ID A0A1S3FY95_DIPOR Unreviewed; 978 AA.
AC A0A1S3FY95;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 47.
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|RefSeq:XP_012881009.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012881009.1};
RN [1] {ECO:0000313|RefSeq:XP_012881009.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012881009.1};
RG RefSeq;
RL Submitted (AUG-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 RefSeq; XP_012881009.1; XM_013025555.1.
DR AlphaFoldDB; A0A1S3FY95; -.
DR FunCoup; A0A1S3FY95; 931.
DR STRING; 10020.ENSDORP00000009298; -.
DR GeneID; 105992611; -.
DR KEGG; dord:105992611; -.
DR CTD; 1436; -.
DR InParanoid; A0A1S3FY95; -.
DR OrthoDB; 6077854at2759; -.
DR Proteomes; UP000081671; Unplaced.
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:0019903; F:protein phosphatase binding; IEA:UniProtKB-ARBA.
DR GO; GO:0009653; P:anatomical structure morphogenesis; 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:0061518; P:microglial cell proliferation; 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:0008284; P:positive regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR GO; GO:0010604; P:positive regulation of macromolecule metabolic process; IEA:UniProtKB-ARBA.
DR GO; GO:0022604; P:regulation of cell 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 GO; GO:0006950; P:response to stress; IEA:UniProtKB-ARBA.
DR CDD; cd00096; Ig; 1.
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:001101; 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; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
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};
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:UP000081671};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..978
FT /note="Macrophage colony-stimulating factor 1 receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010299063"
FT TRANSMEM 513..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..100
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 203..294
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 401..501
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 578..916
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 920..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..947
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 774
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 557
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 584..592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT BINDING 585..592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 660..666
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 778
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 779
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 792
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 919
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT DISULFID 42..84
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 127..177
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 224..278
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 418..484
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ SEQUENCE 978 AA; 109329 MW; 7F579D1DB7FECA21 CRC64;
MGLGALLILL VATAWLGQGT PVIEPSGPEL VVEPGTVVTL RCVGNGSVQW DGPTPPLWKL
DPDNPSSIWI TNNATFQHTG TYRCSETGGL SGGTASIHLY VKDPVRPWKL LAEEVTVFEG
EDAVLPCLLT DPALSAHVSL MRERGRPVGR HIVYSFSPLR GFTIHKAKYL DSHYYQCRVL
VNGRMVPSLG IKLKVNKVLK GPPALTLEPT ELVRIRGENA QITCKATEPG VHFYVLLKHG
DTKLNISQEV DFQDNKYHKV LALNLSAVDF QDSGNYTCLA TNSMGVRSNS MILQVVESAY
LNLTSEQNLL QEVTVGESLN LKVKVDAYPG LQTYSWTYLG PFFDHQPSLD FIIKKDTYSR
YSTLLSLPRL KPWEAGRYSF RARNARGWSA LTFNLTLQYP PEVSVTWARI NGSNILFCNV
SGYPQPNVTW LMCRGHTDRC ERAQMLQTWE DSELKVLYQE PFRKVIVQSQ LIVGAFQHNT
TYECRAHNSV GNSSETFRAV TSESVVKPPE GSLFMPVVVS CLVVMTFLLL LLLYKYKQKP
KYQIRWKIIE SYEGNNYTFI DPTQLPYNEK WEFPRNNLQF GKTLGAGAFG KVVEATAFGL
GKEDAVLKVA VKMLKSTAHA DEKEALMSEL KIMSHLGQHE NIVNLLGACT HGGPVLVITE
YCCYGDLLNF LRRKAEAMLG PSLNPSQDPE GETSYKNVHL EKKYIRRDSG FSSQGMDTYV
EMRPVSTSSN DSFPEQDLDK EESRPLELWD LLHFSTQVAQ GMAFLASKNC IHRDVAARNV
LLTNGHVAKI GDFGLARDIM NDSNYIVKGN ARLPVKWMAP ESIFDCIYTV QSDVWSYGIL
LWEIFSLGLN PYPGILVNSK FYKLVKDGYQ MAQPAFAPKN IYSIMQACWD LEPTQRPTFQ
QICTLLQKQD QAHRREQDYA NLPNSSSSNG DGCGSSSSSN NSSSSSSMEP EESASEHLAC
CEPDAAQPLL QPNNYQFC
//
