ID A0AAY4B9D6_9TELE Unreviewed; 970 AA.
AC A0AAY4B9D6;
DT 05-FEB-2025, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 1.
DT 28-JAN-2026, entry version 5.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=csf1rb {ECO:0000313|Ensembl:ENSDCDP00010017589.1};
OS Denticeps clupeoides (denticle herring).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Clupei; Clupeiformes;
OC Denticipitoidei; Denticipitidae; Denticeps.
OX NCBI_TaxID=299321 {ECO:0000313|Ensembl:ENSDCDP00010017589.1, ECO:0000313|Proteomes:UP000694580};
RN [1] {ECO:0000313|Ensembl:ENSDCDP00010017589.1, ECO:0000313|Proteomes:UP000694580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSDCDP00010017589.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSDCDP00010017589.1}
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 RefSeq; XP_028838239.1; XM_028982406.1.
DR AlphaFoldDB; A0AAY4B9D6; -.
DR Ensembl; ENSDCDT00010018644.1; ENSDCDP00010017589.1; ENSDCDG00010007689.1.
DR GeneID; 114791882; -.
DR GeneTree; ENSGT00940000155506; -.
DR Proteomes; UP000694580; Chromosome 6.
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:0001667; P:ameboidal-type cell migration; 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:0043408; P:regulation of MAPK cascade; IEA:TreeGrafter.
DR FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 1.10.510.10:FF:000140; Platelet-derived growth factor receptor beta; 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; 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; 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 SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
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}; 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 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:UP000694580};
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};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..970
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044343590"
FT TRANSMEM 521..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 202..294
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 299..400
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 584..915
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 779
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 563
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 590..598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT BINDING 591..598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 666..672
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 783
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 784
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 797
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 923
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT DISULFID 47..86
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 127..176
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 223..278
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 418..482
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ SEQUENCE 970 AA; 109439 MW; C5F6C9A7C3C5ECE5 CRC64;
MLYLALFLIV LPSTAQARNL PRIRLNSREV TQTEVMLTVG INFSLSCTGD PPISWAMVPP
HCRKQTYEDK IIINYAIAHC TGTYRCKTQQ GIYSDVYLYV KDRDDLFTPQ LLQNEVKKEG
SSHLFDCRLT DPRATDFSLL LGNGSTVPRG MRYVADPKGG IIVKDLLPQH SGNYKCSARI
DGVQKFSSLY HLSIIEKVRT PPAISAEQDR YVRCVGETLE ISCTFTNPNF VFTVTWTHSS
GQEVKFQTKP EFQKNKVRIT SIVKIKNATL SDSGNFTCTA SNEAGFNSST IHLQVIDEPY
IRLRPIVPDQ QGRDIKINEG ENLELDVEVE SYPEIESQWW DTPTHENSRN ASFREEACLR
TKNGCKNTLR LKRIRAEERG QYTLHARSSR VYTSISFNVS VHQKPRVVGR WENRSLTCSA
TGFPLPSIYW YQCSNIQTIC NGSDRVSLPA QTVLVMMGEQ GPVRAKSTPR FSQTNSTITL
ECIATNIAGE DRTTFVMPFS PNFTSARVIE VWHSQVFTPS LMGASGLALV LLLILVVVFY
KYKQKPKFEI RWKIIEANDG NNYTFVDPSQ LPYNEKWEFP RDKLKFGHIL GAGAFGKVVE
ATAYGLGTDE IITRVAVKML KPSAHSEERE ALMSELKILS HLGPHDNIVN LLGACTQGGP
MLMITEYCSH GDLLNFLRSR GEMFIISIIS EHGSSEDSCL YKNISKQEVR IRSDSGISCS
ASDYQDMTLG MKSRPLSEGC SYGSETEMNS LGLEDLIRFS YEVAQGMDFL ASRNCIHRDV
AARNVLLTEC CVAKICDFGL ARDIMNDSNY VVKGNARLPV KWMSPESIFD CVYTVQSDVW
SYGIMLWEIF SLGKSPYPEI MVDPRFYKMI KDGYHMSSPD FAPPEIYNIM EMCWNLEPTL
RPTFSKVGQL IEKLLPGSSF QRYTNMQPSQ DDQEASKLCD SPSACEESCD QSPDHGAEQQ
PLMKNNYQFC
//
