLS PGQDPEGDSS YKNIHLEKKY VRRDSGFSSQ GVDTYVEMRP VSTSSNDSFF
KQDLDKEASR PLELWDLLHF SSQVAQGMAF LASKNCIHRD VAARNVLLTS GHVAKIGDFG
LARDIMNDSN YVVKGNARLP VKWMAPESIF DCVYTVQSDV WSYGILLWEI FSLGLNPYPG
ILVNNKFYKL VKDGYQMAQP VFAPENIYSI MQSCWDLEPT KRPTFQQICF LLQEQARLER
REQDYANLPS SSSSSSSSSD SGGGSGGSSS EPEEESSSEH LACCEPGDIA QPLLQPNNYQ
FC
//
