ID A0A8C9CP78_PHOSS Unreviewed; 1029 AA.
AC A0A8C9CP78;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
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 Name=CSF1R {ECO:0000313|Ensembl:ENSPSNP00000025198.1};
OS Phocoena sinus (Vaquita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Phocoenidae; Phocoena.
OX NCBI_TaxID=42100 {ECO:0000313|Ensembl:ENSPSNP00000025198.1, ECO:0000313|Proteomes:UP000694554};
RN [1] {ECO:0000313|Ensembl:ENSPSNP00000025198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Morin P., Mountcastle J., Fungtammasan C., Rhie A., Rojas-Bracho L.,
RA Smith C.R., Taylor B.L., Gulland F.M.D., Musser W., Houck M., Haase B.,
RA Paez S., Howe K., Torrance J., Formenti G., Phillippy A., Ryder O.,
RA Jarvis E.D., Fedrigo O.;
RT "Phocoena sinus (Vaquita) genome, mPhoSin1, primary haplotype.";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPSNP00000025198.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSPSNP00000025198.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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 RefSeq; XP_032484482.1; XM_032628591.1.
DR AlphaFoldDB; A0A8C9CP78; -.
DR Ensembl; ENSPSNT00000028331.1; ENSPSNP00000025198.1; ENSPSNG00000018376.1.
DR GeneID; 116752024; -.
DR KEGG; psiu:116752024; -.
DR CTD; 1436; -.
DR GeneTree; ENSGT00940000155506; -.
DR Proteomes; UP000694554; Chromosome 3.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:1990682; C:CSF1-CSF1R complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0019838; F:growth factor binding; IEA:TreeGrafter.
DR GO; GO:0005011; F:macrophage colony-stimulating factor receptor activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; IEA:Ensembl.
DR GO; GO:0045217; P:cell-cell junction maintenance; IEA:Ensembl.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:UniProtKB-ARBA.
DR GO; GO:0021879; P:forebrain neuron differentiation; IEA:Ensembl.
DR GO; GO:0044794; P:host-mediated activation of viral process; IEA:Ensembl.
DR GO; GO:0061518; P:microglial cell proliferation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0021772; P:olfactory bulb development; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl.
DR GO; GO:0120041; P:positive regulation of macrophage proliferation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0031529; P:ruffle organization; IEA:Ensembl.
DR CDD; cd00096; Ig; 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; IPR013098; Ig_I-set.
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; PF07679; I-set; 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; 5.
DR SMART; SM00408; IGc2; 3.
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}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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:UP000694554};
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 579..603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..153
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 271..360
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 468..567
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 647..981
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..25
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 844
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 626
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 653..661
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT BINDING 654..661
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 729..735
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 848
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 849
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 862
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 989
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT DISULFID 110..152
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 195..245
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 292..346
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 485..550
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ SEQUENCE 1029 AA; 114163 MW; 7F74EA01B9245C71 CRC64;
MDSNSTSTIW GRRGISPRRR KRKIRQTASA AERSSCPVVL VPEEPVSRNL APCPPPSPAS
ACRLPPEAMG PGTLLILLVA TAWHGQGLPV IEPSGPELVV EPGTAVTLRC VSNGSVEWDG
PISTYWTLDA DAPSGILTTN NATFLNTGTY RCTERGDPLG GSATIHLYVK DPVRPWRVLV
EEVTVMEGQD ALLPCLLTDP ALGAGVSLVR VRGRPVLRQT NYSFLPSHGF IIHKAKFIES
QDYECSARVD GRMVKSLSIR LKVQKVIPGP PTLTLKPTEL VRIQGEAAQI ICSASDVDVN
FDVFLQHGDT KLTISQQSDF HDNRYQKVLT LNLDHVDFQD AGNYTCMATN ARGIHSTSMV
FWVVDSAYLN LTSEQNLLQE VTVGEKIELK VKVEAYPSLQ SFNWTYQGPF LGHQPKLNFV
TNKGTYRYTS TLTLLRLKPF EAGHYSFQAR NARGEETLTF ELTLLYPPEV EVTWTLINGS
KTLLCEASGY PQPNVTWVQC RGHTNRCGKT QVLVLDDPNP EVLSQKPFHK VTVQSLLATG
TLEHNRTYEC RAYNSLGNSS QAFGPVSVGA YTQPLDEPLF TPVLVACMSV TALLLLLLLL
LLYKYKQKPK YQVRWKIIES YGGNSYTFID PTQLPYNEKW EFPRNNLQFG KTLGAGAFGK
VVEATAFGLG EEDAVLKVAV KMLKSTAHAD EKEALMSELK IMSHLGQHEN IVNLLGACTH
GGPVLVITEY CCYGDLLNFL RRKAEAMLGP SLNPGQDPKA GTGYKNIHLE KKYIRRDSGF
SSQGVDTYVE MRPVSTSSSN DSFSEQDLDK ENGRLLELRD LLHFSSQVAQ GMAFLASKNC
IHRDVAARNV LLTSGHVAKI GDFGLARDIM NDSNYIVKGN ARLPVKWMAP ESIFDCVYTV
QSDVWSYGIL LWEIFSLGLN PYPGILVNSK FYKLVKDGYQ MAQPAFAPKN IYSIMQACWA
LEPTRRPTFQ QICSLLQEQV LVDRREQDYS NLPSSSSEPE EESSSEHLGC CEQGGIAQPL
LQPNNYEFC
//
