ID A0A8B9D2S3_ANSCY Unreviewed; 1031 AA.
AC A0A8B9D2S3;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS Anser cygnoides (Swan goose).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anserinae; Anser.
OX NCBI_TaxID=8845 {ECO:0000313|Ensembl:ENSACDP00005001213.1, ECO:0000313|Proteomes:UP000694521};
RN [1] {ECO:0000313|Ensembl:ENSACDP00005001213.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSACDP00005001213.1}
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: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, 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 AlphaFoldDB; A0A8B9D2S3; -.
DR Ensembl; ENSACDT00005001441.1; ENSACDP00005001213.1; ENSACDG00005000832.1.
DR Proteomes; UP000694521; 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 CDD; cd00096; Ig; 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; 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; PF13927; Ig_3; 2.
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; 2.
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:UP000694521};
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 572..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..160
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 264..356
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 640..982
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..800
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 846
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 619
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 646..654
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT BINDING 647..654
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 722..728
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 850
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 851
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 864
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT DISULFID 108..146
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 189..239
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 286..340
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 480..545
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ SEQUENCE 1031 AA; 115079 MW; F77B1E987041F594 CRC64;
MGLKVSRATR PEQQKQQKKK EFLNLWSTQK GEAPAEGELG TAPARRGACC SSRVPAPWGD
TVVPGDMGPG LLLLLTAASI WHGSASPVIS PNLSALVVNT GDPVTLRCSG ESQVKWYTQK
HTSTNHTSST LSIPKATYMD TGTYACAYVN SSDKDAASIH LFVRDPDNVW YTPNFRIPVN
KGGNAQFPCL ITAPEYGSRV TLIMDDASPL SPGTNYSFST EKGITLYNVQ RHQKGYYRCQ
TVINGKIKKS PRIRLIVEEA LEKPVSVTME PIDHVRIVGE PFEVTCRVIS PSHKYDIKWV
TAAKNVRSTK IPTFVDENYF INAVLSIPAV TLEDSGKYTC IANNSAGFKN ASTMLHVVER
GYILLTPVQA ISQEVALGED LKLQVQIEAY PKLVSWHWEH KSPFKNSEST KFVGKMISGN
NWYNNTLFLN RLQEGERGLY TFYAVNNETK ASVNFSISVK FAPRVCYVWV PANDSGNLHC
IAIGYPAPRI EWYQCPTYSD RYNEDYKLLL NDSSPQVVNM LSFQEVEVES VLPFQDLGAN
FTFCCVAVNR EGNTSDVLHS VVRNVMAPPN KLFSPILSTC VSTLVLLLLL LLFLLYKYNQ
KPKYQVRWKI IEACEGNNYI FIDPTQLPYN EKWEFPRNNL QFGKTLGAGA FGKVVEATAF
GLGKEDSVLK VAVKMLKSSA DTDEQEALMS ELKIMSHLGH HENIVNLLGA CTYGGPILVI
TEYCRYGDLL NFLRRKAESI IIQDSSLDTS LDSTADYKNI DLEKKYIRSD SGFASQGLET
YVEMRPVSAS SSASSDSAQA RGKSSEEEVE TREDLRPLNL SDLLQFSSQV AQGMAFLASK
NCIHRDLAAR NVLVSDGRVA KICDFGLARD IMNDSNYVVK GNARLPVKWM APESIFDCIY
TVQSDVWSYG ILLWEIFSLG KSPYPGMVVN SKFYSMVKQG YQMARPDFAP LEMYTIMQAC
WSLEPTQRPT FDQICCFIQK ELEVHKEQDQ TNLPSTAEED SGCDTSGCCE ESCEQEQSGQ
PLLKSNNYQF C
//
