ID A0A8C4UQV2_FALTI Unreviewed; 990 AA.
AC A0A8C4UQV2;
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=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS Falco tinnunculus (Common kestrel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Falconiformes; Falconidae; Falco.
OX NCBI_TaxID=100819 {ECO:0000313|Ensembl:ENSFTIP00000016705.1, ECO:0000313|Proteomes:UP000694562};
RN [1] {ECO:0000313|Ensembl:ENSFTIP00000016705.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSFTIP00000016705.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A8C4UQV2; -.
DR Ensembl; ENSFTIT00000017408.1; ENSFTIP00000016705.1; ENSFTIG00000011026.1.
DR OMA; TIHKAKY; -.
DR OrthoDB; 6077854at2759; -.
DR Proteomes; UP000694562; Unplaced.
DR GO; GO:1990682; C:CSF1-CSF1R complex; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
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: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:0043408; P:regulation of MAPK cascade; IEA:TreeGrafter.
DR FunFam; 2.60.40.10:FF:001169; Macrophage colony-stimulating factor 1 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; 4.
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:UP000694562};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..990
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034445010"
FT TRANSMEM 508..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..91
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 198..290
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 397..498
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 576..943
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 722..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..735
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 783
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 555
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 582..590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT BINDING 583..590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 658..664
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 787
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 788
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 801
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT DISULFID 42..80
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 123..173
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 220..274
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 414..479
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ SEQUENCE 990 AA; 109969 MW; BA423A5A60BC0C69 CRC64;
MGPALLLLLT TAGIWHGSAS PLISPDLPAL VVNTGDPVIL RCSGESEVEW KSQKDAFSNH
TSSTLSILKA TYRDTGTYKC AYVNSSDKGI ATVHLFVRDP SNVWYTPTFR IFVTRGSNAE
LPCLITAPEY GSSVTLIMDE TSHLSPGTNY SFSNEKGITL FNVQSEQKGF YRCQAVINGK
IKKSSRIRLI VEEALEKPVS VMMDPIDHVR IVGEPFQVTC RVIAPSHKYD IRWVTAAKNV
RRTKKPSFEN ENYFISDILS VPAVTMEDSG KYTCIANNSA GFRNASTMLQ VVERGYVFLT
PVQAASQEIA LGESLELQVH IEAYPKLLHW GWEHTNPLKN SETITSKDVM ISGNNWYNNT
LFLNRLQEGE GGLYTFYALN NETNASVTFS ISVKSPPRIC KIKVPANDSS ILQCMAIGYP
APRIEWYQCP IHSERYSEDY RLLLNDSSPQ VVNVLPFREV EVESIVPFQE LGDNFTFCCV
AINREGNASD MFHSLTITRS VMAPPNKFFS PILSTCIGTS VLLLLLLLFL LYKYNQKPKY
QVRWKIIEAC EGNNYIFIDP TQLPYNEKWE FPRNNLQFGK TLGAGAFGKV VEATAFGLGK
EDSVLKVAVK MLKSSADTDE QEALMSELKI MSHLGHHENI VNLLGACTYG GPILVITEYC
RYGDLLNFLR KKAEYIIIQD SALDTSLDSA ADYKNIDLEK KYIRSDSGFS SQGLETYVEM
KPVSSSSSSA SSDSAQARGK SSEEEDETRE DLCPLSLSDL LQFSSQVAQG MAFLASKNCI
HRDLAARNVL ISDGRVAKIC DFGLARDIMN DSNYVVKGNA RLPVKWMAPE SIFDCIYTVQ
SDVWSYGILL WEIFSLGTAS CRHAGAWSPP RDLPLTRSAA SSRKSWRCRR SRTTPTCPPL
LRKTVAAIPL AAVRSPASKR RVASPFLRAT TISSVSWYHH PRVDPSPPSS AECTVLPCPR
TQVPPALALL SVISEIQVLP PPLAERTVLE
//
