ID CSF2_MOUSE Reviewed; 141 AA. AC P01587; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 04-NOV-2026, entry version 186. DE RecName: Full=Granulocyte-macrophage colony-stimulating factor; DE Short=GM-CSF; DE AltName: Full=Colony-stimulating factor; DE Short=CSF; DE Flags: Precursor; GN Name=Csf2; Synonyms=Csfgm; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3876930; DOI=10.1002/j.1460-2075.1985.tb03971.x; RA Miyatake S., Otsuka T., Yokota T., Lee F., Arai K.; RT "Structure of the chromosomal gene for granulocyte-macrophage colony RT stimulating factor: comparison of the mouse and human genes."; RL EMBO J. 4:2561-2568(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3876931; DOI=10.1002/j.1460-2075.1985.tb03972.x; RA Stanley E.R., Metcalf D., Sobieszczuk P., Gough N.M., Dunn A.R.; RT "The structure and expression of the murine gene encoding granulocyte- RT macrophage colony stimulating factor: evidence for utilisation of RT alternative promoters."; RL EMBO J. 4:2569-2573(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3902470; DOI=10.1002/j.1460-2075.1985.tb03973.x; RA Delamarter J.F., Mermod J.-J., Liang C.M., Eliason J.F., Thatcher D.R.; RT "Recombinant murine GM-CSF from E. coli has biological activity and is RT neutralized by a specific antiserum."; RL EMBO J. 4:2575-2581(1985). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; RX PubMed=3874057; DOI=10.1002/j.1460-2075.1985.tb03678.x; RA Gough N.M., Metcalf D., Gough J., Grail D., Dunn A.R.; RT "Structure and expression of the mRNA for murine granulocyte-macrophage RT colony stimulating factor."; RL EMBO J. 4:645-653(1985). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-141. RC TISSUE=Lung; RX PubMed=6610831; DOI=10.1038/309763a0; RA Gough N.M., Gough J., Metcalf D., Kelso A., Grail D., Nicola N.A., RA Burgess A.W., Dunn A.R.; RT "Molecular cloning of cDNA encoding a murine haematopoietic growth RT regulator, granulocyte-macrophage colony stimulating factor."; RL Nature 309:763-767(1984). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-141. RX PubMed=3898082; DOI=10.1073/pnas.82.18.6250; RA Cantrell M.A., Anderson D., Cerretti D.P., Price V., McKereghan K., RA Tushinski R.J., Mochizuki D.Y., Larsen A., Grabstein S., Gillis S., RA Cosman D.; RT "Cloning, sequence, and expression of a human granulocyte/macrophage RT colony-stimulating factor."; RL Proc. Natl. Acad. Sci. U.S.A. 82:6250-6254(1985). RN [7] RP PROTEIN SEQUENCE OF 24-57. RX PubMed=3871523; DOI=10.1073/pnas.82.2.292; RA Sparrow L.G., Metcalf D., Hunkapiller M.W., Hood L.E., Burgess A.W.; RT "Purification and partial amino acid sequence of asialo murine granulocyte- RT macrophage colony stimulating factor."; RL Proc. Natl. Acad. Sci. U.S.A. 82:292-296(1985). RN [8] RP DISULFIDE BONDS. RX PubMed=3318813; DOI=10.1042/bj2470195; RA Schrimser J.L., Rose K., Simona M.G., Wingfield P.; RT "Characterization of human and mouse granulocyte-macrophage-colony- RT stimulating factors derived from Escherichia coli."; RL Biochem. J. 247:195-199(1987). RN [9] RP MUTAGENESIS. RX PubMed=2002066; DOI=10.1016/s0021-9258(19)67792-6; RA Altmann S.W., Johnson G.D., Prystowsky M.B.; RT "Single proline substitutions in predicted alpha-helices of murine RT granulocyte-macrophage colony-stimulating factor result in a loss in RT bioactivity and altered glycosylation."; RL J. Biol. Chem. 266:5333-5341(1991). CC -!- FUNCTION: Cytokine that stimulates the growth and differentiation of CC hematopoietic precursor cells from various lineages, including CC granulocytes, macrophages, eosinophils and erythrocytes. CC -!- SUBUNIT: Monomer. The signaling GM-CSF receptor complex is a dodecamer CC of two head-to-head hexamers of two alpha, two beta, and two ligand CC subunits (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the GM-CSF family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA26192.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X03020; CAA26821.1; -; Genomic_DNA. DR EMBL; X03019; CAA26820.1; -; mRNA. DR EMBL; X02333; CAA26193.1; -; mRNA. DR EMBL; X02333; CAA26192.1; ALT_INIT; mRNA. DR EMBL; X05906; CAA29336.1; -; mRNA. DR EMBL; M11848; AAA37483.1; -; mRNA. DR CCDS; CCDS24692.1; -. DR PIR; I48368; FQMSGM. DR RefSeq; NP_034099.2; NM_009969.4. DR AlphaFoldDB; P01587; -. DR SMR; P01587; -. DR FunCoup; P01587; 565. DR STRING; 10090.ENSMUSP00000019060; -. DR GlyCosmos; P01587; 4 sites, No reported glycans. DR GlyGen; P01587; 5 sites. DR PhosphoSitePlus; P01587; -. DR PaxDb; 10090-ENSMUSP00000019060; -. DR Antibodypedia; 14363; 2128 antibodies from 56 providers. DR DNASU; 12981; -. DR Ensembl; ENSMUST00000019060.6; ENSMUSP00000019060.6; ENSMUSG00000018916.6. DR GeneID; 12981; -. DR KEGG; mmu:12981; -. DR UCSC; uc007ixm.1; mouse. DR AGR; MGI:1339752; -. DR CTD; 1437; -. DR MGI; MGI:1339752; Csf2. DR VEuPathDB; HostDB:ENSMUSG00000018916; -. DR eggNOG; ENOG502TDUI; Eukaryota. DR GeneTree; ENSGT00390000013425; -. DR HOGENOM; CLU_152286_0_0_1; -. DR