Reviewed, UniProtKB/Swiss-Prot P09581 (CSF1R_MOUSE)

Names and origin

Protein names

Recommended name:
    Macrophage colony-stimulating factor 1 receptor
      Short name=CSF-1-R
    EC=2.7.10.1
Alternative name(s):
    Fms proto-oncogene
    c-fms
    CD_antigen=CD115

Gene names

Name:	Csf1r
Synonyms:	Csfmr, Fms

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	977 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	Protein tyrosine-kinase transmembrane receptor for CSF1 and IL34.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Interacts with INPPL1/SHIP2 and THOC5. Ref.8 Ref.9
Subcellular location	Membrane; Single-pass type I membrane protein.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily. Contains 5 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Disease	Proto-oncogene
Domain	Immunoglobulin domain Repeat Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro transmembrane receptor protein tyrosine kinase signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay. Source: MGI receptor complex Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cytokine binding Inferred from physical interaction. Source: UniProtKB protein homodimerization activity Inferred from physical interaction. Source: UniProtKB transmembrane receptor protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 977	958	Macrophage colony-stimulating factor 1 receptor		PRO_0000016766
Regions
	Topological domain	20 – 511	492	Extracellular Potential
	Transmembrane	512 – 536	25	Potential
	Topological domain	537 – 977	441	Cytoplasmic Potential
	Domain	24 – 104	81	Ig-like C2-type 1
	Domain	107 – 197	91	Ig-like C2-type 2
	Domain	204 – 298	95	Ig-like C2-type 3
	Domain	299 – 397	99	Ig-like C2-type 4
	Domain	398 – 503	106	Ig-like C2-type 5
	Domain	580 – 913	334	Protein kinase
	Nucleotide binding	586 – 594	9	ATP By similarity
Sites
	Active site	776	1	Proton acceptor By similarity
	Binding site	614	1	ATP By similarity
Amino acid modifications
	Modified residue	554	1	Phosphotyrosine By similarity
	Modified residue	560	1	Phosphothreonine By similarity
	Modified residue	565	1	Phosphothreonine By similarity
	Modified residue	697	1	Phosphotyrosine; by autocatalysis
	Modified residue	706	1	Phosphotyrosine; by autocatalysis Ref.7
	Modified residue	714	1	Phosphoserine
	Modified residue	807	1	Phosphotyrosine; by autocatalysis Ref.7
	Glycosylation	45	1	N-linked (GlcNAc...) Potential
	Glycosylation	73	1	N-linked (GlcNAc...) Potential
	Glycosylation	302	1	N-linked (GlcNAc...) Potential
	Glycosylation	335	1	N-linked (GlcNAc...) Potential
	Glycosylation	389	1	N-linked (GlcNAc...) Potential
	Glycosylation	410	1	N-linked (GlcNAc...) Potential
	Glycosylation	449	1	N-linked (GlcNAc...) Potential
	Glycosylation	478	1	N-linked (GlcNAc...) Potential
	Glycosylation	491	1	N-linked (GlcNAc...) Ref.10
	Disulfide bond	42 ↔ 84		Potential
	Disulfide bond	127 ↔ 177		Potential
	Disulfide bond	224 ↔ 278		Potential
	Disulfide bond	417 ↔ 483		Potential
Experimental info
	Mutagenesis	544	1	Y → F: No effect on binding to THOC5. Ref.8
	Mutagenesis	614	1	K → M: Abolishes binding to THOC5. Ref.8
	Mutagenesis	706	1	Y → F: No effect on binding to THOC5. Ref.8
	Mutagenesis	721	1	Y → F: No effect on binding to THOC5. Ref.8
	Mutagenesis	807	1	Y → F: Diminishes binding to THOC5. Ref.8
	Sequence conflict	446	1	Q → E Ref.1
	Sequence conflict	553	1	R → S Ref.1
	Sequence conflict	616	1	L → I Ref.1
	Sequence conflict	744	1	A → H in CAA29666. Ref.1
	Sequence conflict	814	1	Missing in CAA29666. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P09581-1 [UniParc]. Last modified May 10, 2002. Version 3. Checksum: 7EDF8310CCF98906	FASTA	977	109,179
	10 20 30 40 50 60 MELGPPLVLL LATVWHGQGA PVIEPSGPEL VVEPGETVTL RCVSNGSVEW DGPISPYWTL 70 80 90 100 110 120 DPESPGSTLT TRNATFKNTG TYRCTELEDP MAGSTTIHLY VKDPAHSWNL LAQEVTVVEG 130 140 150 160 170 180 QEAVLPCLIT DPALKDSVSL MREGGRQVLR KTVYFFSPWR GFIIRKAKVL DSNTYVCKTM 190 200 210 220 230 240 VNGRESTSTG IWLKVNRVHP EPPQIKLEPS KLVRIRGEAA QIVCSATNAE VGFNVILKRG 250 260 270 280 290 300 DTKLEIPLNS DFQDNYYKKV RALSLNAVDF QDAGIYSCVA SNDVGTRTAT MNFQVVESAY 310 320 330 340 350 360 LNLTSEQSLL QEVSVGDSLI LTVHADAYPS IQHYNWTYLG PFFEDQRKLE FITQRAIYRY 370 380 390 400 410 420 TFKLFLNRVK ASEAGQYFLM AQNKAGWNNL TFELTLRYPP EVSVTWMPVN GSDVLFCDVS 430 440 450 460 470 480 GYPQPSVTWM ECRGHTDRCD EAQALQVWND THPEVLSQKP FDKVIIQSQL PIGTLKHNMT 490 500 510 520 530 540 YFCKTHNSVG NSSQYFRAVS LGQSKQLPDE SLFTPVVVAC MSVMSLLVLL LLLLLYKYKQ 550 560 570 580 590 600 KPKYQVRWKI IERYEGNSYT FIDPTQLPYN EKWEFPRNNL QFGKTLGAGA FGKVVEATAF 610 620 630 640 650 660 GLGKEDAVLK VAVKMLKSTA HADEKEALMS ELKIMSHLGQ HENIVNLLGA CTHGGPVLVI 670 680 690 700 710 720 TEYCCYGDLL NFLRRKAEAM LGPSLSPGQD SEGDSSYKNI HLEKKYVRRD SGFSSQGVDT 730 740 750 760 770 780 YVEMRPVSTS SSDSFFKQDL DKEASRPLEL WDLLHFSSQV AQGMAFLASK NCIHRDVAAR 790 800 810 820 830 840 NVLLTSGHVA KIGDFGLARD IMNDSNYVVK GNARLPVKWM APESIFDCVY TVQSDVWSYG 850 860 870 880 890 900 ILLWEIFSLG LNPYPGILVN NKFYKLVKDG YQMAQPVFAP KNIYSIMQSC WDLEPTRRPT 910 920 930 940 950 960 FQQICFLLQE QARLERRDQD YANLPSSGGS SGSDSGGGSS GGSSSEPEEE SSSEHLACCE 970 PGDIAQPLLQ PNNYQFC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Murine c-fms cDNA: cloning, sequence analysis and retroviral expression." Rothwell V.M., Rohrschneider L.R. Oncogene Res. 1:311-324(1987) [PubMed: 2966922] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Rothwell V.M. Submitted (SEP-1988) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Reassessment of the murine c-fms proto-oncogene sequence." de Parseval N., Bordereaux D., Gisselbrecht S., Sola B. Nucleic Acids Res. 21:750-750(1993) [PubMed: 8441691] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Liver and Urinary bladder.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[6]	"Expression of mRNA encoding the macrophage colony-stimulating factor receptor (c-fms) is controlled by a constitutive promoter and tissue-specific transcription elongation." Yue X., Favot P., Dunn T.L., Cassady A.I., Hume D.A. Mol. Cell. Biol. 13:3191-3201(1993) [PubMed: 8497248] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[7]	"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." van der Geer P., Hunter T. Mol. Cell. Biol. 10:2991-3002(1990) [PubMed: 2160591] [Abstract] Cited for: PHOSPHORYLATION AT TYR-706 AND TYR-807.
[8]	"FMIP, a novel Fms-interacting protein, affects granulocyte/macrophage differentiation." Tamura T., Mancini A., Joos H., Koch A., Hakim C., Dumanski J., Weidner K.M., Niemann H. Oncogene 18:6488-6495(1999) [PubMed: 10597251] [Abstract] Cited for: INTERACTION WITH THOC5, MUTAGENESIS OF TYR-544; LYS-614; TYR-706; TYR-721 AND TYR-807.
[9]	"SHIP2 is recruited to the cell membrane upon macrophage colony-stimulating factor (M-CSF) stimulation and regulates M-CSF-induced signaling." 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. J. Immunol. 173:6820-6830(2004) [PubMed: 15557176] [Abstract] Cited for: INTERACTION WITH INPPL1.
[10]	"Proteome-wide characterization of N-glycosylation events by diagonal chromatography." Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K. J. Proteome Res. 5:2438-2447(2006) [PubMed: 16944957] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-491, MASS SPECTROMETRY. Tissue: Plasma.
[11]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X06368 mRNA. Translation: CAA29666.1. Sequence problems.
AK004947 mRNA. Translation: BAB23691.1.
AK079247 mRNA. Translation: BAC37587.1.
AK143545 mRNA. Translation: BAE25430.1.
AK154653 mRNA. Translation: BAE32744.1.
BC043054 mRNA. Translation: AAH43054.1.
S62219 Genomic DNA. No translation available.

