ID KIT_TAKRU Reviewed; 984 AA.
AC Q8AXC6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 28-JAN-2026, entry version 127.
DE RecName: Full=Mast/stem cell growth factor receptor Kit;
DE Short=SCFR;
DE EC=2.7.10.1;
DE AltName: Full=Tyrosine-protein kinase kit;
DE Flags: Precursor;
GN Name=kit;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12592706; DOI=10.1080/1042517021000011627;
RA Williams H., Brenner S., Venkatesh B.;
RT "Characterization of the platelet-derived growth factor receptor alpha and
RT c-kit genes in the pufferfish Fugu rubripes.";
RL DNA Seq. 13:263-270(2002).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC for the cytokine kitlg/scf and plays an essential role in the
CC regulation of cell survival and proliferation, hematopoiesis, stem cell
CC maintenance, gametogenesis, mast cell development, migration and
CC function, and in melanogenesis. {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Rapidly ubiquitinated after autophosphorylation
CC induced by kitlg/scf binding, leading to internalization and
CC degradation. {ECO:0000250}.
CC -!- PTM: Autophosphorylated on tyrosine residues. Phosphorylated tyrosine
CC residues are important for interaction with specific binding partners
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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 EMBL; AF456419; AAN87555.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8AXC6; -.
DR SMR; Q8AXC6; -.
DR FunCoup; Q8AXC6; 805.
DR STRING; 31033.ENSTRUP00000063495; -.
DR GlyCosmos; Q8AXC6; 7 sites, No reported glycans.
DR GeneID; 101073765; -.
DR CTD; 30256; -.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; Q8AXC6; -.
DR OrthoDB; 6077854at2759; -.
DR Proteomes; UP000005226; Unplaced.
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-KW.
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: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:0030318; P:melanocyte differentiation; IEA:UniProtKB-ARBA.
DR GO; GO:0097324; P:melanocyte migration; IEA:UniProtKB-ARBA.
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; 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; 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; 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:SF46; MAST_STEM CELL GROWTH FACTOR RECEPTOR KIT; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500951; SCGF_recepter; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
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; 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; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..984
FT /note="Mast/stem cell growth factor receptor Kit"
FT /id="PRO_0000248881"
FT TOPO_DOM 22..514
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..984
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..97
FT /note="Ig-like C2-type 1"
FT DOMAIN 98..197
FT /note="Ig-like C2-type 2"
FT DOMAIN 203..300
FT /note="Ig-like C2-type 3"
FT DOMAIN 311..395
FT /note="Ig-like C2-type 4"
FT DOMAIN 398..498
FT /note="Ig-like C2-type 5"
FT DOMAIN 579..926
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 711..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..723
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..749
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 781
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 558
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 586..593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 661..667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 785
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 786
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 799
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 558
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 560
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 690
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 707
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 812
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 925
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 129..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 226..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 421..487
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 984 AA; 110732 MW; 27D1EDC837CE8295 CRC64;
MEYHWILLCV SLCFTFHPGD TKPTITPAGT YVVVSLNAPL ELQCQGEKAM QWQREERPKV
RGETKVDGKS TLYIPKAHPA HMGRYICLEE TSQERASIYI YVKDPDNPFR KSMVSNILSR
EGDSASIPCL ATDPSLENLQ LKTCSSKALA SGLHFSPSLE QGIIIHNTQK SYEGCYVCTG
RLKETNVRSH DYHLTVRPVP VAPPVIMMQA PKRVILIRDE SLYLTCNTTN VNGNIKLKWV
APLGSQPAKV DGSSRILTEN FTQARSATLH IAAVRIQDTG RYQCEAENEK GVSTQSVWLD
VFEKGFMYSN PVNNGTIQVR AGESLLLSVS IEAYPMPRSA SWSFMGRGLH NTSDHVITTR
SHEYTYSSEL KLVRLKMSEG GVYTFQASNG DASVNHTFTI FVISKPEIVS HEGPVDGQVR
CVAEGFPAPQ ITWYYCEQPY ARCSQQVNAT QEEQNVITVT LFSPLFGKTE VESRVNISRG
RFSTLECVAT VEGEQAFTLF SISERTISHD LFSPLLIGSV SAACILCLIL IVLFYKYMQK
PKYQIQWKVI EGIHGNNYVY IDPTQLPYDH QWEFPRKNLR FGKTLGSGAF GKVVEATAYG
LANEDSMMTV AVKMLKSSAH STEKEALMSE LKVLIYLGNH INIVNLLGAC TVGGPTLVIT
EYCCFGDLLN FLRRKRESFI CFKLEEDCHY RNIMLQREMA GDSLNGYMTM RPSAAGKPSS
SSSSEKRRSL REGSPYVEED SESEMFDEDS LSLDTEDLLS FSYQVAKGME FLTSKNCIHR
DLAARNILLT QGRVAKICDF GLARDINTDS NYVVKGNARL PVKWMSPESI FECVYTFESD
VWSYGILLWE IFSLGNSPYP GMPVDAKFYK LIKEGYRMDA PEFAPSEMYQ IMRSCWDADP
LNRPPFRKVV ERIEQQLSDT TKHIYLNFSS RVPVMPRGRE ESSTHSMASQ PFNSAGNNSP
PSRPLLLHHE VFLEGTEPFR VQRV
//
