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P07141 (CSF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Macrophage colony-stimulating factor 1

Short name=CSF-1
Short name=MCSF

Cleaved into the following chain:

  1. Processed macrophage colony-stimulating factor 1
Gene names
Name:Csf1
Synonyms:Csfm
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance.

Subunit structure

Homodimer or heterodimer; disulfide-linked. Interacts with CSF1R. Ref.14

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Processed macrophage colony-stimulating factor 1: Secretedextracellular space By similarity.

Post-translational modification

N-glycosylated. The predominant soluble form is a chondroitin sulfate-containing proteoglycan.

Involvement in disease

A defect in Csf1 is the cause of osteopetrosis. Osteopetrotic mice (op/op) are severely deficient in mature macrophages and osteoclasts, display failed tooth eruption, and have a restricted capacity for bone remodeling. Ref.13

Caution

The sequence reported in Ref.3 was thought to originate from rat, but was later shown (Ref.10 and Ref.11) to be derived from mouse.

Ontologies

Keywords
   Biological processImmunity
Inflammatory response
Innate immunity
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionCytokine
Growth factor
   PTMDisulfide bond
Glycoprotein
Proteoglycan
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbranching involved in mammary gland duct morphogenesis

Inferred from mutant phenotype PubMed 10804170. Source: MGI

developmental process involved in reproduction

Inferred from mutant phenotype PubMed 16237150. Source: BHF-UCL

homeostasis of number of cells within a tissue

Inferred from mutant phenotype PubMed 9215625. Source: MGI

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

macrophage differentiation

Inferred from electronic annotation. Source: Ensembl

mammary duct terminal end bud growth

Inferred from mutant phenotype PubMed 10804170. Source: MGI

mammary gland fat development

Inferred from mutant phenotype PubMed 10804170. Source: MGI

odontogenesis

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from electronic annotation. Source: Ensembl

osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

osteoclast proliferation

Inferred from direct assay PubMed 22451653. Source: MGI

positive regulation of Ras protein signal transduction

Inferred from direct assay PubMed 17053831. Source: MGI

positive regulation of cell migration

Inferred from genetic interaction PubMed 17053831. Source: MGI

positive regulation of cell-matrix adhesion

Inferred from genetic interaction PubMed 17053831. Source: MGI

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage derived foam cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage differentiation

Inferred from mutant phenotype PubMed 9215625. Source: MGI

positive regulation of monocyte differentiation

Inferred from mutant phenotype PubMed 9215625. Source: MGI

positive regulation of mononuclear cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of multicellular organism growth

Inferred from mutant phenotype PubMed 12865350. Source: MGI

positive regulation of odontogenesis of dentin-containing tooth

Inferred from mutant phenotype PubMed 12865350. Source: MGI

positive regulation of osteoclast differentiation

Inferred from direct assay PubMed 15657444. Source: MGI

positive regulation of protein kinase activity

Inferred from genetic interaction PubMed 17053831. Source: MGI

regulation of ossification

Inferred from mutant phenotype PubMed 12865350. Source: MGI

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

receptor complex

Inferred from direct assay Ref.14. Source: BHF-UCL

   Molecular_functionmacrophage colony-stimulating factor receptor binding

Inferred from physical interaction Ref.14. Source: BHF-UCL

protein homodimerization activity

Inferred from physical interaction Ref.14. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07141-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P07141-2)

The sequence of this isoform differs from the canonical sequence as follows:
     182-476: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Ref.8
Chain33 – 552520Macrophage colony-stimulating factor 1
PRO_0000005858
Chain33 – ?Processed macrophage colony-stimulating factor 1PRO_0000296232

Regions

Topological domain33 – 492460Extracellular Potential
Transmembrane493 – 51523Helical; Potential
Topological domain516 – 55237Cytoplasmic Potential

Amino acid modifications

Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation1721N-linked (GlcNAc...) Potential
Disulfide bond39 ↔ 122 Ref.14
Disulfide bond63Interchain Ref.14
Disulfide bond80 ↔ 171 Ref.14
Disulfide bond134 ↔ 178 Ref.14
Disulfide bond189Interchain By similarity
Disulfide bond191Interchain By similarity

Natural variations

Alternative sequence182 – 476295Missing in isoform 2.
VSP_001189
Natural variant2921D → G.
Natural variant3451S → P.

Experimental info

Sequence conflict31Missing in AAA37480. Ref.7
Sequence conflict61A → R in AAA37480. Ref.7
Sequence conflict7 – 82AG → PR in AAA37480. Ref.7
Sequence conflict2461P → A in CAA28660. Ref.1

Secondary structure

....................... 552
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 3886D72D70E770AF

FASTA55260,649
        10         20         30         40         50         60 
MTARGAAGRC PSSTWLGSRL LLVCLLMSRS IAKEVSEHCS HMIGNGHLKV LQQLIDSQME 

        70         80         90        100        110        120 
TSCQIAFEFV DQEQLDDPVC YLKKAFFLVQ DIIDETMRFK DNTPNANATE RLQELSNNLN 

       130        140        150        160        170        180 
SCFTKDYEEQ NKACVRTFHE TPLQLLEKIK NFFNETKNLL EKDWNIFTKN CNNSFAKCSS 

       190        200        210        220        230        240 
RDVVTKPDCN CLYPKATPSS DPASASPHQP PAPSMAPLAG LAWDDSQRTE GSSLLPSELP 

       250        260        270        280        290        300 
LRIEDPGSAK QRPPRSTCQT LESTEQPNHG DRLTEDSQPH PSAGGPVPGV EDILESSLGT 

       310        320        330        340        350        360 
NWVLEEASGE ASEGFLTQEA KFSPSTPVGG SIQAETDRPR ALSASPFPKS TEDQKPVDIT 

       370        380        390        400        410        420 
DRPLTEVNPM RPIGQTQNNT PEKTDGTSTL REDHQEPGSP HIATPNPQRV SNSATPVAQL 

       430        440        450        460        470        480 
LLPKSHSWGI VLPLGELEGK RSTRDRRSPA ELEGGSASEG AARPVARFNS IPLTDTGHVE 

       490        500        510        520        530        540 
QHEGSSDPQI PESVFHLLVP GIILVLLTVG GLLFYKWKWR SHRDPQTLDS SVGRPEDSSL 

       550 
TQDEDRQVEL PV 

« Hide

Isoform 2 [UniParc].

Checksum: E1EF2A20C416E591
Show »

FASTA25729,353

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a cDNA encoding murine CSF-1 (Macrophage-CSF)."
Delamarter J.F., Hession C., Semon D., Gough N.M., Rothenbuhler R., Mermod J.-J.
Nucleic Acids Res. 15:2389-2390(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"cDNA cloning and expression of murine macrophage colony-stimulating factor from L929 cells."
Ladner M.B., Martin G.A., Noble J.A., Wittman V.P., Warren M.K., McGrogan M., Stanley E.R.
Proc. Natl. Acad. Sci. U.S.A. 85:6706-6710(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Isolation and characterization of a cDNA clone encoding for rat CSF-1 gene. Post-transcriptional repression occurs in myogenic differentiation."
Borycki A.G., Lenormund J., Guillier M., Leibovitch S.A.
Biochim. Biophys. Acta 1174:143-152(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Head and Spinal cord.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Embryonic germ cell and Neural stem cell.
[7]"Cloning and tissue-specific expression of mouse macrophage colony-stimulating factor mRNA."
Rajavashisth T.B., Eng R., Shadduck R.K., Waheed A., Ben-Avram C.M., Shively J.E., Lusis A.J.
Proc. Natl. Acad. Sci. U.S.A. 84:1157-1161(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-100.
[8]"Amino-terminal amino acid sequence of murine colony-stimulating factor 1."
Ben-Avram C.M., Shively J.E., Shadduck R.K., Waheed A., Rajavashisth T.B., Lusis A.J.
Proc. Natl. Acad. Sci. U.S.A. 82:4486-4489(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-57.
[9]"Cloning and characterization of the murine promoter for the colony-stimulating factor-1-encoding gene."
Harrington M.A., Edenberg H.J., Saxman S.M., Pedigo L.M., Daub R., Broxmeyer H.E.
Gene 102:165-170(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-13.
[10]"Mutation of macrophage colony stimulating factor (Csf1) causes osteopetrosis in the tl rat."
Dobbins D.E., Sood R., Hashiramoto A., Hansen C.T., Wilder R.L., Remmers E.F.
Biochem. Biophys. Res. Commun. 294:1114-1120(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:8357831 ORIGINATES FROM MOUSE.
[11]"The osteopetrotic mutation toothless (tl) is a loss-of-function frameshift mutation in the rat Csf1 gene: evidence of a crucial role for CSF-1 in osteoclastogenesis and endochondral ossification."
Van Wesenbeeck L., Odgren P.R., MacKay C.A., D'Angelo M., Safadi F.F., Popoff S.N., Van Hul W., Marks S.C. Jr.
Proc. Natl. Acad. Sci. U.S.A. 99:14303-14308(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:8357831 ORIGINATES FROM MOUSE.
[12]"The predominant form of secreted colony stimulating factor-1 is a proteoglycan."
Price L.K.H., Choi H.U., Rosenberg L., Stanley E.R.
J. Biol. Chem. 267:2190-2199(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[13]"The murine mutation osteopetrosis is in the coding region of the macrophage colony stimulating factor gene."
Yoshida H., Hayashi S., Kunisada T., Ogawa M., Nishikawa S., Okamura H., Sudo T., Shultz L.D., Nishikawa S.
Nature 345:442-444(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[14]"Structure of macrophage colony stimulating factor bound to FMS: diverse signaling assemblies of class III receptor tyrosine kinases."
Chen X., Liu H., Focia P.J., Shim A.H., He X.
Proc. Natl. Acad. Sci. U.S.A. 105:18267-18272(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 36-180 IN COMPLEX WITH CSF1R, SUBUNIT, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05010 mRNA. Translation: CAA28660.1.
M21952 mRNA. Translation: AAA37481.1.
M21149 mRNA. Translation: AAA37482.1.
M84361 mRNA. Translation: AAA03032.1.
AK138489 mRNA. Translation: BAE23681.1.
AK154872 mRNA. Translation: BAE32893.1.
AK160995 mRNA. Translation: BAE36140.1.
CH466607 Genomic DNA. Translation: EDL01916.1.
CH466607 Genomic DNA. Translation: EDL01919.1.
BC025593 mRNA. Translation: AAH25593.1.
BC066187 mRNA. Translation: AAH66187.1.
BC066200 mRNA. Translation: AAH66200.1.
BC066205 mRNA. Translation: AAH66205.1.
M15692 mRNA. Translation: AAA37480.1.
M81316 Unassigned DNA. Translation: AAA19866.1.
PIRA31401.
RefSeqNP_001107001.1. NM_001113529.1.
NP_001107002.1. NM_001113530.1.
NP_031804.3. NM_007778.4.
UniGeneMm.795.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EJJX-ray2.40A/B36-180[»]
3UF5X-ray2.80A/B33-181[»]
4ADQX-ray4.50E/F/G/H33-181[»]
ProteinModelPortalP07141.
SMRP07141. Positions 36-180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-45278N.
IntActP07141. 42 interactions.

PTM databases

PhosphoSiteP07141.

Proteomic databases

PaxDbP07141.
PRIDEP07141.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000014743; ENSMUSP00000014743; ENSMUSG00000014599. [P07141-1]
ENSMUST00000118593; ENSMUSP00000113136; ENSMUSG00000014599. [P07141-2]
ENSMUST00000120243; ENSMUSP00000113617; ENSMUSG00000014599. [P07141-1]
GeneID12977.
KEGGmmu:12977.
UCSCuc008qxk.2. mouse. [P07141-1]
uc008qxl.2. mouse. [P07141-2]

Organism-specific databases

CTD1435.
MGIMGI:1339753. Csf1.

Phylogenomic databases

eggNOGNOG43822.
GeneTreeENSGT00390000015805.
HOGENOMHOG000112010.
HOVERGENHBG005410.
InParanoidQ3U395.
KOK05453.
OMADTGHERQ.
OrthoDBEOG7GBFZ6.
PhylomeDBP07141.
TreeFamTF337718.

Gene expression databases

ArrayExpressP07141.
BgeeP07141.
CleanExMM_CSF1.
GenevestigatorP07141.

Family and domain databases

InterProIPR009079. 4_helix_cytokine-like_core.
IPR008001. MCSF-1.
[Graphical view]
PANTHERPTHR10058. PTHR10058. 1 hit.
PfamPF05337. CSF-1. 2 hits.
[Graphical view]
PIRSFPIRSF001948. MCSF-1. 1 hit.
SUPFAMSSF47266. SSF47266. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP07141.
NextBio282746.
PROP07141.
SOURCESearch...

Entry information

Entry nameCSF1_MOUSE
AccessionPrimary (citable) accession number: P07141
Secondary accession number(s): Q3U395, Q8R3C8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot