UniProt: A0A673WU59

Database: UniProt
Entry: A0A673WU59_SALTR

LinkDB:  A0A673WU59_SALTR 
Original site:  A0A673WU59_SALTR

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Ontology (19)   
   GO (19)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (26)   
   InterPro (14)   
   Pfam (4)   
   PROSITE (5)   
   SMART (3)   
All databases (52)   

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ID   A0A673WU59_SALTR        Unreviewed;      1113 AA.
AC   A0A673WU59;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   28-JAN-2026, entry version 28.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=LOC115205390 {ECO:0000313|Ensembl:ENSSTUP00000012172.1};
OS   Salmo trutta (Brown trout).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000012172.1, ECO:0000313|Proteomes:UP000472277};
RN   [1] {ECO:0000313|Ensembl:ENSSTUP00000012172.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSSTUP00000012172.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC       for CSF1 and plays an essential role in the regulation of survival,
CC       proliferation and differentiation of hematopoietic precursor cells,
CC       especially mononuclear phagocytes, such as macrophages and monocytes.
CC       Plays an important role in innate immunity and in inflammatory
CC       processes. Plays an important role in the regulation of osteoclast
CC       proliferation and differentiation, the regulation of bone resorption,
CC       and is required for normal bone development. Promotes reorganization of
CC       the actin cytoskeleton, regulates formation of membrane ruffles, cell
CC       adhesion and cell migration. Activates several signaling pathways in
CC       response to ligand binding. {ECO:0000256|ARBA:ARBA00058066}.
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   -!- SUBUNIT: Monomer. Homodimer. Interacts with CSF1.
CC       {ECO:0000256|ARBA:ARBA00062014}.
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_029627194.1; XM_029771334.1.
DR   AlphaFoldDB; A0A673WU59; -.
DR   FunCoup; A0A673WU59; 1193.
DR   Ensembl; ENSSTUT00000012901.1; ENSSTUP00000012172.1; ENSSTUG00000003249.1.
DR   GeneID; 115205390; -.
DR   KEGG; stru:115205390; -.
DR   GeneTree; ENSGT00940000155506; -.
DR   InParanoid; A0A673WU59; -.
DR   OMA; TIHKAKY; -.
DR   OrthoDB; 6077854at2759; -.
DR   Proteomes; UP000472277; Chromosome 13.
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:0048513; P:animal organ development; IEA:UniProtKB-ARBA.
DR   GO; GO:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; 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:0030318; P:melanocyte differentiation; IEA:UniProtKB-ARBA.
DR   GO; GO:0097324; P:melanocyte migration; IEA:UniProtKB-ARBA.
DR   GO; GO:0030316; P:osteoclast differentiation; IEA:TreeGrafter.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:TreeGrafter.
DR   GO; GO:0022603; P:regulation of anatomical structure 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   CDD; cd05106; PTKc_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:002322; 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; 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   PRINTS; PR01832; VEGFRECEPTOR.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR500947-52};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW   ECO:0000256|RuleBase:RU000311};
KW   Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   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:UP000472277};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   TRANSMEM        652..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          342..433
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          715..1048
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        912
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         694
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         721..729
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT   BINDING         722..729
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         749
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         797..803
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         916
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         917
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         930
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   SITE            1059
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT   DISULFID        175..219
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        267..316
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        363..418
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT   DISULFID        557..626
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ   SEQUENCE   1113 AA;  126013 MW;  36F6551CFF4D1EAA CRC64;
     MALGLGGPAC LLTKPRRMVI SGERDTSVCP SVCLYLFYCL RVRLRETETE EKQGWRDFTR
     FWMLDPYSLV RSDLTTALKT STEKKKCMTA ELQPDDSSFL SLTTDAITTL RDIQTYSQTQ
     SWRRSRMVLY LAFLLGILPT AAQAQWRHPV IKLNSKLVVG PEVVLNPGTP LVLRCEGDGP
     VNWLTRLAKH KRFISKVKGR VRTFRVDRPS AEHTGTYKCE YTSVNAKGQD LFSTVHVYVK
     DPDSLFWTSS TSLSVVRKEG ENYLLPCLLT DPEATDLGLR MDNCTSVPPG MNYTADPRRG
     ILIRNLQPSY NADYVCSAKL HGVERTSKAF SINIIQRLRF PPYVFLEKDE YVRIVGEKLR
     IHCTTHNPNF NYNVTWNYSS KKRSTIEENV QSKDSRLDIE SILTIPAVDQ SDTGNITCTG
     TNEAGVNSSA TYLLVVEEPY IRLSPQLSSK LAHQGLSIEV NEGEDLKLCV LIEAYPQIIA
     QSWDTPTSSP TQEHIFTRYN NRYSATLLLK RMIAQEQGQY TFYARSAMAN ASITFQVQMY
     QKPVAVVRWE NITSLMCTSF GYPAPIILWY QCSGIRATCN ENNTGLQMPA PLLAQTVEVQ
     REEYGPVEVE SVLTVGPSNR RMTVECVAFN LAGVGKDTFA MDVSDKVFTS TLSGAAGVLA
     FLILLLIILL YKYKQKPRYE IRWKIIQASD GNNYTFIDPS QLPYNEKWEF PRDKLKLGKI
     LGAGAFGKVV EATAYGLGED DNAIRVAVKM LKARAHSDER EALMSELKIL SHLGQHKNIV
     NLLGACTQAG PVLVITEYCS HGDLLNFLRH KQETFLNFVM NMPEVPEETS DYKNVCEEKQ
     FIRSDSGISS VSSDSYLEMR PGPQPVNSSL DSLCEEGGPD SWPLDMDDLL RFSYQVAQGL
     DFLAAKNCIH RDVAARNVLL TDRRVAKICD FGLARDIMND SNYVVKGNAR LPVKWMAPES
     IFDCLYTVQS DVWSYGILLW EIFSLGKSPY PSILVDTKFY KMIESGYQMS RPDFAPPEMY
     TIMKMCWNLE PTERPTFSKI SQLIERVLGE QPECPDQQYQ NIQQQDMVIE ELEPCDDDDD
     DDETKFCDGS CDQSCEHEVD EQPLMKTNNY QFC
//

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