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 29-MAY-2013, entry version 91.
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).
CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC [protein]-L-tyrosine phosphate.
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).
CC -!- SUBUNIT: Monomer. Homodimer. Interacts with CSF1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (By similarity). Note=The autophosphorylated receptor is
CC ubiquitinated and internalized, leading to its degradation (By
CC similarity).
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).
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).
CC -!- PTM: Autophosphorylated in response to CSF1 binding (By
CC similarity). autophosphorylation, leading to its degradation (By
CC similarity).
CC -!- PTM: Ubiquitinated. Becomes rapidly polyubiquitinated after
CC autophosphorylation, leading to its degradation (By similarity).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily.
CC -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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DR EMBL; AF240639; AAF76872.1; -; mRNA.
DR IPI; IPI00484881; -.
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 OrthoDB; EOG4BP1B0; -.
DR NextBio; 20901948; -.
DR GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; 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:0048246; P:macrophage chemotaxis; IMP:ZFIN.
DR GO; GO:0036035; P:osteoclast development; IMP:ZFIN.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:InterPro.
DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IEA:GOC.
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_cat_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 InterPro; IPR009134; Tyr_kinase_VEGFR_rcpt_N.
DR Pfam; PF07714; Pkinase_Tyr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Kinase_like; 1.
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 Potential.
FT CHAIN 19 977 Macrophage colony-stimulating factor 1
FT receptor.
FT /FTId=PRO_0000249006.
FT TOPO_DOM 19 519 Extracellular (Potential).
FT TRANSMEM 520 540 Helical; (Potential).
FT TOPO_DOM 541 977 Cytoplasmic (Potential).
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.
FT NP_BIND 590 598 ATP (By similarity).
FT REGION 544 576 Regulatory juxtamembrane domain (By
FT similarity).
FT REGION 799 821 Activation loop (By similarity).
FT COMPBIAS 379 382 Poly-Leu.
FT ACT_SITE 781 781 Proton acceptor (By similarity).
FT BINDING 618 618 ATP (By similarity).
FT MOD_RES 563 563 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT MOD_RES 701 701 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT MOD_RES 725 725 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT MOD_RES 812 812 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT MOD_RES 929 929 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT MOD_RES 974 974 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT CARBOHYD 98 98 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 101 101 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 154 154 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 163 163 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 244 244 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 286 286 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 298 298 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 361 361 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 424 424 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 455 455 N-linked (GlcNAc...) (Potential).
FT DISULFID 48 92 By similarity.
FT DISULFID 138 187 By similarity.
FT DISULFID 234 289 By similarity.
FT DISULFID 430 495 By similarity.
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
//
