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Reviewed, UniProtKB/Swiss-Prot P09581 (CSF1R_MOUSE)

Last modified June 16, 2009. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length977 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 977958Macrophage colony-stimulating factor 1 receptor
PRO_0000016766

Regions

Topological domain20 – 511492Extracellular Potential
Transmembrane512 – 53625 Potential
Topological domain537 – 977441Cytoplasmic Potential
Domain24 – 10481Ig-like C2-type 1
Domain107 – 19791Ig-like C2-type 2
Domain204 – 29895Ig-like C2-type 3
Domain299 – 39799Ig-like C2-type 4
Domain398 – 503106Ig-like C2-type 5
Domain580 – 913334Protein kinase
Nucleotide binding586 – 5949ATP By similarity

Sites

Active site7761Proton acceptor By similarity
Binding site6141ATP By similarity

Amino acid modifications

Modified residue5541Phosphotyrosine By similarity
Modified residue5601Phosphothreonine By similarity
Modified residue5651Phosphothreonine By similarity
Modified residue6971Phosphotyrosine; by autocatalysis
Modified residue7061Phosphotyrosine; by autocatalysis Ref.7
Modified residue7141Phosphoserine
Modified residue8071Phosphotyrosine; by autocatalysis Ref.7
Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation3891N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Glycosylation4491N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Ref.10
Disulfide bond42 ↔ 84 Potential
Disulfide bond127 ↔ 177 Potential
Disulfide bond224 ↔ 278 Potential
Disulfide bond417 ↔ 483 Potential

Experimental info

Mutagenesis5441Y → F: No effect on binding to THOC5. Ref.8
Mutagenesis6141K → M: Abolishes binding to THOC5. Ref.8
Mutagenesis7061Y → F: No effect on binding to THOC5. Ref.8
Mutagenesis7211Y → F: No effect on binding to THOC5. Ref.8
Mutagenesis8071Y → F: Diminishes binding to THOC5. Ref.8
Sequence conflict4461Q → E Ref.1
Sequence conflict5531R → S Ref.1
Sequence conflict6161L → I Ref.1
Sequence conflict7441A → H in CAA29666. Ref.1
Sequence conflict8141Missing in CAA29666. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P09581-1 [UniParc].

Last modified May 10, 2002. Version 3.
Checksum: 7EDF8310CCF98906

FASTA977109,179
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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

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.
IPIIPI00108003.
PIRTVMSMD. S01880.
RefSeqNP_001032948.2.
UniGeneMm.22574

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3EJJX-ray2.40X20-296[»]
ModBaseSearch...

PTM databases

PhosphoSiteP09581.

Proteomic databases

PRIDEP09581.

Genome annotation databases

EnsemblENSMUSG00000024621. Mus musculus. [Contig view]
GeneID12978.
KEGGmmu:12978.

Organism-specific databases

MGIMGI:1339758. Csf1r.

Phylogenomic databases

HOGENOMP09581.
HOVERGENP09581.
OMAP09581. KEDAVLK.

Enzyme and pathway databases

BRENDA2.7.10.1. 244.

Gene expression databases

BgeeP09581.
CleanExMM_CSF1R.
GermOnlineENSMUSG00000024621. Mus musculus.

Family and domain databases

InterProIPR013151. 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]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 3 hits.
PfamPF00047. ig. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PIRSFPIRSF000615. TyrPK_CSF1-R. 1 hit.
ProDomPD000001. Prot_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00409. IG. 3 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS50835. 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]
ProtoNetSearch...

Other Resources

NextBio282750.
SOURCESearch...

Entry information

Entry nameCSF1R_MOUSE
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents