P01587 (CSF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Granulocyte-macrophage colony-stimulating factor
Short name=GM-CSF

Alternative name(s):
Colony-stimulating factor
Short name=CSF

Gene names

Name:	Csf2
Synonyms:	Csfgm

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	141 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Subunit structure	Monomer. The signaling GM-CSF receptor complex is a dodecamer of two head-to-head hexamers of two alpha, two beta, and two ligand subunits By similarity.
Subcellular location	Secreted.
Sequence similarities	Belongs to the GM-CSF family.
Sequence caution	The sequence CAA26192.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Cytokine Growth factor
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to lipopolysaccharide Inferred from electronic annotation. Source: Compara dendritic cell differentiation Inferred from electronic annotation. Source: Compara embryonic placenta development Inferred from mutant phenotype PubMed 19228596. Source: MGI epithelial fluid transport Inferred from electronic annotation. Source: Compara immune response Inferred from electronic annotation. Source: InterPro macrophage activation Inferred from electronic annotation. Source: Compara myeloid dendritic cell differentiation Inferred from direct assay PubMed 12021780. Source: MGI negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of cytolysis Inferred from electronic annotation. Source: Compara positive regulation of DNA replication Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from direct assay PubMed 10652277PubMed 1350248. Source: MGI positive regulation of gene expression Inferred from electronic annotation. Source: Compara positive regulation of interleukin-23 production Inferred from electronic annotation. Source: Compara positive regulation of macrophage derived foam cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of podosome assembly Inferred from electronic annotation. Source: Compara positive regulation of tyrosine phosphorylation of Stat5 protein Inferred from electronic annotation. Source: Compara regulation of gene expression Inferred from direct assay PubMed 9697835. Source: MGI
Cellular_component	extracellular space Inferred from direct assay PubMed 7690439. Source: MGI
Molecular_function	cytokine activity Inferred from direct assay PubMed 10652277PubMed 1350248. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17
	Chain	18 – 141	124	Granulocyte-macrophage colony-stimulating factor		PRO_0000005866
Amino acid modifications
	Glycosylation	22	1	O-linked (GalNAc...) By similarity
	Glycosylation	27	1	O-linked (GalNAc...) By similarity
	Glycosylation	83	1	N-linked (GlcNAc...)
	Glycosylation	92	1	N-linked (GlcNAc...)
	Disulfide bond	68 ↔ 110		Ref.8
	Disulfide bond	102 ↔ 135		Ref.8
Experimental info
	Mutagenesis	38	1	E → P: Reduction in bioactivity.
	Mutagenesis	73	1	L → P: 25-fold reduction in bioactivity.
	Mutagenesis	77	1	E → P: 50-fold reduction in bioactivity.
	Mutagenesis	80	1	L → P: 450-fold reduction in bioactivity.
	Mutagenesis	124	1	L → P: 5500-fold reduction in bioactivity.
	Sequence conflict	25	1	T → I in CAA29336. Ref.5
	Sequence conflict	25	1	T → I AA sequence Ref.7
	Sequence conflict	114	1	V → A in AAA37483. Ref.6
	Sequence conflict	139	1	G → S in CAA29336. Ref.5
	Sequence conflict	139	1	G → V in CAA26820. Ref.2
	Sequence conflict	139	1	G → V no nucleotide entry Ref.3
	Sequence conflict	139	1	G → V in CAA26192. Ref.4
	Sequence conflict	139	1	G → V in CAA26193. Ref.4
	Sequence conflict	139	1	G → V in AAA37483. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P01587 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 209C7CBB4FF77349	FASTA	141	16,091
	10 20 30 40 50 60 MWLQNLLFLG IVVYSLSAPT RSPITVTRPW KHVEAIKEAL NLLDDMPVTL NEEVEVVSNE 70 80 90 100 110 120 FSFKKLTCVQ TRLKIFEQGL RGNFTKLKGA LNMTASYYQT YCPPTPETDC ETQVTTYADF 130 140 IDSLKTFLTD IPFECKKPGQ K