IPI

IPI00108003.

PIR

TVMSMD. S01880.

RefSeq

NP_001032948.2.

UniGene

Mm.22574

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EJJ	X-ray	2.40	X	20-296	[»]

ModBase

Search...

PTM databases

PhosphoSite

P09581.

Proteomic databases

PRIDE

P09581.

Genome annotation databases

Ensembl

ENSMUSG00000024621. Mus musculus. [Contig view]

GeneID

12978.

KEGG

mmu:12978.

Organism-specific databases

MGI

MGI:1339758. Csf1r.

Phylogenomic databases

HOGENOM

P09581.

HOVERGEN

P09581.

OMA

P09581. KEDAVLK.

Enzyme and pathway databases

BRENDA

2.7.10.1. 244.

Gene expression databases

Bgee

P09581.

CleanEx

MM_CSF1R.

GermOnline

ENSMUSG00000024621. Mus musculus.

Family and domain databases

InterPro

IPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001824. Recept_tyr_kinase-III_CS.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
IPR016243. TyrPK_CSF1-R.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 3 hits.

Pfam

PF00047. ig. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]

PIRSF

PIRSF000615. TyrPK_CSF1-R. 1 hit.

ProDom

PD000001. Prot_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00409. IG. 3 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

282750.

SOURCE

Search...

Entry information

Entry name

CSF1R_MOUSE

Accession

Primary (citable) accession number: P09581
Secondary accession number(s): Q3U3P1, Q9DBH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	May 10, 2002
Last modified:	June 16, 2009
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)