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Macrophage colony-stimulating factor 1 (CSF-1) (M-CSF) (MCSF) (Lanimostim) [Cleaved into: Processed macrophage colony-stimulating factor 1]

 CSF1_HUMAN              Reviewed;         554 AA.
P09603; A8K6J5; Q13130; Q14086; Q14806; Q5VVF3; Q5VVF4; Q9UQR8;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 2.
25-OCT-2017, entry version 187.
RecName: Full=Macrophage colony-stimulating factor 1;
Short=CSF-1;
Short=M-CSF;
Short=MCSF;
AltName: Full=Lanimostim;
Contains:
RecName: Full=Processed macrophage colony-stimulating factor 1;
Flags: Precursor;
Name=CSF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-44 (ISOFORM
3), AND VARIANT SER-489.
TISSUE=Pancreatic carcinoma, and Urine;
PubMed=2996129; DOI=10.1126/science.2996129;
Kawasaki E.S., Ladner M.B., Wang A.M., van Arsdell J.N., Warren M.K.,
Coyne M.Y., Schweickart V.L., Lee M.-T., Wilson K.J., Boosman A.,
Stanley E.R., Ralph P., Mark D.F.;
"Molecular cloning of a complementary DNA encoding human macrophage-
specific colony-stimulating factor (CSF-1).";
Science 230:291-296(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
VARIANT SER-489.
TISSUE=Trophoblast, and Urine;
PubMed=3493529; DOI=10.1126/science.3493529;
Wong G.G., Temple P.A., Leary A.C., Witek-Giannotti J.S., Yang Y.C.,
Ciarletta A.B., Chung M., Murtha P., Kriz R., Kaufman R.J.,
Ferenz C.R., Sibley B.S., Turner K.J., Hewick R.M., Clark S.C.,
Yanai N., Yokota H., Yamada M., Saito M., Motoyoshi K., Takaku F.;
"Human CSF-1: molecular cloning and expression of 4-kb cDNA encoding
the human urinary protein.";
Science 235:1504-1508(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, MUTAGENESIS OF
ISOFORM 3, AND VARIANT SER-489.
TISSUE=Pancreatic carcinoma;
PubMed=2460758; DOI=10.1016/0161-5890(88)90112-5;
Cerretti D.P., Wignall J., Anderson D., Tushinski R.J., Gallis B.M.,
Stya M., Gillis S., Urdal D.L., Cosman D.;
"Human macrophage-colony stimulating factor: alternative RNA and
protein processing from a single gene.";
Mol. Immunol. 25:761-770(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PRO-408 AND
SER-489.
TISSUE=T lymphoblast;
PubMed=2660794; DOI=10.1016/0006-291X(89)92683-1;
Takahashi M., Hirato T., Takano M., Nishida T., Nagamura K.,
Kamogashira T., Nakai S., Hirai Y.;
"Amino-terminal region of human macrophage colony-stimulating factor
(M-CSF) is sufficient for its in vitro biological activity: molecular
cloning and expression of carboxyl-terminal deletion mutants of human
M-CSF.";
Biochem. Biophys. Res. Commun. 161:892-901(1989).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-489.
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-489.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-489.
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-13 AND 19-554 (ISOFORM
1), AND VARIANT SER-489.
TISSUE=Pancreatic carcinoma;
PubMed=3500041;
Ladner M.B., Martin G.A., Noble J.A., Nikoloff D.M., Tal R.,
Kawasaki E.S., White T.J.;
"Human CSF-1: gene structure and alternative splicing of mRNA
precursors.";
EMBO J. 6:2693-2698(1987).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 13-554 (ISOFORM 3), AND VARIANT SER-489.
TISSUE=Endometrium;
PubMed=1791839; DOI=10.1210/mend-5-12-1931;
Pampfer S., Tabibzadeh S., Chuan F.-C., Pollard J.W.;
"Expression of colony-stimulating factor-1 (CSF-1) messenger RNA in
human endometrial glands during the menstrual cycle: molecular cloning
of a novel transcript that predicts a cell surface form of CSF-1.";
Mol. Endocrinol. 5:1931-1938(1991).
[11]
PROTEIN SEQUENCE OF 33-185 (ISOFORM 1).
TISSUE=T lymphoblast;
PubMed=8262907;
Yamanishi K., Yasuda S., Masui Y., Nishida T., Shindo Y., Takano M.,
Ohmoto Y., Takahashi M., Adachi M.;
"The structure of recombinant human carboxy-terminal-truncated
macrophage colony-stimulating factor derived from mammalian cells.";
J. Biochem. 114:255-262(1993).
[12]
PROTEIN SEQUENCE OF 33-76.
PubMed=3498652; DOI=10.1016/0014-5793(87)80398-8;
Sakai N., Umeda T., Suzuki H., Ishimatsu Y., Shikita M.;
"Macrophage colony-stimulating factor purified from normal human
urine. Amino-terminal sequence and amino acid composition.";
FEBS Lett. 222:341-344(1987).
[13]
PROTEIN SEQUENCE OF 35-61.
PubMed=3259875; DOI=10.1016/S0006-291X(88)80441-8;
Takahashi M., Hong Y.M., Yasuda S., Takano M., Kawai K., Nakai S.,
Hirai Y.;
"Macrophage colony-stimulating factor is produced by human T
lymphoblastoid cell line, CEM-ON: identification by amino-terminal
amino acid sequence analysis.";
Biochem. Biophys. Res. Commun. 152:1401-1409(1988).
[14]
CHARACTERIZATION (ISOFORM 3).
PubMed=3039346; DOI=10.1128/MCB.7.7.2378;
Rettenmier C.W., Roussel M.F., Ashmun R.A., Ralph P., Price K.,
Sherr C.J.;
"Synthesis of membrane-bound colony-stimulating factor 1 (CSF-1) and
downmodulation of CSF-1 receptors in NIH 3T3 cells transformed by
cotransfection of the human CSF-1 and c-fms (CSF-1 receptor) genes.";
Mol. Cell. Biol. 7:2378-2387(1987).
[15]
PROTEOLYTIC PROCESSING, SUBUNIT, GLYCOSYLATION, AND SUBCELLULAR
LOCATION.
PubMed=3264877; DOI=10.1128/MCB.8.11.5026;
Rettenmier C.W., Roussel M.F.;
"Differential processing of colony-stimulating factor 1 precursors
encoded by two human cDNAs.";
Mol. Cell. Biol. 8:5026-5034(1988).
[16]
PROTEOLYTIC PROCESSING, SUBUNIT, SUBCELLULAR LOCATION, AND STRUCTURE
OF CARBOHYDRATES.
PubMed=1531650;
Suzu S., Ohtsuki T., Yanai N., Takatsu Z., Kawashima T., Takaku F.,
Nagata N., Motoyoshi K.;
"Identification of a high molecular weight macrophage colony-
stimulating factor as a glycosaminoglycan-containing species.";
J. Biol. Chem. 267:4345-4348(1992).
[17]
DISULFIDE BONDS.
PubMed=8422357; DOI=10.1021/bi00053a012;
Glocker M.O., Arbogast B., Schreurs J., Deinzer M.L.;
"Assignment of the inter- and intramolecular disulfide linkages in
recombinant human macrophage colony stimulating factor using fast atom
bombardment mass spectrometry.";
Biochemistry 32:482-488(1993).
[18]
REVIEW ON FUNCTION AND SIGNALING PATHWAYS.
PubMed=15519852; DOI=10.1016/j.tcb.2004.09.016;
Pixley F.J., Stanley E.R.;
"CSF-1 regulation of the wandering macrophage: complexity in action.";
Trends Cell Biol. 14:628-638(2004).
[19]
REVIEW ON FUNCTION IN IMMUNITY AND INFLAMMATION, AND ROLE IN DISEASE.
PubMed=16337366; DOI=10.1016/j.coi.2005.11.006;
Chitu V., Stanley E.R.;
"Colony-stimulating factor-1 in immunity and inflammation.";
Curr. Opin. Immunol. 18:39-48(2006).
[20]
REVIEW ON FUNCTION AND SIGNALING PATHWAYS.
PubMed=18687298; DOI=10.1016/j.intimp.2008.04.016;
Douglass T.G., Driggers L., Zhang J.G., Hoa N., Delgado C.,
Williams C.C., Dan Q., Sanchez R., Jeffes E.W., Wepsic H.T.,
Myers M.P., Koths K., Jadus M.R.;
"Macrophage colony stimulating factor: not just for macrophages
anymore! A gateway into complex biologies.";
Int. Immunopharmacol. 8:1354-1376(2008).
[21]
ROLE IN DISEASE.
PubMed=19934330; DOI=10.1158/0008-5472.CAN-09-1868;
Patsialou A., Wyckoff J., Wang Y., Goswami S., Stanley E.R.,
Condeelis J.S.;
"Invasion of human breast cancer cells in vivo requires both paracrine
and autocrine loops involving the colony-stimulating factor-1
receptor.";
Cancer Res. 69:9498-9506(2009).
[22]
FUNCTION IN RELEASE OF PROINFLAMMATORY CHEMOKINES.
PubMed=20829061; DOI=10.1016/j.cyto.2010.08.005;
Eda H., Zhang J., Keith R.H., Michener M., Beidler D.R., Monahan J.B.;
"Macrophage-colony stimulating factor and interleukin-34 induce
chemokines in human whole blood.";
Cytokine 52:215-220(2010).
[23]
FUNCTION, AND INTERACTION WITH CSF1R.
PubMed=20504948; DOI=10.1189/jlb.1209822;
Wei S., Nandi S., Chitu V., Yeung Y.G., Yu W., Huang M.,
Williams L.T., Lin H., Stanley E.R.;
"Functional overlap but differential expression of CSF-1 and IL-34 in
their CSF-1 receptor-mediated regulation of myeloid cells.";
J. Leukoc. Biol. 88:495-505(2010).
[24]
GLYCOSYLATION AT THR-363 AND THR-365, STRUCTURE OF CARBOHYDRATES, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 0:0-0(2011).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[27]
PHOSPHORYLATION AT THR-266.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[28]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 33-190.
PubMed=1455231; DOI=10.1126/science.1455231;
Pandit J., Bohm A., Jancarik J., Halenbeck R., Koths K., Kim S.H.;
"Three-dimensional structure of dimeric human recombinant macrophage
colony-stimulating factor.";
Science 258:1358-1362(1992).
-!- 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.
{ECO:0000269|PubMed:16337366, ECO:0000269|PubMed:19934330,
ECO:0000269|PubMed:20504948, ECO:0000269|PubMed:20829061}.
-!- SUBUNIT: Homodimer or heterodimer; disulfide-linked. Interacts
with CSF1R. {ECO:0000269|PubMed:1531650,
ECO:0000269|PubMed:20504948, ECO:0000269|PubMed:3264877,
ECO:0000269|PubMed:8422357}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-2872294, EBI-2872294;
P03228:BARF1 (xeno); NbExp=9; IntAct=EBI-2872294, EBI-16007073;
P0CW72:BARF1 (xeno); NbExp=3; IntAct=EBI-2872294, EBI-2620133;
P07333:CSF1R; NbExp=13; IntAct=EBI-2872294, EBI-2835440;
P09581:Csf1r (xeno); NbExp=2; IntAct=EBI-2872294, EBI-6305373;
Q13643:FHL3; NbExp=3; IntAct=EBI-2872294, EBI-741101;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-2872294, EBI-945833;
O43765:SGTA; NbExp=5; IntAct=EBI-2872294, EBI-347996;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1531650,
ECO:0000269|PubMed:3264877}; Single-pass type I membrane protein
{ECO:0000269|PubMed:1531650, ECO:0000269|PubMed:3264877}.
-!- SUBCELLULAR LOCATION: Processed macrophage colony-stimulating
factor 1: Secreted, extracellular space.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P09603-1; Sequence=Displayed;
Name=2;
IsoId=P09603-2; Sequence=VSP_001188;
Name=3;
IsoId=P09603-3; Sequence=VSP_001187;
-!- PTM: N- and O-glycosylated. Glycosylation and proteolytic cleavage
yield different soluble forms. One high molecular weight soluble
form is a proteoglycan containing chondroitin sulfate. O-
glycosylated with core 1 or possibly core 8 glycans. Isoform 1 is
N- and O-glycosylated. Isoform 3 is only N-glycosylated.
{ECO:0000269|PubMed:1531650, ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:3264877}.
-!- DISEASE: Note=Aberrant expression of CSF1 or CSF1R can promote
cancer cell proliferation, invasion and formation of metastases.
Overexpression of CSF1 or CSF1R is observed in a significant
percentage of breast, ovarian, prostate, and endometrial cancers.
-!- DISEASE: Note=Aberrant expression of CSF1 or CSF1R may play a role
in inflammatory diseases, such as rheumatoid arthritis,
glomerulonephritis, atherosclerosis, and allograft rejection.
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EMBL; M11296; AAB59527.1; -; Genomic_DNA.
EMBL; M11038; AAB59527.1; JOINED; Genomic_DNA.
EMBL; M11295; AAB59527.1; JOINED; Genomic_DNA.
EMBL; M37435; AAA52117.1; -; mRNA.
EMBL; M64592; AAA59572.1; -; mRNA.
EMBL; U22386; AAA64849.1; -; mRNA.
EMBL; M27087; AAA59573.1; -; mRNA.
EMBL; AK291660; BAF84349.1; -; mRNA.
EMBL; AL450468; CAH71146.1; -; Genomic_DNA.
EMBL; AL450468; CAH71147.1; -; Genomic_DNA.
EMBL; CH471122; EAW56416.1; -; Genomic_DNA.
EMBL; BC021117; AAH21117.1; -; mRNA.
EMBL; X05825; CAA29265.1; -; mRNA.
EMBL; X06106; CAA29479.1; -; Genomic_DNA.
EMBL; M76453; AAA52120.2; -; mRNA.
CCDS; CCDS30797.1; -. [P09603-3]
CCDS; CCDS816.1; -. [P09603-1]
CCDS; CCDS817.1; -. [P09603-2]
PIR; A47583; FQHUMP.
RefSeq; NP_000748.3; NM_000757.5.
RefSeq; NP_757349.1; NM_172210.2.
RefSeq; NP_757350.1; NM_172211.3.
RefSeq; NP_757351.1; NM_172212.2.
UniGene; Hs.173894; -.
PDB; 1HMC; X-ray; 2.50 A; A/B=36-181.
PDB; 3UEZ; X-ray; 3.41 A; E/F/G/H=33-181.
PDB; 3UF2; X-ray; 2.75 A; A/B/C/D/E/F/G/H/I/J=33-181.
PDB; 4ADF; X-ray; 4.40 A; G/H/I/J/K/L/S/T/U/V/W/X=33-181.
PDB; 4FA8; X-ray; 2.20 A; E/F/G=36-180.
PDB; 4WRL; X-ray; 2.80 A; B/D=33-181.
PDB; 4WRM; X-ray; 6.85 A; B=33-181.
PDB; 5LXF; X-ray; 2.00 A; A/B=33-181.
PDBsum; 1HMC; -.
PDBsum; 3UEZ; -.
PDBsum; 3UF2; -.
PDBsum; 4ADF; -.
PDBsum; 4FA8; -.
PDBsum; 4WRL; -.
PDBsum; 4WRM; -.
PDBsum; 5LXF; -.
ProteinModelPortal; P09603; -.
SMR; P09603; -.
BioGrid; 107822; 7.
DIP; DIP-41860N; -.
IntAct; P09603; 14.
MINT; MINT-196477; -.
STRING; 9606.ENSP00000327513; -.
iPTMnet; P09603; -.
PhosphoSitePlus; P09603; -.
BioMuta; CSF1; -.
DMDM; 311033367; -.
MaxQB; P09603; -.
PaxDb; P09603; -.
PeptideAtlas; P09603; -.
PRIDE; P09603; -.
DNASU; 1435; -.
Ensembl; ENST00000329608; ENSP00000327513; ENSG00000184371. [P09603-1]
Ensembl; ENST00000369801; ENSP00000358816; ENSG00000184371. [P09603-2]
Ensembl; ENST00000369802; ENSP00000358817; ENSG00000184371. [P09603-1]
Ensembl; ENST00000420111; ENSP00000407317; ENSG00000184371. [P09603-3]
GeneID; 1435; -.
KEGG; hsa:1435; -.
UCSC; uc001dyt.3; human. [P09603-1]
CTD; 1435; -.
DisGeNET; 1435; -.
EuPathDB; HostDB:ENSG00000184371.13; -.
GeneCards; CSF1; -.
HGNC; HGNC:2432; CSF1.
HPA; HPA076624; -.
MIM; 120420; gene.
neXtProt; NX_P09603; -.
OpenTargets; ENSG00000184371; -.
PharmGKB; PA26935; -.
eggNOG; ENOG410II8R; Eukaryota.
eggNOG; ENOG410Z5Q9; LUCA.
GeneTree; ENSGT00390000015805; -.