References

[1]	"Structure of the chromosomal gene for granulocyte-macrophage colony stimulating factor: comparison of the mouse and human genes." Miyatake S., Otsuka T., Yokota T., Lee F., Arai K. EMBO J. 4:2561-2568(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The structure and expression of the murine gene encoding granulocyte-macrophage colony stimulating factor: evidence for utilisation of alternative promoters." Stanley E.R., Metcalf D., Sobieszczuk P., Gough N.M., Dunn A.R. EMBO J. 4:2569-2573(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Recombinant murine GM-CSF from E. coli has biological activity and is neutralized by a specific antiserum." Delamarter J.F., Mermod J.-J., Liang C.M., Eliason J.F., Thatcher D.R. EMBO J. 4:2575-2581(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Structure and expression of the mRNA for murine granulocyte-macrophage colony stimulating factor." Gough N.M., Metcalf D., Gough J., Grail D., Dunn A.R. EMBO J. 4:645-653(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[5]	"Molecular cloning of cDNA encoding a murine haematopoietic growth regulator, granulocyte-macrophage colony stimulating factor." Gough N.M., Gough J., Metcalf D., Kelso A., Grail D., Nicola N.A., Burgess A.W., Dunn A.R. Nature 309:763-767(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-141. Tissue: Lung.
[6]	"Cloning, sequence, and expression of a human granulocyte/macrophage colony-stimulating factor." Cantrell M.A., Anderson D., Cerretti D.P., Price V., McKereghan K., Tushinski R.J., Mochizuki D.Y., Larsen A., Grabstein S., Gillis S., Cosman D. Proc. Natl. Acad. Sci. U.S.A. 82:6250-6254(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-141.
[7]	"Purification and partial amino acid sequence of asialo murine granulocyte-macrophage colony stimulating factor." Sparrow L.G., Metcalf D., Hunkapiller M.W., Hood L.E., Burgess A.W. Proc. Natl. Acad. Sci. U.S.A. 82:292-296(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-57.
[8]	"Characterization of human and mouse granulocyte-macrophage-colony-stimulating factors derived from Escherichia coli." Schrimser J.L., Rose K., Simona M.G., Wingfield P. Biochem. J. 247:195-199(1987) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS.
[9]	"Single proline substitutions in predicted alpha-helices of murine granulocyte-macrophage colony-stimulating factor result in a loss in bioactivity and altered glycosylation." Altmann S.W., Johnson G.D., Prystowsky M.B. J. Biol. Chem. 266:5333-5341(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X03020 Genomic DNA. Translation: CAA26821.1. X03019 mRNA. Translation: CAA26820.1. X02333 mRNA. Translation: CAA26193.1. X02333 mRNA. Translation: CAA26192.1. Different initiation. X05906 mRNA. Translation: CAA29336.1. M11848 mRNA. Translation: AAA37483.1.
IPI	IPI00323907.
PIR	FQMSGM. I48368.
RefSeq	NP_034099.2. NM_009969.4.
UniGene	Mm.4922.
3D structure databases
ProteinModelPortal	P01587.
SMR	P01587. Positions 21-138.
ModBase	Search...
PTM databases
PhosphoSite	P01587.
Proteomic databases
PRIDE	P01587.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000019060; ENSMUSP00000019060; ENSMUSG00000018916.
GeneID	12981.
KEGG	mmu:12981.
UCSC	uc007ixm.1. mouse.
Organism-specific databases
CTD	1437.
MGI	MGI:1339752. Csf2.
Phylogenomic databases
eggNOG	NOG42131.
HOGENOM	HOG000037940.
HOVERGEN	HBG000532.
InParanoid	P01587.
KO	K05427.
OMA	TCLQTRL.
OrthoDB	EOG4255V3.
Gene expression databases
ArrayExpress	P01587.
Bgee	P01587.
Genevestigator	P01587.
GermOnline	ENSMUSG00000018916. Mus musculus.
Family and domain databases
Gene3D	1.20.1250.10. 1 hit.
InterPro	IPR009079. 4_helix_cytokine-like_core. IPR012351. 4_helix_cytokine_core. IPR000773. GM_colony-stim-fac. [Graphical view]
PANTHER	PTHR10059. PTHR10059. 1 hit.
Pfam	PF01109. GM_CSF. 1 hit. [Graphical view]
PRINTS	PR00693. GMCSFACTOR.
ProDom	PD007349. GM_colony-stim-fac. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00040. CSF2. 1 hit. [Graphical view]
SUPFAM	SSF47266. 4_helix_cytokine. 1 hit.
PROSITE	PS00702. GM_CSF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CSF2. mouse.
NextBio	282756.
SOURCE	Search...

Entry information

Entry name

CSF2_MOUSE

Accession

Primary (citable) accession number: P01587

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	May 29, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program