InParanoid; P01587; -. DR OMA; ACNEQTI; -. DR OrthoDB; 9633166at2759; -. DR PhylomeDB; P01587; -. DR Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling. DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade. DR Reactome; R-MMU-912526; Interleukin receptor SHC signaling. DR BioGRID-ORCS; 12981; 2 hits in 81 CRISPR screens. DR PRO; PR:P01587; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P01587; protein. DR Bgee; ENSMUSG00000018916; Expressed in left lung lobe and 20 other cell types or tissues. DR ExpressionAtlas; P01587; baseline and differential. DR GO; GO:0005576; C:extracellular region; IDA:MGI. DR GO; GO:0030526; C:granulocyte macrophage colony-stimulating factor receptor complex; ISO:GO_Central. DR GO; GO:0005125; F:cytokine activity; IDA:MGI. DR GO; GO:0005129; F:granulocyte macrophage colony-stimulating factor receptor binding; IEA:InterPro. DR GO; GO:0008083; F:growth factor activity; IEA:InterPro. DR GO; GO:0007259; P:cell surface receptor signaling pathway via JAK-STAT; ISO:GO_Central. DR GO; GO:0097696; P:cell surface receptor signaling pathway via STAT; ISO:GO_Central. DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISO:GO_Central. DR GO; GO:0097028; P:dendritic cell differentiation; ISO:GO_Central. DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI. DR GO; GO:0042045; P:epithelial fluid transport; ISO:GO_Central. DR GO; GO:0038157; P:granulocyte-macrophage colony-stimulating factor signaling pathway; ISO:GO_Central. DR GO; GO:0001821; P:histamine secretion; ISO:GO_Central. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0030225; P:macrophage differentiation; ISO:GO_Central. DR GO; GO:0030224; P:monocyte differentiation; IDA:MGI. DR GO; GO:0030099; P:myeloid cell differentiation; IBA:GO_Central. DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IDA:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:GO_Central. DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:GO_Central. DR GO; GO:0030223; P:neutrophil differentiation; IDA:MGI. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:GO_Central. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:GO_Central. DR GO; GO:0032747; P:positive regulation of interleukin-23 production; ISO:GO_Central. DR GO; GO:0070665; P:positive regulation of leukocyte proliferation; ISO:GO_Central. DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:GO_Central. DR GO; GO:0071803; P:positive regulation of podosome assembly; ISO:GO_Central. DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI. DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; ISO:GO_Central. DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI. DR CDD; cd00040; CSF2; 1. DR Gene3D; 1.20.1250.10; -; 1. DR InterPro; IPR009079; 4_helix_cytokine-like_core. DR InterPro; IPR000773; GM_colony-stim-fac. DR PANTHER; PTHR10059:SF0; GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR; 1. DR PANTHER; PTHR10059; GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR GM-CSF; 1. DR Pfam; PF01109; GM_CSF; 1. DR PRINTS; PR00693; GMCSFACTOR. DR SMART; SM00040; CSF2; 1. DR SUPFAM; SSF47266; 4-helical cytokines; 1. DR PROSITE; PS00702; GM_CSF; 1. PE 1: Evidence at protein level; KW Cytokine; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Growth factor; Reference proteome; Secreted; Signal. FT SIGNAL 1..17 FT CHAIN 18..141 FT /note="Granulocyte-macrophage colony-stimulating factor" FT /id="PRO_0000005866" FT CARBOHYD 22 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000250" FT CARBOHYD 27 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000250" FT CARBOHYD 83 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 92 FT /note="N-linked (GlcNAc...) asparagine" FT DISULFID 68..110 FT /evidence="ECO:0000269|PubMed:3318813" FT DISULFID 102..135 FT /evidence="ECO:0000269|PubMed:3318813" FT MUTAGEN 38 FT /note="E->P: Reduction in bioactivity." FT /evidence="ECO:0000269|PubMed:2002066" FT MUTAGEN 73 FT /note="L->P: 25-fold reduction in bioactivity." FT /evidence="ECO:0000269|PubMed:2002066" FT MUTAGEN 77 FT /note="E->P: 50-fold reduction in bioactivity." FT /evidence="ECO:0000269|PubMed:2002066" FT MUTAGEN 80 FT /note="L->P: 450-fold reduction in bioactivity." FT /evidence="ECO:0000269|PubMed:2002066" FT MUTAGEN 124 FT /note="L->P: 5500-fold reduction in bioactivity." FT /evidence="ECO:0000269|PubMed:2002066" FT CONFLICT 25 FT /note="T -> I (in Ref. 5; CAA29336 and 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 114 FT /note="V -> A (in Ref. 6; AAA37483)" FT /evidence="ECO:0000305" FT CONFLICT 139 FT /note="G -> S (in Ref. 5; CAA29336)" FT /evidence="ECO:0000305" FT CONFLICT 139 FT /note="G -> V (in Ref. 2; CAA26820, 3; no nucleotide entry, FT 4; CAA26192/CAA26193 and 6; AAA37483)" FT /evidence="ECO:0000305" SQ SEQUENCE 141 AA; 16091 MW; 209C7CBB4FF77349 CRC64; MWLQNLLFLG IVVYSLSAPT RSPITVTRPW KHVEAIKEAL NLLDDMPVTL NEEVEVVSNE FSFKKLTCVQ TRLKIFEQGL RGNFTKLKGA LNMTASYYQT YCPPTPETDC ETQVTTYADF IDSLKTFLTD IPFECKKPGQ K //