HOVERGEN; HBG005410; -.
InParanoid; P09603; -.
KO; K05453; -.
OMA; DTGHERQ; -.
OrthoDB; EOG091G0TMC; -.
PhylomeDB; P09603; -.
TreeFam; TF337718; -.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SignaLink; P09603; -.
SIGNOR; P09603; -.
ChiTaRS; CSF1; human.
EvolutionaryTrace; P09603; -.
GeneWiki; Macrophage_colony-stimulating_factor; -.
GenomeRNAi; 1435; -.
PMAP-CutDB; P09603; -.
PRO; PR:P09603; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000184371; -.
CleanEx; HS_CSF1; -.
ExpressionAtlas; P09603; baseline and differential.
Genevisible; P09603; HS.
GO; GO:1990682; C:CSF1-CSF1R complex; ISS:BHF-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005157; F:macrophage colony-stimulating factor receptor binding; ISS:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0003006; P:developmental process involved in reproduction; ISS:BHF-UCL.
GO; GO:0030097; P:hemopoiesis; NAS:UniProtKB.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0038145; P:macrophage colony-stimulating factor signaling pathway; IEA:Ensembl.
GO; GO:0030225; P:macrophage differentiation; TAS:UniProtKB.
GO; GO:0060763; P:mammary duct terminal end bud growth; IEA:Ensembl.
GO; GO:0060611; P:mammary gland fat development; IEA:Ensembl.
GO; GO:0042117; P:monocyte activation; NAS:BHF-UCL.
GO; GO:0030316; P:osteoclast differentiation; IDA:BHF-UCL.
GO; GO:0002158; P:osteoclast proliferation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:BHF-UCL.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IDA:BHF-UCL.
GO; GO:1902228; P:positive regulation of macrophage colony-stimulating factor signaling pathway; IDA:BHF-UCL.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IDA:BHF-UCL.
GO; GO:1904141; P:positive regulation of microglial cell migration; IDA:BHF-UCL.
GO; GO:0045657; P:positive regulation of monocyte differentiation; ISS:BHF-UCL.
GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; IDA:BHF-UCL.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0042488; P:positive regulation of odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:BHF-UCL.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:BHF-UCL.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0010743; P:regulation of macrophage derived foam cell differentiation; NAS:BHF-UCL.
GO; GO:0030278; P:regulation of ossification; IEA:Ensembl.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:BHF-UCL.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR008001; MCSF-1.
PANTHER; PTHR10058; PTHR10058; 1.
Pfam; PF05337; CSF-1; 1.
PIRSF; PIRSF001948; MCSF-1; 1.
SUPFAM; SSF47266; SSF47266; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Cytokine; Direct protein sequencing; Disulfide bond; Glycoprotein;
Growth factor; Immunity; Inflammatory response; Innate immunity;
Membrane; Phosphoprotein; Polymorphism; Proteoglycan;
Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 32 {ECO:0000269|PubMed:3498652}.
CHAIN 33 554 Macrophage colony-stimulating factor 1.
/FTId=PRO_0000005857.
CHAIN 33 450 Processed macrophage colony-stimulating
factor 1. {ECO:0000250|UniProtKB:Q8JZQ0}.
/FTId=PRO_0000296231.
TOPO_DOM 33 496 Lumenal. {ECO:0000255}.
TRANSMEM 497 517 Helical. {ECO:0000255}.
TOPO_DOM 518 554 Cytoplasmic. {ECO:0000255}.
REGION 406 426 O-glycosylated at one site.
MOD_RES 266 266 Phosphothreonine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 363 363 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:22171320}.
CARBOHYD 365 365 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:22171320}.
DISULFID 39 122 {ECO:0000269|PubMed:8422357}.
DISULFID 63 63 Interchain. {ECO:0000269|PubMed:8422357}.
DISULFID 80 171 {ECO:0000269|PubMed:8422357}.
DISULFID 134 178 {ECO:0000269|PubMed:8422357}.
DISULFID 189 189 Interchain. {ECO:0000269|PubMed:8422357}.
DISULFID 191 191 Interchain. {ECO:0000269|PubMed:8422357}.
VAR_SEQ 182 479 Missing (in isoform 3).
{ECO:0000303|PubMed:1791839}.
/FTId=VSP_001187.
VAR_SEQ 365 480 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_001188.
