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Macrophage colony-stimulating factor 1 receptor (CSF-1 receptor) (CSF-1-R) (CSF-1R) (M-CSF-R) (EC 2.7.10.1) (Proto-oncogene c-Fms) (CD antigen CD115)

 CSF1R_MOUSE             Reviewed;         977 AA.
P09581; Q3U3P1; Q9DBH9;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
10-MAY-2002, sequence version 3.
30-AUG-2017, entry version 204.
RecName: Full=Macrophage colony-stimulating factor 1 receptor;
AltName: Full=CSF-1 receptor;
Short=CSF-1-R;
Short=CSF-1R;
Short=M-CSF-R;
EC=2.7.10.1;
AltName: Full=Proto-oncogene c-Fms;
AltName: CD_antigen=CD115;
Flags: Precursor;
Name=Csf1r; Synonyms=Csfmr, Fms;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2966922;
Rothwell V.M., Rohrschneider L.R.;
"Murine c-fms cDNA: cloning, sequence analysis and retroviral
expression.";
Oncogene Res. 1:311-324(1987).
[2]
SEQUENCE REVISION.
Rothwell V.M.;
Submitted (SEP-1988) to the EMBL/GenBank/DDBJ databases.
[3]
SEQUENCE REVISION.
PubMed=8441691; DOI=10.1093/nar/21.3.750;
de Parseval N., Bordereaux D., Gisselbrecht S., Sola B.;
"Reassessment of the murine c-fms proto-oncogene sequence.";
Nucleic Acids Res. 21:750-750(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
PubMed=8497248; DOI=10.1128/MCB.13.6.3191;
Yue X., Favot P., Dunn T.L., Cassady A.I., Hume D.A.;
"Expression of mRNA encoding the macrophage colony-stimulating factor
receptor (c-fms) is controlled by a constitutive promoter and tissue-
specific transcription elongation.";
Mol. Cell. Biol. 13:3191-3201(1993).
[7]
PHOSPHORYLATION AT TYR-706 AND TYR-807.
PubMed=2160591;
van der Geer P., Hunter T.;
"Identification of tyrosine 706 in the kinase insert as the major
colony-stimulating factor 1 (CSF-1)-stimulated autophosphorylation
site in the CSF-1 receptor in a murine macrophage cell line.";
Mol. Cell. Biol. 10:2991-3002(1990).
[8]
FUNCTION IN CELL PROLIFERATION AND PHOSPHORYLATION OF PIK3R1,
INTERACTION WITH PIK3R1, PHOSPHORYLATION AT TYR-706 AND TYR-807, AND
MUTAGENESIS OF TYR-706 AND TYR-807.
PubMed=1652061;
van der Geer P., Hunter T.;
"Tyrosine 706 and 807 phosphorylation site mutants in the murine
colony-stimulating factor-1 receptor are unaffected in their ability
to bind or phosphorylate phosphatidylinositol-3 kinase but show
differential defects in their ability to induce early response gene
transcription.";
Mol. Cell. Biol. 11:4698-4709(1991).
[9]
FUNCTION AS CSF1 RECEPTOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION,
PHOSPHORYLATION AT TYR-697; TYR-706; TYR-721 AND TYR-807, MUTAGENESIS
OF LYS-614; TYR-697 AND TYR-721, AND INTERACTION WITH GRB2.
PubMed=8262059;
van der Geer P., Hunter T.;
"Mutation of Tyr697, a GRB2-binding site, and Tyr721, a PI 3-kinase
binding site, abrogates signal transduction by the murine CSF-1
receptor expressed in Rat-2 fibroblasts.";
EMBO J. 12:5161-5172(1993).
[10]
FUNCTION AS CSF1 RECEPTOR IN CELL PROLIFERATION AND IN ACTIVATION OF
AKT1; MAPK1/ERK2; MAPK3/ERK1; STAT3; STAT5A AND STAT5B, INTERACTION
WITH CBL; YES1; FYN AND SRC, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-559 AND TYR-807,
UBIQUITINATION, AND MUTAGENESIS OF TYR-559.
PubMed=8007983; DOI=10.1128/MCB.14.7.4843;
Myles G.M., Brandt C.S., Carlberg K., Rohrschneider L.R.;
"Tyrosine 569 in the c-Fms juxtamembrane domain is essential for
kinase activity and macrophage colony-stimulating factor-dependent
internalization.";
Mol. Cell. Biol. 14:4843-4854(1994).
[11]
FUNCTION IN MACROPHAGE PROLIFERATION; MACROPHAGE DIFFERENTIATION;
PHOSPHORYLATION OF PLCG2; PHOSPHORYLATION OF PIK3R1 AND
PHOSPHORYLATION OF GRB2, CATALYTIC ACTIVITY, INTERACTION WITH PIK3R1;
GRB2; PLCG2 AND FYN, AND MUTAGENESIS OF LYS-614; TYR-697; TYR-721 AND
TYR-807.
PubMed=9312046; DOI=10.1093/emboj/16.19.5880;
Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.;
"Sequential activation of phoshatidylinositol 3-kinase and
phospholipase C-gamma2 by the M-CSF receptor is necessary for
differentiation signaling.";
EMBO J. 16:5880-5893(1997).
[12]
INTERACTION WITH THOC5, AND MUTAGENESIS OF TYR-544; LYS-614; TYR-706;
TYR-721 AND TYR-807.
PubMed=10597251; DOI=10.1038/sj.onc.1203062;
Tamura T., Mancini A., Joos H., Koch A., Hakim C., Dumanski J.,
Weidner K.M., Niemann H.;
"FMIP, a novel Fms-interacting protein, affects granulocyte/macrophage
differentiation.";
Oncogene 18:6488-6495(1999).
[13]
FUNCTION.
PubMed=10958675; DOI=10.1128/MCB.20.18.6779-6798.2000;
Lee A.W., States D.J.;
"Both src-dependent and -independent mechanisms mediate
phosphatidylinositol 3-kinase regulation of colony-stimulating factor
1-activated mitogen-activated protein kinases in myeloid
progenitors.";
Mol. Cell. Biol. 20:6779-6798(2000).
[14]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=11756160; DOI=10.1182/blood.V99.1.111;
Dai X.M., Ryan G.R., Hapel A.J., Dominguez M.G., Russell R.G.,
Kapp S., Sylvestre V., Stanley E.R.;
"Targeted disruption of the mouse colony-stimulating factor 1 receptor
gene results in osteopetrosis, mononuclear phagocyte deficiency,
increased primitive progenitor cell frequencies, and reproductive
defects.";
Blood 99:111-120(2002).
[15]
INTERACTION WITH CBL, AND PHOSPHORYLATION AT TYR-974.
PubMed=11850825; DOI=10.1038/sj.onc.1205166;
Wilhelmsen K., Burkhalter S., van der Geer P.;
"C-Cbl binds the CSF-1 receptor at tyrosine 973, a novel
phosphorylation site in the receptor's carboxy-terminus.";
Oncogene 21:1079-1089(2002).
[16]
MUTAGENESIS OF TYR-559, PHOSPHORYLATION AT TYR-559, DOMAIN, AND ENZYME
REGULATION.
PubMed=15297464; DOI=10.1074/jbc.M314170200;
Rohde C.M., Schrum J., Lee A.W.;
"A juxtamembrane tyrosine in the colony stimulating factor-1 receptor
regulates ligand-induced Src association, receptor kinase function,
and down-regulation.";
J. Biol. Chem. 279:43448-43461(2004).
[17]
INTERACTION WITH INPPL1.
PubMed=15557176; DOI=10.4049/jimmunol.173.11.6820;
Wang Y., Keogh R.J., Hunter M.G., Mitchell C.A., Frey R.S., Javaid K.,
Malik A.B., Schurmans S., Tridandapani S., Marsh C.B.;
"SHIP2 is recruited to the cell membrane upon macrophage colony-
stimulating factor (M-CSF) stimulation and regulates M-CSF-induced
signaling.";
J. Immunol. 173:6820-6830(2004).
[18]
FUNCTION.
PubMed=16950670; DOI=10.1016/j.bone.2006.06.012;
Sakai H., Chen Y., Itokawa T., Yu K.P., Zhu M.L., Insogna K.;
"Activated c-Fms recruits Vav and Rac during CSF-1-induced
cytoskeletal remodeling and spreading in osteoclasts.";
Bone 39:1290-1301(2006).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-491.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[20]
PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2.
PubMed=16705167; DOI=10.1128/MCB.01932-05;
Simoncic P.D., Bourdeau A., Lee-Loy A., Rohrschneider L.R.,
Tremblay M.L., Stanley E.R., McGlade C.J.;
"T-cell protein tyrosine phosphatase (Tcptp) is a negative regulator
of colony-stimulating factor 1 signaling and macrophage
differentiation.";
Mol. Cell. Biol. 26:4149-4160(2006).
