CSF11_TAKRU
ID CSF11_TAKRU Reviewed; 975 AA.
AC P79750;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Macrophage colony-stimulating factor 1 receptor 1;
DE Short=CSF-1-R 1;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=csf1r1;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8973913; DOI=10.1101/gr.6.12.1185;
RA How G.F., Venkatesh B., Brenner S.;
RT "Conserved linkage between the puffer fish (Fugu rubripes) and human genes
RT for platelet-derived growth factor receptor and macrophage colony-
RT stimulating factor receptor.";
RL Genome Res. 6:1185-1191(1996).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC for CSF1 and plays an essential role in the regulation of survival,
CC proliferation and differentiation of hematopoietic precursor cells,
CC especially mononuclear phagocytes, such as macrophages and monocytes.
CC Plays an important role in innate immunity and in inflammatory
CC processes. Plays an important role in the regulation of osteoclast
CC proliferation and differentiation, the regulation of bone resorption,
CC and is required for normal bone development. Promotes reorganization of
CC the actin cytoskeleton, regulates formation of membrane ruffles, cell
CC adhesion and cell migration. Activates several signaling pathways in
CC response to ligand binding (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. CSF1 binding leads to dimerization and activation by
CC autophosphorylation on tyrosine residues (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Homodimer. Interacts with CSF1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Note=The autophosphorylated receptor is
CC ubiquitinated and internalized, leading to its degradation.
CC {ECO:0000250}.
CC -!- DOMAIN: The juxtamembrane domain functions as autoinhibitory region.
CC Phosphorylation of tyrosine residues in this region leads to a
CC conformation change and activation of the kinase (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The activation loop plays an important role in the regulation
CC of kinase activity. Phosphorylation of tyrosine residues in this region
CC leads to a conformation change and activation of the kinase (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated in response to CSF1 binding.
CC autophosphorylation, leading to its degradation. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Becomes rapidly polyubiquitinated after
CC autophosphorylation, leading to its degradation (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; U63926; AAC60063.1; -; Genomic_DNA.
DR PIR; T30816; T30816.
DR AlphaFoldDB; P79750; -.
DR SMR; P79750; -.
DR STRING; 31033.ENSTRUP00000016089; -.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; P79750; -.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019955; F:cytokine binding; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR030658; CSF-1_receptor.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500947; CSF-1_receptor; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Inflammatory response; Innate immunity; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..975
FT /note="Macrophage colony-stimulating factor 1 receptor 1"
FT /id="PRO_0000249007"
FT TOPO_DOM 18..519
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..975
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..113
FT /note="Ig-like C2-type 1"
FT DOMAIN 125..208
FT /note="Ig-like C2-type 2"
FT DOMAIN 221..310
FT /note="Ig-like C2-type 3"
FT DOMAIN 329..407
FT /note="Ig-like C2-type 4"
FT DOMAIN 404..513
FT /note="Ig-like C2-type 5"
FT DOMAIN 584..918
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 544..576
FT /note="Regulatory juxtamembrane domain"
FT /evidence="ECO:0000250"
FT REGION 800..822
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 939..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 782
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 590..598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 563
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 702
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 726
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 813
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 929
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 972
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 140..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 236..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 426..495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 975 AA; 110914 MW; 582E64863DF7580D CRC64;
MQSFLPLLMG IMASASSVEW RHPVIWFNSK VVQSSEVVVK PGTSLELKCG GDGPVNWQTR
LPKHKRYMSR SPGNLRTIRV ARPTAEFTGT YKCFYSAWAQ HRHLTSSVHV YVKDPNRVFW
TSSTSLRVVR KEGEDYLLPC LLTDPEATDL GLRMDNGTTV PPEMNYTVYR HRGILIRSLQ
PSFNADYVCT AKVKGVEKTS KTFSINVIQK LRFPPYVFLE MDEYVRIVGE ELQIRCMTHN
PNFNYNVTWN YTTKSRVTIE ERVRSSGENR LDIQSILTIS AVDLADTGNI SCIGTNEAGV
NSSNTYLLVV EKPYIRLWPQ LIPKLASQGL SVEVNEGEDL ELGVMVEAYP QITDHRWHTP
TSPSTSMQEH IYHARLQLKR MNAQEQGQYT FYAKSNLANG SISFHVKMYQ KPIAVVRWEN
ITTLTCTSFG YPAPQIIWYQ CSGIRPTCNG NNTGLPKQNH PQALTVEVQR EEYGAVEVES
VFTVGLSNHR MTVECVAFNL VGVSSDTFTV EVSDKLFTST LIGAAGVLAI FLLLLVFLLY
KYKQKPRFEI RWKIIEAREG NNYTFIDPTQ LPYNEKWEFP RDKLKLGKVL GAGAFGKVVE
ATAFGLGEDK DNTLRVAVKM LKANAHSDER EALMSELKIL SHLGHHQNIV NLLGACTYGG
PVLVITEYCS LGDLLNFLRQ KAETFVNLVM NIPEIMENSN DYKNICNQKW YIRSDSGISS
TSSSTYLEMR PSQQSHIEAS GRKSLCEDNG DWPLDIDDLL RFSLQVAQGL DFLASRNCIH
RDVAARNVLL TDKRVAKICD FGLARDIMND SNYVVKGNAR LPVKWMAPES IFDCVYTVQS
DVWSYGILLW EIFSLGKSPY PSMAVDSRFY KMVKRGYQMS QPDFALPEIY MIMKMCWNLE
PTERPTFSMI SQMINRLLGG QDEQEKLIYR NVQPEQVAEG EACDEPKRYD PPCERSCDHE
EEEEPLMKTN NYQFC
