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Q9I8N6 · CSF1R_DANRE

Function

function

Tyrosine-protein kinase that acts as a cell-surface receptor for CSF1 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. 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. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Activates several signaling pathways in response to ligand binding (By similarity).

Catalytic activity

Activity regulation

Present in an inactive conformation in the absence of bound ligand. CSF1 binding leads to dimerization and activation by autophosphorylation on tyrosine residues (By similarity).

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site590-598ATP (UniProtKB | ChEBI)
Binding site618ATP (UniProtKB | ChEBI)
Active site781Proton acceptor

GO annotations

AspectTerm
Cellular ComponentCSF1-CSF1R complex
Cellular Componentplasma membrane
Cellular Componentreceptor complex
Molecular FunctionATP binding
Molecular Functioncytokine binding
Molecular Functiongrowth factor binding
Molecular Functionmacrophage colony-stimulating factor receptor activity
Biological Processcell surface receptor protein tyrosine kinase signaling pathway
Biological Processdevelopmental pigmentation
Biological Processimmune response in brain or nervous system
Biological Processinflammatory response
Biological Processinnate immune response
Biological Processlipid metabolic process
Biological Processmacrophage chemotaxis
Biological Processmelanocyte differentiation
Biological Processmelanocyte migration
Biological Processmicroglia development
Biological Processmicroglia differentiation
Biological Processosteoclast development
Biological Processosteoclast differentiation
Biological Processosteoclast maturation
Biological Processpigmentation
Biological Processpositive regulation of cell migration
Biological Processpositive regulation of macrophage chemotaxis
Biological Processpositive regulation of neural retina development
Biological Processprotein phosphorylation
Biological Processregulation of developmental pigmentation
Biological Processregulation of endocytosis
Biological Processregulation of MAPK cascade
Biological Processregulation of myelination
Biological Processregulation of odontogenesis
Biological Processregulation of osteoclast development
Biological Processregulation of xanthophore differentiation
Biological Processswimming behavior
Biological Processxanthophore differentiation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Macrophage colony-stimulating factor 1 receptor
  • Alternative names
    • CSF-1 receptor (CSF-1-R; CSF-1R; M-CSF-R) (EC:2.7.10.1) . EC:2.7.10.1 (UniProtKB | ENZYME | Rhea)
    • Proto-oncogene c-Fms homolog

Gene names

    • Name
      csf1r
    • Synonyms
      fms

Organism names

  • Taxonomic identifier
  • Strain
    • AB
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    Q9I8N6

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Single-pass type I membrane protein
Note: The autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain19-519Extracellular
Transmembrane520-540Helical
Topological domain541-977Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue.

Type
IDPosition(s)Description
Signal1-18
ChainPRO_000024900619-977Macrophage colony-stimulating factor 1 receptor
Disulfide bond48↔92
Glycosylation98N-linked (GlcNAc...) asparagine
Glycosylation101N-linked (GlcNAc...) asparagine
Disulfide bond138↔187
Glycosylation154N-linked (GlcNAc...) asparagine
Glycosylation163N-linked (GlcNAc...) asparagine
Disulfide bond234↔289
Glycosylation244N-linked (GlcNAc...) asparagine
Glycosylation286N-linked (GlcNAc...) asparagine
Glycosylation298N-linked (GlcNAc...) asparagine
Glycosylation361N-linked (GlcNAc...) asparagine
Glycosylation424N-linked (GlcNAc...) asparagine
Disulfide bond430↔495
Glycosylation455N-linked (GlcNAc...) asparagine
Modified residue563Phosphotyrosine; by autocatalysis
Modified residue701Phosphotyrosine; by autocatalysis
Modified residue725Phosphotyrosine; by autocatalysis
Modified residue812Phosphotyrosine; by autocatalysis
Modified residue929Phosphotyrosine; by autocatalysis
Modified residue974Phosphotyrosine; by autocatalysis

Post-translational modification

Autophosphorylated in response to CSF1 binding. autophosphorylation, leading to its degradation.
Ubiquitinated. Becomes rapidly polyubiquitinated after autophosphorylation, leading to its degradation (By similarity).

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Monomer. Homodimer. Interacts with CSF1 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain22-109Ig-like C2-type 1
Domain120-198Ig-like C2-type 2
Domain213-305Ig-like C2-type 3
Domain316-407Ig-like C2-type 4
Domain408-513Ig-like C2-type 5
Region544-576Regulatory juxtamembrane domain
Domain584-917Protein kinase
Region799-821Activation loop
Compositional bias919-938Polar residues
Region919-977Disordered
Compositional bias942-956Basic and acidic residues

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).
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).

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    977
  • Mass (Da)
    110,188
  • Last updated
    2000-10-01 v1
  • MD5 Checksum
    E6295AFB0C04E7178B9DA52E2D5894BC
MFFALLFLIGILLGQVQGWSEPRIRLSSGALAGTDVILESGSPLQLVCEGDGPVTFLPRLAKHKRYISKEVGKIRSFRVEKTTVDFTGTYKCVYMNGNDSNLSSSVHVFVRDSRVLFVSPSTSLRYVRKEGEDLLLPCLLTDPEATDFTFRMDNGSAAPYGMNITYDPRKGVLIRNVHPGFNADYICCARIGGAEKVSKIFSINIIQRLRFPPYVYLKRNEYVKLVGERLQISCTTNNPNFYYNVTWTHSSRMLPKAEEKSTMEGDRLAIESILTIPSVQLSHTGNITCTGQNEAGANSSTTQLLVVEEPYIRLSPKLSSKLTHRGLSIEVSEGDDVDLGVLIEAYPPLTSHKWETPTSHNASLPENRFFNHNDRYEALLLLKRLNFEEIGQYTLNVKNSMKSASITFDIKMYTKPVARVKWENVTTLSCRSYGYPAPSILWYQCTGIRTTCPENTTDLQPIQTQTVEFQKESFGAVGVESVLTVGPNRRMTVVCVAFNLVGQGSDTFSMEVSDQIFTSAMCGSTVAMVVLGLLLIFMIYKYKQKPRYEIRWKIIEATNGNNYTFIDPTQLPYNEKWEFPRDKLKLGKTLGAGAFGKVVEATAYGLGKEDNITRVAVKMLKASAHPDEREALMSELKILSHLGQHKNIVNLLGACTHGGPVLVITEYCCHGDLLNFLRSKAENFLNFVMTIPNFPEPMTDYKNVSTERMFVRSDSGISSTCSDHYLDMRPVTSRPTNSALDSSSECQEDSWPLDMDDLLRFSSQVAQGLDFLAAKNCIHRDVAARNVLLTNSRVAKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFECVYTVQSDVWSYGIMLWEIFSLGKSPYPNILVDSKFYKMIKCGYQMSRPDFAPPEMYTIMKMCWNLDAAERPTFSKISQMIQRMLGETSEQQDTQEYKNIPTEAEAEQQLESCDPVKHEDESFETSCDQEEEDQPLMKPNNYQFC

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8M9QKN6A0A8M9QKN6_DANREcsf1ra977

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias919-938Polar residues
Compositional bias942-956Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF240639
EMBL· GenBank· DDBJ
AAF76872.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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