[21]
FUNCTION IN PHOSPHORYLATION OF SLA2, INTERACTION WITH SLA2 AND CBL,
SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=17353186; DOI=10.1074/jbc.M701182200;
Pakuts B., Debonneville C., Liontos L.M., Loreto M.P., McGlade C.J.;
"The Src-like adaptor protein 2 regulates colony-stimulating factor-1
receptor signaling and down-regulation.";
J. Biol. Chem. 282:17953-17963(2007).
[22]
FUNCTION, MUTAGENESIS OF TYR-559, AND PHOSPHORYLATION AT TYR-921.
PubMed=17420255; DOI=10.1074/jbc.M610938200;
Takeshita S., Faccio R., Chappel J., Zheng L., Feng X., Weber J.D.,
Teitelbaum S.L., Ross F.P.;
"c-Fms tyrosine 559 is a major mediator of M-CSF-induced proliferation
of primary macrophages.";
J. Biol. Chem. 282:18980-18990(2007).
[23]
FUNCTION.
PubMed=17420256; DOI=10.1074/jbc.M610937200;
Faccio R., Takeshita S., Colaianni G., Chappel J., Zallone A.,
Teitelbaum S.L., Ross F.P.;
"M-CSF regulates the cytoskeleton via recruitment of a multimeric
signaling complex to c-Fms Tyr-559/697/721.";
J. Biol. Chem. 282:18991-18999(2007).
[24]
FUNCTION, AND SIGNALING PATHWAY.
PubMed=17972959; DOI=10.1038/sj.leu.2404986;
Bourgin-Hierle C., Gobert-Gosse S., Therier J., Grasset M.F.,
Mouchiroud G.;
"Src-family kinases play an essential role in differentiation
signaling downstream of macrophage colony-stimulating factor receptors
mediating persistent phosphorylation of phospholipase C-gamma2 and MAP
kinases ERK1 and ERK2.";
Leukemia 22:161-169(2008).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[26]
FUNCTION IN OSTEOCLAST DIFFERENTIATION, ROLE IN DISEASE, AND ENZYME
REGULATION.
PubMed=18814279; DOI=10.1002/ijc.23903;
Hiraga T., Nakamura H.;
"Imatinib mesylate suppresses bone metastases of breast cancer by
inhibiting osteoclasts through the blockade of c-Fms signals.";
Int. J. Cancer 124:215-222(2009).
[27]
ROLE IN DISEASE.
PubMed=20181277; DOI=10.1186/ar2940;
Paniagua R.T., Chang A., Mariano M.M., Stein E.A., Wang Q.,
Lindstrom T.M., Sharpe O., Roscow C., Ho P.P., Lee D.M.,
Robinson W.H.;
"c-Fms-mediated differentiation and priming of monocyte lineage cells
play a central role in autoimmune arthritis.";
Arthritis Res. Ther. 12:R32-R32(2010).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-711, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[29]
FUNCTION AS IL34 AND CSF1 RECEPTOR, FUNCTION IN ACTIVATION OF
MAPK1/ERK2 AND MAPK3/ERK1, PHOSPHORYLATION AT TYR-559; TYR-807 AND
TYR-721, AUTOPHOSPHORYLATION, AND TISSUE SPECIFICITY.
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).
[30]
FUNCTION.
PubMed=21727904; DOI=10.1038/icb.2011.58;
Lenzo J.C., Turner A.L., Cook A.D., Vlahos R., Anderson G.P.,
Reynolds E.C., Hamilton J.A.;
"Control of macrophage lineage populations by CSF-1 receptor and GM-
CSF in homeostasis and inflammation.";
Immunol. Cell Biol. 90:429-440(2012).
[31]
UBIQUITINATION.
PubMed=21041311; DOI=10.1074/jbc.M110.166702;
Xiong Y., Song D., Cai Y., Yu W., Yeung Y.G., Stanley E.R.;
"A CSF-1 receptor phosphotyrosine 559 signaling pathway regulates
receptor ubiquitination and tyrosine phosphorylation.";
J. Biol. Chem. 286:952-960(2011).
[32]
FUNCTION IN REGULATION OF CELL MOTILITY; CELL SHAPE; ACTIN
CYTOSKELETON REORGANIZATION; PHOSPHORYLATION OF AKT1 AND REGULATION OF
PHOSPHATIDYLINOSITOL METABOLISM, INTERACTION WITH PIK3R1 AND PLCG2,
PHOSPHORYLATION AT TYR-706 AND TYR-721, AND MUTAGENESIS OF TYR-721.
PubMed=21610095; DOI=10.1242/jcs.075309;
Sampaio N.G., Yu W., Cox D., Wyckoff J., Condeelis J., Stanley E.R.,
Pixley F.J.;
"Phosphorylation of CSF-1R Y721 mediates its association with PI3K to
regulate macrophage motility and enhancement of tumor cell invasion.";
J. Cell Sci. 124:2021-2031(2011).
[33]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-296 IN COMPLEX WITH CSF1,
GLYCOSYLATION AT ASN-45 AND ASN-73, SUBUNIT, AND DISULFIDE BONDS.
PubMed=19017797; DOI=10.1073/pnas.0807762105;
Chen X., Liu H., Focia P.J., Shim A.H., He X.;
"Structure of macrophage colony stimulating factor bound to FMS:
diverse signaling assemblies of class III receptor tyrosine kinases.";
Proc. Natl. Acad. Sci. U.S.A. 105:18267-18272(2008).
-!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface
receptor for CSF1 and IL34 and 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 in response to IL34 and CSF1, 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 and tooth
development. Required for normal male and female fertility, and
for normal development of milk ducts and acinar structures in the
mammary gland during pregnancy. Promotes reorganization of the
actin cytoskeleton, regulates formation of membrane ruffles, cell
adhesion and cell migration, and promotes cancer cell invasion.
Activates several signaling pathways in response to ligand
binding. Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL.
Activation of PLCG2 leads to the production of the cellular
signaling molecules diacylglycerol and inositol 1,4,5-
trisphosphate, that then lead to the activation of protein kinase
C family members, especially PRKCD. Phosphorylation of PIK3R1, the
regulatory subunit of phosphatidylinositol 3-kinase, leads to
activation of the AKT1 signaling pathway. Activated CSF1R also
mediates activation of the MAP kinases MAPK1/ERK2 and/or
MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1.
Activated CSF1R transmits signals both via proteins that directly
interact with phosphorylated tyrosine residues in its
intracellular domain, or via adapter proteins, such as GRB2.
Promotes activation of STAT family members STAT3, STAT5A and/or
STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP-
1. Receptor signaling is down-regulated by protein phosphatases,
such as INPP5D/SHIP-1, that dephosphorylate the receptor and its
downstream effectors, and by rapid internalization of the
activated receptor. {ECO:0000269|PubMed:10958675,
ECO:0000269|PubMed:11756160, ECO:0000269|PubMed:1652061,
ECO:0000269|PubMed:16950670, ECO:0000269|PubMed:17353186,
ECO:0000269|PubMed:17420255, ECO:0000269|PubMed:17420256,
ECO:0000269|PubMed:17972959, ECO:0000269|PubMed:18814279,
ECO:0000269|PubMed:20181277, ECO:0000269|PubMed:20504948,
ECO:0000269|PubMed:21610095, ECO:0000269|PubMed:21727904,
ECO:0000269|PubMed:8007983, ECO:0000269|PubMed:8262059,
ECO:0000269|PubMed:9312046}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:8007983,
ECO:0000269|PubMed:8262059, ECO:0000269|PubMed:9312046}.
-!- ENZYME REGULATION: Present in an inactive conformation in the
absence of bound ligand. CSF1 or IL34 binding leads to
dimerization and activation by autophosphorylation on tyrosine
residues. Inhibited by imatinib/STI-571 (Gleevec), dasatinib,
sunitinib/SU11248, lestaurtinib/CEP-701, midostaurin/PKC-412,
Ki20227, linifanib/ABT-869, Axitinib/AG013736, sorafenib/BAY 43-
9006 and GW2580. {ECO:0000269|PubMed:15297464,
ECO:0000269|PubMed:18814279}.
-!- SUBUNIT: Monomer. Homodimer. Interacts with CSF1 and IL34.
Interaction with dimeric CSF1 or IL34 leads to receptor
homodimerization. Interacts with INPPL1/SHIP2 and THOC5. Interacts
(tyrosine phosphorylated) with PLCG2 (via SH2 domain). Interacts
(tyrosine phosphorylated) with PIK3R1 (via SH2 domain). Interacts
(tyrosine phosphorylated) with FYN, YES1 and SRC (via SH2 domain).
Interacts (tyrosine phosphorylated) with CBL, GRB2 and SLA2.
