CSF2_PIG
ID CSF2_PIG Reviewed; 144 AA.
AC Q29118; Q29046;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 97.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RA Foss D.L., Murtaugh M.P.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gloster S.E., Sandeman R.M., Strom A.D.G.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8595928; DOI=10.1038/icb.1995.74;
RA Inumaru S., Takamatsu H.;
RT "cDNA cloning of porcine granulocyte-macrophage colony-stimulating
RT factor.";
RL Immunol. Cell Biol. 73:474-476(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cho Y.W., Choi I.-S., Yoo H.S.;
RT "Cloning of porcine granulocyte macrophage-colony stimulating factor in
RT alveolar macrophages.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytokine that stimulates the growth and differentiation of
CC hematopoietic precursor cells from various lineages, including
CC granulocytes, macrophages, eosinophils and erythrocytes. {ECO:0000250}.
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}.
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DR EMBL; U61139; AAB03867.1; -; mRNA.
DR EMBL; U67318; AAB49939.1; -; Genomic_DNA.
DR EMBL; U67175; AAB06854.1; -; mRNA.
DR EMBL; D21074; BAA04649.1; -; mRNA.
DR EMBL; AY116504; AAM48280.1; -; mRNA.
DR RefSeq; NP_999283.1; NM_214118.2.
DR AlphaFoldDB; Q29118; -.
DR SMR; Q29118; -.
DR STRING; 9823.ENSSSCP00000020413; -.
DR PaxDb; Q29118; -.
DR PRIDE; Q29118; -.
DR Ensembl; ENSSSCT00015040085; ENSSSCP00015015867; ENSSSCG00015030234.
DR Ensembl; ENSSSCT00025059383; ENSSSCP00025025192; ENSSSCG00025043767.
DR Ensembl; ENSSSCT00065069179; ENSSSCP00065030133; ENSSSCG00065050499.
DR Ensembl; ENSSSCT00070037176; ENSSSCP00070031092; ENSSSCG00070018837.
DR GeneID; 397208; -.
DR KEGG; ssc:397208; -.
DR CTD; 1437; -.
DR eggNOG; ENOG502TDUI; Eukaryota.
DR InParanoid; Q29118; -.
DR OrthoDB; 1412355at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 2.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; ISS:UniProtKB.
DR GO; GO:0005129; F:granulocyte macrophage colony-stimulating factor receptor binding; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:AgBase.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0072651; P:interferon-tau production; IMP:AgBase.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IMP:AgBase.
DR GO; GO:1904075; P:positive regulation of trophectodermal cell proliferation; IMP:AgBase.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:AgBase.
DR GO; GO:0031929; P:TOR signaling; IMP:AgBase.
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; PTHR10059; 1.
DR Pfam; PF01109; GM_CSF; 1.
DR PRINTS; PR00693; GMCSFACTOR.
DR SMART; SM00040; CSF2; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00702; GM_CSF; 1.
PE 2: Evidence at transcript level;
KW Cytokine; Disulfide bond; Glycoprotein; Growth factor; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..144
FT /note="Granulocyte-macrophage colony-stimulating factor"
FT /id="PRO_0000005867"
FT CARBOHYD 24
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 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..113
FT /evidence="ECO:0000250"
FT DISULFID 105..138
FT /evidence="ECO:0000250"
FT CONFLICT 59
FT /note="V -> I (in Ref. 3; BAA04649)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="G -> E (in Ref. 3; BAA04649)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..143
FT /note="VK -> AQ (in Ref. 3; BAA04649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 144 AA; 16254 MW; 793DACB62CF736D0 CRC64;
MWLQNLLLLG TVVCSISAPT RPPSPVTRPW QHVDAIKEAL SLLNNSNDTA AVMNETVDVV
CEMFDPQEPT CVQTRLNLYK QGLRGSLTRL KSPLTLLAKH YEQHCPLTEE TSCETQSITF
KSFKDSLNKF LFTIPFDCWG PVKK
