ID A0A485NH93_LYNPA Unreviewed; 1019 AA.
AC A0A485NH93;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 08-OCT-2025, entry version 34.
DE RecName: Full=Macrophage colony-stimulating factor 1 receptor {ECO:0000256|ARBA:ARBA00073697};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE AltName: Full=CSF-1 receptor {ECO:0000256|ARBA:ARBA00077528};
DE AltName: Full=Proto-oncogene c-Fms {ECO:0000256|ARBA:ARBA00077514};
GN ORFNames=LYPA_23C011635 {ECO:0000313|EMBL:VFV31743.1};
OS Lynx pardinus (Iberian lynx) (Felis pardina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=191816 {ECO:0000313|EMBL:VFV31743.1, ECO:0000313|Proteomes:UP000386466};
RN [1] {ECO:0000313|EMBL:VFV31743.1, ECO:0000313|Proteomes:UP000386466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00051243};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
CC protein {ECO:0000256|RuleBase:RU000311}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily.
CC {ECO:0000256|RuleBase:RU000311}.
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DR EMBL; CAAGRJ010016033; VFV31743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A485NH93; -.
DR Proteomes; UP000386466; Unassembled WGS sequence.
DR GO; GO:1990682; C:CSF1-CSF1R complex; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019955; F:cytokine binding; IEA:InterPro.
DR GO; GO:0019838; F:growth factor binding; IEA:TreeGrafter.
DR GO; GO:0005011; F:macrophage colony-stimulating factor receptor activity; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-ARBA.
DR GO; GO:0048513; P:animal organ development; IEA:UniProtKB-ARBA.
DR GO; GO:0008283; P:cell population proliferation; IEA:UniProtKB-ARBA.
DR GO; GO:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:TreeGrafter.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:TreeGrafter.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR GO; GO:0010604; P:positive regulation of macromolecule metabolic process; IEA:UniProtKB-ARBA.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:UniProtKB-ARBA.
DR GO; GO:1905521; P:regulation of macrophage migration; IEA:UniProtKB-ARBA.
DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:TreeGrafter.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-ARBA.
DR CDD; cd00096; Ig; 1.
DR CDD; cd20936; IgI_3_CSF-1R; 1.
DR FunFam; 2.60.40.10:FF:001029; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:001088; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:001101; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:001160; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:001169; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 1.10.510.10:FF:000177; Mast/stem cell growth factor receptor; 1.
DR FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR013151; Immunoglobulin_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR050122; RTK.
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 PANTHER; PTHR24416:SF47; MACROPHAGE COLONY-STIMULATING FACTOR 1 RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500947; CSF-1_receptor; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR SUPFAM; SSF56112; Protein kinase-like (PK-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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000615-
KW 2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR500947-52};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000615-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP000386466};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000311};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 551..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..118
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 235..330
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 433..539
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 619..948
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 958..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..979
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 816
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 598
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 625..633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT BINDING 626..633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 701..707
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 820
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 821
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 961
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT DISULFID 75..117
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 160..210
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 257..311
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 450..522
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ SEQUENCE 1019 AA; 112306 MW; DCA84ACA4DAE6F3A CRC64;
MPSGPGHYGA SAETPGPCPP LCPAPSCTIP TEAMGPRALL VLLVATAWHA QGVPVIQPSG
PELVVEPGTT VTLRCVGNGS VEWDGPISPH WNLDLEPPSS ILTTNNATFQ NTGTYHCTEP
GNPQGGNATI HLYVKDPARP WKVLAQEVTV LEGQDALLPC LLTDPALEAG VSLVRVRGRP
VLRQTNYSFS PWHGFTIHKA KFIENHVYQC SARVDGRTVT SMGIWLKVQK DISGPATLTL
EPAELVRIQG EAAQIVCSAS NIDVNFDVSL RHGDTKLTIS QQSDFHDNRY QKVLTLNLDH
VSFQDAGNYS CTATNAWGNH SASMVFRVVE SAYLNLTSEQ SLLQEVTVGE KVDLQVKVEA
YPGLESFNWT YLGPFSDYQD KLDFVTIKDT YRYTSTLSLP RLKRSEAGRY SFLARNAGGQ
NALTFELTLR YPPEVRVTMT LINGSDTLLC EASGYPQPSV TWLQCRSHTD RPHSALPRCD
ESAGLVLEDS HSEVLSQVPF HEVIVHSLLA IGTLEHNRTY ECRAFNSVGN SSQTFWPISI
GAHTQLPDEL LFTPVLLTCM SIMALLLLLL LLLLYKYKQK PKYQVRWKII ESYEGNSYTF
IDPTQLPYNE KWEFPRNNLQ FGKTLGAGAF GKVVEATAFG LGKEDAVLKV AVKMLKSTAH
ADEKEALMSE LKIMSHLGQH ENIVNLLGAC THGGPVLVIT EYCCYGDLLN FLRRQAEAML
GPSLSVGQDP EAGAGYKNIH LEKKYVRRDS GFSSQGVDTY VEMRPVSTSS SNDSFSEEDL
GKEDGRPLEL RDLLHFSSQV AQGMAFLASK NCIHRDVAAR NVLLTSGRVA KIGDFGLARD
IMNDSNYIVK GNARLPVKWM APESIFDCVY TVQSDVWSYG ILLWEIFSLG LNPYPGILVN
SKFYKLVKDG YQMAQPAFAP KNIYSIMQAC WALEPTRRPT FQQICSLLQK QAQEDRRVPN
YTNLPSSSSS SSSSSSCHTG SGGGSSSEPE EESSSEHLAC CEQGDIAQPL LQPNNYQFC
//