{ECO:0000269|PubMed:10597251, ECO:0000269|PubMed:11850825,
ECO:0000269|PubMed:15557176, ECO:0000269|PubMed:1652061,
ECO:0000269|PubMed:17353186, ECO:0000269|PubMed:19017797,
ECO:0000269|PubMed:21610095, ECO:0000269|PubMed:8007983,
ECO:0000269|PubMed:8262059, ECO:0000269|PubMed:9312046}.
-!- INTERACTION:
P07141:Csf1; NbExp=4; IntAct=EBI-6305373, EBI-777188;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17353186,
ECO:0000269|PubMed:8007983}; Single-pass type I membrane protein
{ECO:0000269|PubMed:17353186, ECO:0000269|PubMed:8007983}.
Note=The autophosphorylated receptor is ubiquitinated and
internalized, leading to its degradation.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:20504948}.
-!- DOMAIN: The juxtamembrane domain functions as autoinhibitory
region. Phosphorylation of tyrosine residues in this region leads
to a conformation change and activation of the kinase (By
similarity). {ECO:0000250}.
-!- DOMAIN: The activation loop plays an important role in the
regulation of kinase activity. Phosphorylation of tyrosine
residues in this region leads to a conformation change and
activation of the kinase (By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated in response to CSF1 or IL34 binding.
Phosphorylation at Tyr-559 is important for normal down-regulation
of signaling by ubiquitination, internalization and degradation.
Phosphorylation at Tyr-559 and Tyr-807 is important for
interaction with SRC family members, including FYN, YES1 and SRC,
and for subsequent activation of these protein kinases.
Phosphorylation at Tyr-697 and Tyr-921 is important for
interaction with GRB2. Phosphorylation at Tyr-721 is important for
interaction with PIK3R1. Phosphorylation at Tyr-721 and Tyr-807 is
important for interaction with PLCG2. Phosphorylation at Tyr-974
is important for interaction with CBL. Dephosphorylation by PTPN2
negatively regulates downstream signaling and macrophage
differentiation. {ECO:0000269|PubMed:11850825,
ECO:0000269|PubMed:15297464, ECO:0000269|PubMed:1652061,
ECO:0000269|PubMed:17420255, ECO:0000269|PubMed:20504948,
ECO:0000269|PubMed:2160591, ECO:0000269|PubMed:21610095,
ECO:0000269|PubMed:8007983, ECO:0000269|PubMed:8262059}.
-!- PTM: Ubiquitinated. Becomes rapidly polyubiquitinated after
autophosphorylation, leading to its degradation.
-!- DISRUPTION PHENOTYPE: Mice are born at slightly less than the
expected Mendelian rate, and the number of surviving mice is
significantly reduced after three weeks. Mice are considerably
smaller than wild-type littermates and suffer from general
skeletal deformities with shortened limbs, increased bone density,
and decreased volume of femoral bone marrow. Mice have decreased
numbers of circulating monocytes and lymphocytes, decreased
numbers of tissue macrophages, paired with an increase in the
number of circulating granulocytes. In addition, mice are deaf and
have reduced male and female fertility. In females, the duration
of the diestrous period is increased, and in pregnant females the
lactating mammary gland fails to develop normally. Males mate less
frequently and give rise to fewer pregnant females.
{ECO:0000269|PubMed:11756160}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X06368; CAA29666.1; -; mRNA.
EMBL; AK004947; BAB23691.1; -; mRNA.
EMBL; AK079247; BAC37587.1; -; mRNA.
EMBL; AK143545; BAE25430.1; -; mRNA.
EMBL; AK154653; BAE32744.1; -; mRNA.
EMBL; BC043054; AAH43054.1; -; mRNA.
EMBL; S62219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS29280.1; -.
PIR; S01880; TVMSMD.
RefSeq; NP_001032948.2; NM_001037859.2.
RefSeq; XP_006525647.1; XM_006525584.1.
RefSeq; XP_006525648.1; XM_006525585.3.
RefSeq; XP_006525649.1; XM_006525586.3.
RefSeq; XP_017173299.1; XM_017317810.1.
UniGene; Mm.22574; -.
PDB; 3EJJ; X-ray; 2.40 A; X=20-296.
PDB; 4EXP; X-ray; 2.80 A; X=20-298.
PDBsum; 3EJJ; -.
PDBsum; 4EXP; -.
ProteinModelPortal; P09581; -.
SMR; P09581; -.
BioGrid; 198928; 15.
DIP; DIP-46415N; -.
IntAct; P09581; 5.
MINT; MINT-8013693; -.
STRING; 10090.ENSMUSP00000025523; -.
BindingDB; P09581; -.
ChEMBL; CHEMBL5570; -.
iPTMnet; P09581; -.
PhosphoSitePlus; P09581; -.
PaxDb; P09581; -.
PeptideAtlas; P09581; -.
PRIDE; P09581; -.
Ensembl; ENSMUST00000025523; ENSMUSP00000025523; ENSMUSG00000024621.
Ensembl; ENSMUST00000115268; ENSMUSP00000110923; ENSMUSG00000024621.
GeneID; 12978; -.
KEGG; mmu:12978; -.
UCSC; uc008fbn.1; mouse.
CTD; 1436; -.
MGI; MGI:1339758; Csf1r.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000112008; -.
HOVERGEN; HBG004335; -.
InParanoid; P09581; -.
KO; K05090; -.
OMA; WKIIESY; -.
OrthoDB; EOG091G01TL; -.
PhylomeDB; P09581; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-449836; Other interleukin signaling.
ChiTaRS; Csf1r; mouse.
EvolutionaryTrace; P09581; -.
PRO; PR:P09581; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024621; -.
CleanEx; MM_CSF1R; -.
ExpressionAtlas; P09581; baseline and differential.
Genevisible; P09581; MM.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:1990682; C:CSF1-CSF1R complex; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019955; F:cytokine binding; IDA:UniProtKB.
GO; GO:0005011; F:macrophage colony-stimulating factor receptor activity; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:MGI.
GO; GO:0007411; P:axon guidance; IMP:ParkinsonsUK-UCL.
GO; GO:0008283; P:cell proliferation; ISO:MGI.
GO; GO:0045217; P:cell-cell junction maintenance; ISO:MGI.
GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:UniProtKB.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IMP:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
GO; GO:0021879; P:forebrain neuron differentiation; IMP:ParkinsonsUK-UCL.
GO; GO:0030097; P:hemopoiesis; ISO:MGI.
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; IDA:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:ParkinsonsUK-UCL.
GO; GO:0021772; P:olfactory bulb development; IMP:ParkinsonsUK-UCL.
GO; GO:0030316; P:osteoclast differentiation; IMP:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:2000147; P:positive regulation of cell motility; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0090197; P:positive regulation of chemokine secretion; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:MGI.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0045124; P:regulation of bone resorption; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0031529; P:ruffle organization; IMP:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:BHF-UCL.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR030658; CSF-1_receptor.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
PANTHER; PTHR24416:SF410; PTHR24416:SF410; 1.
Pfam; PF00047; ig; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500947; CSF-1_receptor; 1.
SMART; SM00409; IG; 5.
SMART; SM00408; IGc2; 2.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 5.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 4.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
Inflammatory response; Innate immunity; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 977 Macrophage colony-stimulating factor 1
receptor.
/FTId=PRO_0000016766.
TOPO_DOM 20 515 Extracellular. {ECO:0000255}.
TRANSMEM 516 536 Helical. {ECO:0000255}.
TOPO_DOM 537 977 Cytoplasmic. {ECO:0000255}.
DOMAIN 24 104 Ig-like C2-type 1.
DOMAIN 107 197 Ig-like C2-type 2.
DOMAIN 204 298 Ig-like C2-type 3.
DOMAIN 299 397 Ig-like C2-type 4.
DOMAIN 398 503 Ig-like C2-type 5.
DOMAIN 580 913 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 586 594 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 540 572 Regulatory juxtamembrane domain.
{ECO:0000250}.
REGION 794 816 Activation loop. {ECO:0000250}.
ACT_SITE 776 776 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 614 614 ATP. {ECO:0000305}.
MOD_RES 544 544 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P07333}.
MOD_RES 559 559 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15297464,
ECO:0000269|PubMed:20504948,
ECO:0000269|PubMed:8007983}.
MOD_RES 697 697 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:8262059}.
MOD_RES 706 706 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:1652061,
ECO:0000269|PubMed:2160591,
ECO:0000269|PubMed:21610095,
ECO:0000269|PubMed:8262059}.
MOD_RES 711 711 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 721 721 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:20504948,
ECO:0000269|PubMed:21610095,
ECO:0000269|PubMed:8262059}.
MOD_RES 807 807 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:1652061,
ECO:0000269|PubMed:20504948,
ECO:0000269|PubMed:2160591,
ECO:0000269|PubMed:8007983,
ECO:0000269|PubMed:8262059}.
MOD_RES 921 921 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:17420255}.
