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P79750 (CSF11_TAKRU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Macrophage colony-stimulating factor 1 receptor 1
Short name=CSF-1-R 1
EC=2.7.10.1
Gene names
Name:csf1r1
OrganismTakifugu rubripes (Japanese pufferfish) (Fugu rubripes)
Taxonomic identifier31033 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Tetraodontiformes › Tetradontoidea › Tetraodontidae › Takifugu

Protein attributes

Sequence length975 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Tyrosine-protein kinase that acts as 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

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme 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.

Subunit structure

Monomer. Homodimer. Interacts with CSF1 By similarity.

Subcellular location

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

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.

Post-translational modification

Autophosphorylated in response to CSF1 binding By similarity. autophosphorylation, leading to its degradation By similarity.

Ubiquitinated. Becomes rapidly polyubiquitinated after autophosphorylation, leading to its degradation By similarity.

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 – 1717 Potential
Chain18 – 975958Macrophage colony-stimulating factor 1 receptor 1
PRO_0000249007

Regions

Topological domain18 – 519502Extracellular Potential
Transmembrane520 – 54021Helical; Potential
Topological domain541 – 975435Cytoplasmic Potential
Domain34 – 11380Ig-like C2-type 1
Domain125 – 20884Ig-like C2-type 2
Domain221 – 31090Ig-like C2-type 3
Domain329 – 40779Ig-like C2-type 4
Domain404 – 513110Ig-like C2-type 5
Domain584 – 918335Protein kinase
Nucleotide binding590 – 5989ATP By similarity
Region544 – 57633Regulatory juxtamembrane domain By similarity
Region800 – 82223Activation loop By similarity
Compositional bias532 – 5354Poly-Leu
Compositional bias960 – 9645Poly-Glu

Sites

Active site7821Proton acceptor By similarity
Binding site6191ATP By similarity

Amino acid modifications

Modified residue5631Phosphotyrosine; by autocatalysis By similarity
Modified residue7021Phosphotyrosine; by autocatalysis By similarity
Modified residue7261Phosphotyrosine; by autocatalysis By similarity
Modified residue8131Phosphotyrosine; by autocatalysis By similarity
Modified residue9291Phosphotyrosine; by autocatalysis By similarity
Modified residue9721Phosphotyrosine; by autocatalysis By similarity
Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation2461N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation2891N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential
Glycosylation3991N-linked (GlcNAc...) Potential
Glycosylation4201N-linked (GlcNAc...) Potential
Glycosylation4511N-linked (GlcNAc...) Potential
Disulfide bond49 ↔ 93 By similarity
Disulfide bond140 ↔ 189 By similarity
Disulfide bond236 ↔ 292 By similarity
Disulfide bond426 ↔ 495 By similarity

Sequences

Sequence LengthMass (Da)Tools
P79750 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 582E64863DF7580D

FASTA975110,914
        10         20         30         40         50         60 
MQSFLPLLMG IMASASSVEW RHPVIWFNSK VVQSSEVVVK PGTSLELKCG GDGPVNWQTR 

        70         80         90        100        110        120 
LPKHKRYMSR SPGNLRTIRV ARPTAEFTGT YKCFYSAWAQ HRHLTSSVHV YVKDPNRVFW 

       130        140        150        160        170        180 
TSSTSLRVVR KEGEDYLLPC LLTDPEATDL GLRMDNGTTV PPEMNYTVYR HRGILIRSLQ 

       190        200        210        220        230        240 
PSFNADYVCT AKVKGVEKTS KTFSINVIQK LRFPPYVFLE MDEYVRIVGE ELQIRCMTHN 

       250        260        270        280        290        300 
PNFNYNVTWN YTTKSRVTIE ERVRSSGENR LDIQSILTIS AVDLADTGNI SCIGTNEAGV 

       310        320        330        340        350        360 
NSSNTYLLVV EKPYIRLWPQ LIPKLASQGL SVEVNEGEDL ELGVMVEAYP QITDHRWHTP 

       370        380        390        400        410        420 
TSPSTSMQEH IYHARLQLKR MNAQEQGQYT FYAKSNLANG SISFHVKMYQ KPIAVVRWEN 

       430        440        450        460        470        480 
ITTLTCTSFG YPAPQIIWYQ CSGIRPTCNG NNTGLPKQNH PQALTVEVQR EEYGAVEVES 

       490        500        510        520        530        540 
VFTVGLSNHR MTVECVAFNL VGVSSDTFTV EVSDKLFTST LIGAAGVLAI FLLLLVFLLY 

       550        560        570        580        590        600 
KYKQKPRFEI RWKIIEAREG NNYTFIDPTQ LPYNEKWEFP RDKLKLGKVL GAGAFGKVVE 

       610        620        630        640        650        660 
ATAFGLGEDK DNTLRVAVKM LKANAHSDER EALMSELKIL SHLGHHQNIV NLLGACTYGG 

       670        680        690        700        710        720 
PVLVITEYCS LGDLLNFLRQ KAETFVNLVM NIPEIMENSN DYKNICNQKW YIRSDSGISS 

       730        740        750        760        770        780 
TSSSTYLEMR PSQQSHIEAS GRKSLCEDNG DWPLDIDDLL RFSLQVAQGL DFLASRNCIH 

       790        800        810        820        830        840 
RDVAARNVLL TDKRVAKICD FGLARDIMND SNYVVKGNAR LPVKWMAPES IFDCVYTVQS 

       850        860        870        880        890        900 
DVWSYGILLW EIFSLGKSPY PSMAVDSRFY KMVKRGYQMS QPDFALPEIY MIMKMCWNLE 

       910        920        930        940        950        960 
PTERPTFSMI SQMINRLLGG QDEQEKLIYR NVQPEQVAEG EACDEPKRYD PPCERSCDHE 

       970 
EEEEPLMKTN NYQFC

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References

[1]"Conserved linkage between the puffer fish (Fugu rubripes) and human genes for platelet-derived growth factor receptor and macrophage colony-stimulating factor receptor."
How G.F., Venkatesh B., Brenner S.
Genome Res. 6:1185-1191(1996) [PubMed: 8973913] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U63926 Genomic DNA. Translation: AAC60063.1.
PIRT30816.

3D structure databases

HSSPHSSP built from PDB template 1Y6A based on UniProtKB P35968.
ProteinModelPortalP79750.
SMRP79750. Positions 549-926.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGfiNOG10151.
GeneTreeENSGT00600000084056.
PhylomeDBP79750.

Family and domain databases

InterProIPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
IPR009134. Tyr_kinase_VEGFR_rcpt_N.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 5 hits.
PfamPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000615. TyrPK_CSF1-R. 1 hit.
PRINTSPR01832. VEGFRECEPTOR.
SMARTSM00409. IG. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS50835. IG_LIKE. 2 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...

Entry information

Entry nameCSF11_TAKRU
AccessionPrimary (citable) accession number: P79750
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: May 1, 1997
Last modified: December 14, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents