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Database: UniProt
Entry: A0A8C6P1H9_NOTFU
LinkDB: A0A8C6P1H9_NOTFU
Original site: A0A8C6P1H9_NOTFU 
ID   A0A8C6P1H9_NOTFU        Unreviewed;       916 AA.
AC   A0A8C6P1H9;
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};
DE   AltName: Full=Tyrosine-protein kinase Kit {ECO:0000256|ARBA:ARBA00032147};
GN   Name=kitb {ECO:0000313|Ensembl:ENSNFUP00015036965.1};
OS   Nothobranchius furzeri (Turquoise killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Nothobranchiidae;
OC   Nothobranchius.
OX   NCBI_TaxID=105023 {ECO:0000313|Ensembl:ENSNFUP00015036965.1, ECO:0000313|Proteomes:UP000694548};
RN   [1] {ECO:0000313|Ensembl:ENSNFUP00015036965.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GRZ {ECO:0000313|Ensembl:ENSNFUP00015036965.1};
RA   Senf B., Petzold A., Downie B.R., Koch P., Platzer M.;
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNFUP00015036965.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSNFUP00015036965.1}
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   AlphaFoldDB; A0A8C6P1H9; -.
DR   Ensembl; ENSNFUT00015038597.1; ENSNFUP00015036965.1; ENSNFUG00015017809.1.
DR   GeneTree; ENSGT00940000155626; -.
DR   Proteomes; UP000694548; Chromosome sgr08.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001667; P:ameboidal-type cell migration; IEA:UniProtKB-ARBA.
DR   GO; GO:0030183; P:B cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0038093; P:Fc receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:TreeGrafter.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; 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; 4.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR050122; RTK.
DR   InterPro; IPR027263; SCGF_receptor.
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:SF599; MAST_STEM CELL GROWTH FACTOR RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF25305; Ig_PDGFR_d4; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF21339; VEGFR-1-like_Ig-like; 1.
DR   PIRSF; PIRSF500951; SCGF_recepter; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000615-3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   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:UP000694548};
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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..916
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5034990027"
FT   TRANSMEM        496..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          23..90
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          206..242
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          298..381
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          564..877
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        742
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         543
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         571..578
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         598
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         646..652
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         746
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         747
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         760
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ   SEQUENCE   916 AA;  102949 MW;  C5B2C0A24790BCA0 CRC64;
     IEHLWKELKH ILFVLFVLVW SKPVISPSGP HIVVPKKGKL ELSCHDNATA SQLKWGNDRN
     RKLEIKVEEG GVASVRVSAV QAYHMGRYTC VNVITKEQSS IYVFVKDSEN AFHRTMVNNI
     LVRAGEDCII PCLVTNPEIT SLTLETCDGQ PLPSGMSFHS NFERGIIIND TTEEYVGCYV
     CTAQLSGNKV TSSLYTVDVQ LAPESPPVIT LSQKDVIILK AGEQFELTCS STNVNPEFSL
     KWDFPLTAVR FITLFVQDLS NGGMTQRASQ TLCTQSLFSK LIHLCSAGQG FIKMLGSPGP
     VQADVREGES FSLKVEFDAY PPPHSLSWSY NNKRLLNTTE HVITVHHRKY RYTSELRLVR
     VLGSEGGIYE FSASHEDASV AHLFHVYVNS KPVIVAHEGP VDGQVRCIAA GYPVPKISWY
     VCELPHTRCS LLPNATHWET TEVTILSESP FGRSEVESRL NVTKEHAQFH TLECVASTEG
     EEAYTLFSIS VVPHRLFTPL LTGMLATGAF LVLFLVVLLY KYMQKPKFQI QWKVIESING
     NNYIYVDPLQ LPYDIKWEFP RQKLRFGKTL GSGAFGKVVR ATAYGLCSVD TVTTVAVKML
     KPNAHSTEKE ALMSELKVLS YLGNHVNIVN LLGACTVGGP ILVITEYCCY GDLLNFLRRK
     RQSFLNSQVG DGYYRNISNQ TDRGVTGPGY MPMHPSEKER SSQSGNHFID ELSLDVEDLL
     SFSYQVAKGM EYITSKNCIH RDLAARNVLL THGRVAKICD FGLARDITTD ASYVLRGNAR
     LPVKWMSPES IFDCIYTFES DVWSYGILLW EIFSLGNSPY PGMQVCSVFY KMIQEGHRMS
     RPEFASIEMY EMMLSCWNHD PLKRPSFRKL VERTELLLSE NTKNRMPSRR LSSVCSTTAP
     TQPLLQNTAD VFMDYV
//
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