MOD_RES 974 974 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11850825}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19017797}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19017797}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 449 449 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
DISULFID 42 84 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:19017797}.
DISULFID 127 177 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:19017797}.
DISULFID 224 278 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:19017797}.
DISULFID 417 483 {ECO:0000255|PROSITE-ProRule:PRU00114}.
MUTAGEN 544 544 Y->F: No effect on binding to THOC5.
{ECO:0000269|PubMed:10597251}.
MUTAGEN 559 559 Y->F: Reduced interaction with CBL.
Prolonged signaling, due to reduced
internalization and degradation. Reduced
interaction with FYN. Promotes cell
proliferation. Reduced
autophosphorylation at Tyr-807.
{ECO:0000269|PubMed:15297464,
ECO:0000269|PubMed:17420255,
ECO:0000269|PubMed:8007983}.
MUTAGEN 614 614 K->A: Loss of kinase activity.
{ECO:0000269|PubMed:10597251,
ECO:0000269|PubMed:8262059,
ECO:0000269|PubMed:9312046}.
MUTAGEN 614 614 K->M: Loss of kinase activity. Abolishes
binding to THOC5.
{ECO:0000269|PubMed:10597251,
ECO:0000269|PubMed:8262059,
ECO:0000269|PubMed:9312046}.
MUTAGEN 697 697 Y->F: Abolishes interaction with GRB2.
{ECO:0000269|PubMed:8262059,
ECO:0000269|PubMed:9312046}.
MUTAGEN 706 706 Y->F: No effect on binding to THOC5.
Slightly reduced enhancement of cell
proliferation.
{ECO:0000269|PubMed:10597251,
ECO:0000269|PubMed:1652061}.
MUTAGEN 706 706 Y->G: Slightly impaired signaling.
{ECO:0000269|PubMed:10597251,
ECO:0000269|PubMed:1652061}.
MUTAGEN 721 721 Y->F: Abolishes interaction with PIK3R1.
Strongly reduced phosphorylation of
PLCG2. No effect on binding to THOC5.
{ECO:0000269|PubMed:10597251,
ECO:0000269|PubMed:21610095,
ECO:0000269|PubMed:8262059,
ECO:0000269|PubMed:9312046}.
MUTAGEN 807 807 Y->F: Reduced kinase activity. Strongly
reduced phosphorylation of PLCG2.
Diminishes binding to THOC5.
{ECO:0000269|PubMed:10597251,
ECO:0000269|PubMed:1652061,
ECO:0000269|PubMed:9312046}.
MUTAGEN 807 807 Y->G: May alter protein folding or
stability. Loss of kinase activity. No
effect on interaction with PIK3R1.
{ECO:0000269|PubMed:10597251,
ECO:0000269|PubMed:1652061,
ECO:0000269|PubMed:9312046}.
CONFLICT 57 57 Y -> I (in Ref. 1; CAA29666).
{ECO:0000305}.
CONFLICT 72 72 R -> S (in Ref. 1; CAA29666).
{ECO:0000305}.
CONFLICT 162 162 F -> S (in Ref. 1; CAA29666).
{ECO:0000305}.
CONFLICT 446 447 QV -> HL (in Ref. 1; CAA29666).
{ECO:0000305}.
CONFLICT 474 474 T -> P (in Ref. 1; CAA29666).
{ECO:0000305}.
CONFLICT 660 660 I -> Y (in Ref. 1; CAA29666).
{ECO:0000305}.
CONFLICT 669 669 L -> H (in Ref. 1; CAA29666).
{ECO:0000305}.
CONFLICT 744 744 A -> H (in Ref. 1; CAA29666).
{ECO:0000305}.
CONFLICT 814 814 Missing (in Ref. 1; CAA29666).
{ECO:0000305}.
CONFLICT 830 830 Y -> I (in Ref. 1; CAA29666).
{ECO:0000305}.
CONFLICT 858 858 L -> H (in Ref. 1; CAA29666).
{ECO:0000305}.
STRAND 22 25 {ECO:0000244|PDB:3EJJ}.
STRAND 27 32 {ECO:0000244|PDB:3EJJ}.
STRAND 38 43 {ECO:0000244|PDB:3EJJ}.
STRAND 49 51 {ECO:0000244|PDB:3EJJ}.
STRAND 55 60 {ECO:0000244|PDB:3EJJ}.
STRAND 64 66 {ECO:0000244|PDB:4EXP}.
STRAND 68 73 {ECO:0000244|PDB:3EJJ}.
