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Database: UniProt
Entry: Q9I8N6
LinkDB: Q9I8N6
Original site: Q9I8N6 
ID   CSF1R_DANRE             Reviewed;         977 AA.
AC   Q9I8N6;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   01-OCT-2014, entry version 100.
DE   RecName: Full=Macrophage colony-stimulating factor 1 receptor;
DE   AltName: Full=CSF-1 receptor;
DE            Short=CSF-1-R;
DE            Short=CSF-1R;
DE            Short=M-CSF-R;
DE            EC=2.7.10.1;
DE   AltName: Full=Proto-oncogene c-Fms homolog;
DE   Flags: Precursor;
GN   Name=csf1r; Synonyms=fms;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=AB;
RX   PubMed=10862741;
RA   Parichy D.M., Ransom D.G., Paw B., Zon L.I., Johnson S.L.;
RT   "An orthologue of the kit-related gene fms is required for development
RT   of neural crest-derived xanthophores and a subpopulation of adult
RT   melanocytes in the zebrafish, Danio rerio.";
RL   Development 127:3031-3044(2000).
CC   -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface
CC       receptor for CSF1 and plays an essential role in the regulation of
CC       survival, proliferation and differentiation of hematopoietic
CC       precursor cells, especially mononuclear phagocytes, such as
CC       macrophages and monocytes. Plays an important role in innate
CC       immunity and in inflammatory processes. Plays an important role in
CC       the regulation of osteoclast proliferation and differentiation,
CC       the regulation of bone resorption, and is required for normal bone
CC       development. Promotes reorganization of the actin cytoskeleton,
CC       regulates formation of membrane ruffles, cell adhesion and cell
CC       migration. Activates several signaling pathways in response to
CC       ligand binding (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
CC       ProRule:PRU10028}.
CC   -!- ENZYME REGULATION: Present in an inactive conformation in the
CC       absence of bound ligand. CSF1 binding leads to dimerization and
CC       activation by autophosphorylation on tyrosine residues (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Homodimer. Interacts with CSF1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}. Note=The autophosphorylated
CC       receptor is ubiquitinated and internalized, leading to its
CC       degradation. {ECO:0000250}.
CC   -!- DOMAIN: The juxtamembrane domain functions as autoinhibitory
CC       region. Phosphorylation of tyrosine residues in this region leads
CC       to a conformation change and activation of the kinase (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The activation loop plays an important role in the
CC       regulation of kinase activity. Phosphorylation of tyrosine
CC       residues in this region leads to a conformation change and
CC       activation of the kinase (By 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.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like)
CC       domains. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AF240639; AAF76872.1; -; mRNA.
DR   RefSeq; NP_571747.1; NM_131672.1.
DR   UniGene; Dr.133025; -.
DR   ProteinModelPortal; Q9I8N6; -.
DR   SMR; Q9I8N6; 545-919.
DR   STRING; 7955.ENSDARP00000013261; -.
DR   PRIDE; Q9I8N6; -.
DR   GeneID; 64274; -.
DR   KEGG; dre:64274; -.
DR   CTD; 64274; -.
DR   ZFIN; ZDB-GENE-001205-1; csf1ra.
DR   eggNOG; COG0515; -.
DR   HOGENOM; HOG000112008; -.
DR   HOVERGEN; HBG004335; -.
DR   KO; K05090; -.
DR   PhylomeDB; Q9I8N6; -.
DR   NextBio; 20901948; -.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0048066; P:developmental pigmentation; IMP:ZFIN.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0048246; P:macrophage chemotaxis; IMP:ZFIN.
DR   GO; GO:0014004; P:microglia differentiation; IMP:ZFIN.
DR   GO; GO:0036035; P:osteoclast development; IMP:ZFIN.
DR   GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:ZFIN.
DR   GO; GO:0061075; P:positive regulation of neural retina development; IMP:ZFIN.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   GO; GO:0050936; P:xanthophore differentiation; IMP:ZFIN.
DR   Gene3D; 2.60.40.10; -; 5.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
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; IPR016243; Tyr_kinase_CSF1/PDGF_rcpt.
DR   InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PIRSF; PIRSF500947; CSF-1_receptor; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 2.
DR   PROSITE; PS50835; IG_LIKE; 3.
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   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Complete proteome; Disulfide bond;
KW   Glycoprotein; Immunity; Immunoglobulin domain; Inflammatory response;
KW   Innate immunity; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Receptor; Reference proteome; Repeat; Signal; Transferase;
KW   Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
KW   Ubl conjugation.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    977       Macrophage colony-stimulating factor 1
FT                                receptor.
FT                                /FTId=PRO_0000249006.
FT   TOPO_DOM     19    519       Extracellular. {ECO:0000255}.
FT   TRANSMEM    520    540       Helical. {ECO:0000255}.
FT   TOPO_DOM    541    977       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       22    109       Ig-like C2-type 1.
FT   DOMAIN      120    198       Ig-like C2-type 2.
FT   DOMAIN      213    305       Ig-like C2-type 3.
FT   DOMAIN      316    407       Ig-like C2-type 4.
FT   DOMAIN      408    513       Ig-like C2-type 5.
FT   DOMAIN      584    917       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     590    598       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      544    576       Regulatory juxtamembrane domain.
FT                                {ECO:0000250}.
FT   REGION      799    821       Activation loop. {ECO:0000250}.
FT   COMPBIAS    379    382       Poly-Leu.
FT   ACT_SITE    781    781       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10028}.
FT   BINDING     618    618       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     563    563       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     701    701       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     725    725       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     812    812       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     929    929       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     974    974       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   CARBOHYD     98     98       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    101    101       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    154    154       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    163    163       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    244    244       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    286    286       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    298    298       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    361    361       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    424    424       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    455    455       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     48     92       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    138    187       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    234    289       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    430    495       {ECO:0000255|PROSITE-ProRule:PRU00114}.
SQ   SEQUENCE   977 AA;  110188 MW;  C91A2F339E746A58 CRC64;
     MFFALLFLIG ILLGQVQGWS EPRIRLSSGA LAGTDVILES GSPLQLVCEG DGPVTFLPRL
     AKHKRYISKE VGKIRSFRVE KTTVDFTGTY KCVYMNGNDS NLSSSVHVFV RDSRVLFVSP
     STSLRYVRKE GEDLLLPCLL TDPEATDFTF RMDNGSAAPY GMNITYDPRK GVLIRNVHPG
     FNADYICCAR IGGAEKVSKI FSINIIQRLR FPPYVYLKRN EYVKLVGERL QISCTTNNPN
     FYYNVTWTHS SRMLPKAEEK STMEGDRLAI ESILTIPSVQ LSHTGNITCT GQNEAGANSS
     TTQLLVVEEP YIRLSPKLSS KLTHRGLSIE VSEGDDVDLG VLIEAYPPLT SHKWETPTSH
     NASLPENRFF NHNDRYEALL LLKRLNFEEI GQYTLNVKNS MKSASITFDI KMYTKPVARV
     KWENVTTLSC RSYGYPAPSI LWYQCTGIRT TCPENTTDLQ PIQTQTVEFQ KESFGAVGVE
     SVLTVGPNRR MTVVCVAFNL VGQGSDTFSM EVSDQIFTSA MCGSTVAMVV LGLLLIFMIY
     KYKQKPRYEI RWKIIEATNG NNYTFIDPTQ LPYNEKWEFP RDKLKLGKTL GAGAFGKVVE
     ATAYGLGKED NITRVAVKML KASAHPDERE ALMSELKILS HLGQHKNIVN LLGACTHGGP
     VLVITEYCCH GDLLNFLRSK AENFLNFVMT IPNFPEPMTD YKNVSTERMF VRSDSGISST
     CSDHYLDMRP VTSRPTNSAL DSSSECQEDS WPLDMDDLLR FSSQVAQGLD FLAAKNCIHR
     DVAARNVLLT NSRVAKICDF GLARDIMNDS NYVVKGNARL PVKWMAPESI FECVYTVQSD
     VWSYGIMLWE IFSLGKSPYP NILVDSKFYK MIKCGYQMSR PDFAPPEMYT IMKMCWNLDA
     AERPTFSKIS QMIQRMLGET SEQQDTQEYK NIPTEAEAEQ QLESCDPVKH EDESFETSCD
     QEEEDQPLMK PNNYQFC
//
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