CSF1_RAT
ID CSF1_RAT Reviewed; 566 AA.
AC Q8JZQ0;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Macrophage colony-stimulating factor 1;
DE Short=CSF-1;
DE Short=MCSF;
DE Contains:
DE RecName: Full=Processed macrophage colony-stimulating factor 1;
DE Flags: Precursor;
GN Name=Csf1; Synonyms=Csfm;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISEASE.
RC STRAIN=Brown Norway/SsN, and Lewis/N;
RX PubMed=12074592; DOI=10.1016/s0006-291x(02)00598-3;
RA Dobbins D.E., Sood R., Hashiramoto A., Hansen C.T., Wilder R.L.,
RA Remmers E.F.;
RT "Mutation of macrophage colony stimulating factor (Csf1) causes
RT osteopetrosis in the tl rat.";
RL Biochem. Biophys. Res. Commun. 294:1114-1120(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISEASE.
RC STRAIN=Fischer 344;
RX PubMed=12379742; DOI=10.1073/pnas.202332999;
RA Van Wesenbeeck L., Odgren P.R., MacKay C.A., D'Angelo M., Safadi F.F.,
RA Popoff S.N., Van Hul W., Marks S.C. Jr.;
RT "The osteopetrotic mutation toothless (tl) is a loss-of-function frameshift
RT mutation in the rat Csf1 gene: evidence of a crucial role for CSF-1 in
RT osteoclastogenesis and endochondral ossification.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14303-14308(2002).
RN [3]
RP CLEAVAGE AFTER ARG-442, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
CC -!- FUNCTION: Cytokine that plays an essential role in the regulation of
CC survival, proliferation and differentiation of hematopoietic precursor
CC cells, especially mononuclear phagocytes, such as macrophages and
CC monocytes. Promotes the release of pro-inflammatory chemokines, and
CC thereby 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. Required for normal male
CC and female fertility. Promotes reorganization of the actin
CC cytoskeleton, regulates formation of membrane ruffles, cell adhesion
CC and cell migration. Plays a role in lipoprotein clearance (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer or heterodimer; disulfide-linked. Interacts with
CC CSF1R (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Processed macrophage colony-stimulating factor
CC 1]: Secreted, extracellular space {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=2 isoforms may be produced.;
CC Name=1;
CC IsoId=Q8JZQ0-1; Sequence=Displayed;
CC -!- PTM: N-glycosylated. The predominant soluble form is a chondroitin
CC sulfate-containing proteoglycan (By similarity). {ECO:0000250}.
CC -!- DISEASE: Note=A defect in Csf1 is the cause of the toothless phenotype
CC (tl). Toothless rats display osteoclastopenia, severe osteopetrosis,
CC and dystrophic growth plates. {ECO:0000269|PubMed:12074592,
CC ECO:0000269|PubMed:12379742}.
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DR EMBL; AF514355; AAM54135.1; -; mRNA.
DR EMBL; AF514356; AAM54136.1; -; mRNA.
DR EMBL; AF515736; AAM94802.1; -; mRNA.
DR AlphaFoldDB; Q8JZQ0; -.
DR SMR; Q8JZQ0; -.
DR STRING; 10116.ENSRNOP00000025221; -.
DR GlyGen; Q8JZQ0; 4 sites.
DR PaxDb; Q8JZQ0; -.
DR UCSC; RGD:621063; rat. [Q8JZQ0-1]
DR RGD; 621063; Csf1.
DR VEuPathDB; HostDB:ENSRNOG00000018659; -.
DR eggNOG; ENOG502S271; Eukaryota.
DR InParanoid; Q8JZQ0; -.
DR PhylomeDB; Q8JZQ0; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-449836; Other interleukin signaling.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q8JZQ0; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000018659; Expressed in spleen and 18 other tissues.
DR ExpressionAtlas; Q8JZQ0; baseline and differential.
DR Genevisible; Q8JZQ0; RN.
DR GO; GO:1990682; C:CSF1-CSF1R complex; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; ISO:RGD.
DR GO; GO:0008083; F:growth factor activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0005157; F:macrophage colony-stimulating factor receptor binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; IDA:RGD.
DR GO; GO:0003006; P:developmental process involved in reproduction; ISO:RGD.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0038145; P:macrophage colony-stimulating factor signaling pathway; ISO:RGD.
DR GO; GO:0030225; P:macrophage differentiation; IDA:RGD.
DR GO; GO:0060763; P:mammary duct terminal end bud growth; ISO:RGD.
DR GO; GO:0060611; P:mammary gland fat development; ISO:RGD.
DR GO; GO:0061518; P:microglial cell proliferation; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:RGD.
DR GO; GO:0042476; P:odontogenesis; IMP:RGD.
DR GO; GO:0001503; P:ossification; IMP:RGD.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:RGD.
DR GO; GO:0002158; P:osteoclast proliferation; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISO:RGD.
DR GO; GO:1902228; P:positive regulation of macrophage colony-stimulating factor signaling pathway; ISO:RGD.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:RGD.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; ISO:RGD.
DR GO; GO:1905523; P:positive regulation of macrophage migration; ISO:RGD.
DR GO; GO:1904141; P:positive regulation of microglial cell migration; ISO:RGD.
DR GO; GO:0045657; P:positive regulation of monocyte differentiation; ISO:RGD.
DR GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; ISO:RGD.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0042488; P:positive regulation of odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:0030278; P:regulation of ossification; ISO:RGD.
DR GO; GO:0002931; P:response to ischemia; ISO:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:RGD.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR008001; MCSF-1.
DR PANTHER; PTHR10058; PTHR10058; 2.
DR Pfam; PF05337; CSF-1; 1.
DR PIRSF; PIRSF001948; MCSF-1; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytokine; Disulfide bond;
KW Glycoprotein; Growth factor; Immunity; Inflammatory response;
KW Innate immunity; Membrane; Proteoglycan; Reference proteome; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..566
FT /note="Macrophage colony-stimulating factor 1"
FT /id="PRO_0000005859"
FT CHAIN 33..442
FT /note="Processed macrophage colony-stimulating factor 1"
FT /evidence="ECO:0000305|PubMed:26479776"
FT /id="PRO_0000296233"
FT TOPO_DOM 33..508
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 197..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 566 AA; 62187 MW; 067BBAE5BC28D892 CRC64;
MTARGAAGRC PSSTWMGSRL LLVCLLVSRS VAEVSEHCSH MIGNGHLQIL QQLIDSQMET
ACLIEYKFVD QEQLDDPVCY LKKAFVLVQV IIEETMRFKD NTPNANATER LQELSMKLNS
CFIKDYKEQN EACVQTYKES PLRLLEKIKN FFNETKNFLE KDWNIFSKNC NDSFAKCSSR
DVVTKPDCNC LYPKATPSSD LASASPHQPP APSMAPLADL AWDDSQRTEG SSLLPSDLPL
RIEDPGSAKQ RPPRSTCQTL ESTEQPNHED PQPHPSAGAP IPGVEDIIES SMGTNWVLEE
ASGEASEGFL TQERKFSPSN PVGGSIQAET DRPWARSASS PFPKLTEDQQ PTNITDTPLT
EVNPMRPTGQ TLNNTPEKTD GSSTLREDQQ EPRSPHFATL NPQRVGNSAT PYAKLLPPKS
HSWGIVLPLG ELEGKKSTRD RRSPAELKGG PASEGAARPV AQSTRDRRSP AELKGGPASE
GAARPVARFN SIPLTDTGSS IQDPQTSAFV FWVLGIILVL LAVGGLLFYS WKRRSHRDPR
TLDSSVGRPE GSSLAQDEDR QVELPV