VARIANT 341 341 S -> N (in dbSNP:rs12565736).
/FTId=VAR_048810.
VARIANT 408 408 L -> P (in dbSNP:rs1058885).
{ECO:0000269|PubMed:2660794}.
/FTId=VAR_020454.
VARIANT 438 438 G -> R (in dbSNP:rs2229165).
/FTId=VAR_029320.
VARIANT 489 489 F -> S (in dbSNP:rs333971).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1791839,
ECO:0000269|PubMed:2460758,
ECO:0000269|PubMed:2660794,
ECO:0000269|PubMed:2996129,
ECO:0000269|PubMed:3493529,
ECO:0000269|PubMed:3500041,
ECO:0000269|Ref.7}.
/FTId=VAR_048811.
VARIANT 496 496 S -> F (in dbSNP:rs12721516).
/FTId=VAR_020455.
VARIANT 531 531 A -> V (in dbSNP:rs2229167).
/FTId=VAR_022146.
MUTAGEN 489 554 Missing: Produces biologically active
protein which is secreted.
{ECO:0000269|PubMed:2460758}.
CONFLICT 69 69 F -> S (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 91 91 D -> Y (in Ref. 1; AAB59527, 3; AAA59572/
AAA64849 and 10; AAA52120).
{ECO:0000305}.
CONFLICT 104 106 PNA -> ANP (in Ref. 2; AAA52117).
{ECO:0000305}.
CONFLICT 364 364 G -> A (in Ref. 2; AAA52117).
{ECO:0000305}.
CONFLICT 374 374 R -> M (in Ref. 2; AAA52117).
{ECO:0000305}.
CONFLICT 412 412 G -> A (in Ref. 2; AAA52117).
{ECO:0000305}.
CONFLICT 450 450 R -> T (in Ref. 2; AAA52117).
{ECO:0000305}.
CONFLICT 457 458 GG -> AA (in Ref. 2; AAA52117).
{ECO:0000305}.
CONFLICT 480 480 Missing (in Ref. 4; AAA59573).
{ECO:0000305}.
HELIX 37 41 {ECO:0000244|PDB:4FA8}.
HELIX 45 57 {ECO:0000244|PDB:4FA8}.
STRAND 65 70 {ECO:0000244|PDB:4FA8}.
TURN 72 74 {ECO:0000244|PDB:4FA8}.
HELIX 78 96 {ECO:0000244|PDB:4FA8}.
HELIX 104 118 {ECO:0000244|PDB:4FA8}.
STRAND 119 123 {ECO:0000244|PDB:4FA8}.
HELIX 128 130 {ECO:0000244|PDB:4FA8}.
STRAND 135 140 {ECO:0000244|PDB:4FA8}.
HELIX 142 162 {ECO:0000244|PDB:4FA8}.
HELIX 166 168 {ECO:0000244|PDB:4FA8}.
HELIX 172 176 {ECO:0000244|PDB:4FA8}.
SEQUENCE 554 AA; 60179 MW; 656B0894F9255AED CRC64;
MTAPGAAGRC PPTTWLGSLL LLVCLLASRS ITEEVSEYCS HMIGSGHLQS LQRLIDSQME
TSCQITFEFV DQEQLKDPVC YLKKAFLLVQ DIMEDTMRFR DNTPNAIAIV QLQELSLRLK
SCFTKDYEEH DKACVRTFYE TPLQLLEKVK NVFNETKNLL DKDWNIFSKN CNNSFAECSS
QDVVTKPDCN CLYPKAIPSS DPASVSPHQP LAPSMAPVAG LTWEDSEGTE GSSLLPGEQP
LHTVDPGSAK QRPPRSTCQS FEPPETPVVK DSTIGGSPQP RPSVGAFNPG MEDILDSAMG
TNWVPEEASG EASEIPVPQG TELSPSRPGG GSMQTEPARP SNFLSASSPL PASAKGQQPA
DVTGTALPRV GPVRPTGQDW NHTPQKTDHP SALLRDPPEP GSPRISSLRP QGLSNPSTLS
AQPQLSRSHS SGSVLPLGEL EGRRSTRDRR SPAEPEGGPA SEGAARPLPR FNSVPLTDTG
HERQSEGSFS PQLQESVFHL LVPSVILVLL AVGGLLFYRW RRRSHQEPQR ADSPLEQPEG
SPLTQDDRQV ELPV


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