ID A0A091D5X4_FUKDA Unreviewed; 1002 AA.
AC A0A091D5X4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Mast/stem cell growth factor receptor Kit {ECO:0000256|ARBA:ARBA00014417};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE AltName: Full=Proto-oncogene c-Kit {ECO:0000256|ARBA:ARBA00032530};
DE AltName: Full=Tyrosine-protein kinase Kit {ECO:0000256|ARBA:ARBA00032147};
GN ORFNames=H920_12153 {ECO:0000313|EMBL:KFO26477.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO26477.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO26477.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO26477.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC 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 EMBL; KN123184; KFO26477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091D5X4; -.
DR STRING; 885580.ENSFDAP00000006399; -.
DR eggNOG; KOG0200; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019955; F:cytokine binding; IEA:InterPro.
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:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0038093; P:Fc receptor signaling pathway; IEA:InterPro.
DR GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
DR CDD; cd00096; Ig; 2.
DR CDD; cd05860; IgI_4_SCFR; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
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; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; PF00047; ig; 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; 3.
DR SMART; SM00408; IGc2; 3.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00023137};
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|PIRSR:PIRSR000615-2, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
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 546..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 240..337
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 614..962
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 41..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..66
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 817
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 593
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 621..628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 696..702
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 821
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 822
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 835
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 961
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR500951-3"
SQ SEQUENCE 1002 AA; 112140 MW; EB9244301E2ED1DB CRC64;
MVSATHQELC GAHLTGPVKK HGLNKETPVC FAAFQQLQVG LHSPPPLPPK GSPQPPASPG
EPSPPSILPA QSELIVRAGD QIRLTCTDPA FVKWTFKTLG DVSENKDSEW IRAEAEAAHT
GKYTCTNRDG LSSSIYVFVR DPAKLFLIGV PLFGKEDNDT LVRCPLTDPE VTDYSLKECE
GRPLPKDLMF VPDPRAGITI RNVKRAYHRL CLRCSASREG KLVLSDKFIL KVRAAIKATP
VVSVSKASYL LREGEEFTVT CTIKDVSSSV GAMWIKENSQ LTEDQVKRNS WHQGDFNYER
LETLTISSTR VNDSGVFMCY ANNTFGSANV TTTLKVVDKG FIKIFSMMNT TVFVNDGENV
DLIVEYEAYP KPEHQQWIYM NRTSSNKWED YPNSENESNI RYVSKLHLTR LKATEGGTYT
FFVSNSDVNA SMTFTIYVNT KPEILIYDRL MNGMLQCVAA GFPEPTIDWY FCSGMEPRCS
NSVQPVDVQI QNSSLPPFGK LLVQSSIDSS MFRHNGTVEC KASNDVGKIS AFFNFAFKEQ
THPHTLFTPL LIGFVITAGM MCIIVMVLTY KCLQKPMYEV QWKVVEEING NNYVYIDPTQ
LPYDHKWEFP RNRLSFGKTL GAGAFGKVVE ATAYGLIKSD AAMTVAVKML KPSAHLTEQE
ALMSELKILS YLGNHMNIVN LLGACTVGGP TLVITEYCCY GDLLNFLRRK HDSFICSKQE
DHAEAALYKN LLHSKGSSCS DSTNEYMDMK PGVSYVVPTK ADKRRSARIG SYIERDVTPA
IMEDDELALD LEDLLSFSYQ VAKGMAFLAS KNCIHRDLAA RNILLTHGRI TKICDFGLAR
DIKNDSNYVV KGNARLPVKW MAPESIFNCV YTFESDVWSY GIFLWELFSL GSSPYPGIPV
DSKFYKMIKE GFRMLSPERA PAEMYDIMKT CWDADPLKRP TFKQIVQLIE KQISDSTNHI
YSNLANCTPN PENPMEVDRS VRVNSVGSSA SSTQPLLVHK DV
//
