ID D5MAV8_HUMAN Unreviewed; 223 AA.
AC D5MAV8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE Flags: Fragment;
GN Name=KIT {ECO:0000313|EMBL:ADF50070.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:ADF50070.1};
RN [1] {ECO:0000313|EMBL:ADF50070.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20658618; DOI=10.1002/pbc.22603;
RA Neumann I., Foell J.L., Bremer M., Volkmer I., Korholz D., Burdach S.,
RA Staege M.S.;
RT "Retinoic acid enhances sensitivity of neuroblastoma cells for imatinib
RT mesylate.";
RL Pediatr. Blood Cancer 55:464-470(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; HM030712; ADF50070.1; -; mRNA.
DR PeptideAtlas; D5MAV8; -.
DR ChiTaRS; KIT; human.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0048584; P:positive regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
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; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transferase {ECO:0000313|EMBL:ADF50070.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 32..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..223
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADF50070.1"
FT NON_TER 223
FT /evidence="ECO:0000313|EMBL:ADF50070.1"
SQ SEQUENCE 223 AA; 25151 MW; 908F35048A669223 CRC64;
ECKAYNDVGK TSAYFNFAFK EQIHPHTLFT PLLIGFVIVA GMMCIIVXIL TYKYLQKPMY
EVQWKVVEEI NGNNYVYIDP TQLPYDHKWE FPRNRLSFGK TLGAGAFGKV VEATAYGLIK
SDAAMTVAVK MLKPSAHLTE REALMSELKV LSYLGNHMNI VNLLGACTIG GPTLVITEYC
CYGDLLNFLR RKRDSFICSK QEDHAEAALY KNLLHSKESS CSD
//