HELIX 76 78 {ECO:0000244|PDB:3EJJ}.
STRAND 80 85 {ECO:0000244|PDB:3EJJ}.
STRAND 95 101 {ECO:0000244|PDB:3EJJ}.
STRAND 107 111 {ECO:0000244|PDB:3EJJ}.
STRAND 113 118 {ECO:0000244|PDB:3EJJ}.
STRAND 123 125 {ECO:0000244|PDB:3EJJ}.
STRAND 127 130 {ECO:0000244|PDB:3EJJ}.
HELIX 132 136 {ECO:0000244|PDB:3EJJ}.
STRAND 137 142 {ECO:0000244|PDB:3EJJ}.
HELIX 143 145 {ECO:0000244|PDB:3EJJ}.
STRAND 154 157 {ECO:0000244|PDB:3EJJ}.
TURN 158 160 {ECO:0000244|PDB:3EJJ}.
STRAND 161 166 {ECO:0000244|PDB:3EJJ}.
HELIX 169 171 {ECO:0000244|PDB:3EJJ}.
STRAND 173 181 {ECO:0000244|PDB:3EJJ}.
STRAND 184 187 {ECO:0000244|PDB:3EJJ}.
STRAND 191 198 {ECO:0000244|PDB:3EJJ}.
STRAND 204 213 {ECO:0000244|PDB:3EJJ}.
STRAND 216 218 {ECO:0000244|PDB:3EJJ}.
STRAND 220 231 {ECO:0000244|PDB:3EJJ}.
STRAND 234 239 {ECO:0000244|PDB:3EJJ}.
STRAND 248 252 {ECO:0000244|PDB:3EJJ}.
STRAND 254 267 {ECO:0000244|PDB:3EJJ}.
STRAND 270 272 {ECO:0000244|PDB:3EJJ}.
STRAND 274 281 {ECO:0000244|PDB:3EJJ}.
STRAND 286 294 {ECO:0000244|PDB:3EJJ}.
SEQUENCE 977 AA; 109179 MW; 7EDF8310CCF98906 CRC64;
MELGPPLVLL LATVWHGQGA PVIEPSGPEL VVEPGETVTL RCVSNGSVEW DGPISPYWTL
DPESPGSTLT TRNATFKNTG TYRCTELEDP MAGSTTIHLY VKDPAHSWNL LAQEVTVVEG
QEAVLPCLIT DPALKDSVSL MREGGRQVLR KTVYFFSPWR GFIIRKAKVL DSNTYVCKTM
VNGRESTSTG IWLKVNRVHP EPPQIKLEPS KLVRIRGEAA QIVCSATNAE VGFNVILKRG
DTKLEIPLNS DFQDNYYKKV RALSLNAVDF QDAGIYSCVA SNDVGTRTAT MNFQVVESAY
LNLTSEQSLL QEVSVGDSLI LTVHADAYPS IQHYNWTYLG PFFEDQRKLE FITQRAIYRY
TFKLFLNRVK ASEAGQYFLM AQNKAGWNNL TFELTLRYPP EVSVTWMPVN GSDVLFCDVS
GYPQPSVTWM ECRGHTDRCD EAQALQVWND THPEVLSQKP FDKVIIQSQL PIGTLKHNMT
YFCKTHNSVG NSSQYFRAVS LGQSKQLPDE SLFTPVVVAC MSVMSLLVLL LLLLLYKYKQ
KPKYQVRWKI IERYEGNSYT FIDPTQLPYN EKWEFPRNNL QFGKTLGAGA FGKVVEATAF
GLGKEDAVLK VAVKMLKSTA HADEKEALMS ELKIMSHLGQ HENIVNLLGA CTHGGPVLVI
TEYCCYGDLL NFLRRKAEAM LGPSLSPGQD SEGDSSYKNI HLEKKYVRRD SGFSSQGVDT
YVEMRPVSTS SSDSFFKQDL DKEASRPLEL WDLLHFSSQV AQGMAFLASK NCIHRDVAAR
NVLLTSGHVA KIGDFGLARD IMNDSNYVVK GNARLPVKWM APESIFDCVY TVQSDVWSYG
ILLWEIFSLG LNPYPGILVN NKFYKLVKDG YQMAQPVFAP KNIYSIMQSC WDLEPTRRPT
FQQICFLLQE QARLERRDQD YANLPSSGGS SGSDSGGGSS GGSSSEPEEE SSSEHLACCE
PGDIAQPLLQ PNNYQFC


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