ID A0A0U2N547_HUMAN Unreviewed; 971 AA.
AC A0A0U2N547;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 28-JAN-2026, entry version 57.
DE RecName: Full=Mast/stem cell growth factor receptor {ECO:0000256|PIRNR:PIRNR500951};
DE EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR500951};
GN Name=KIT {ECO:0000313|EMBL:ALS55361.1,
GN ECO:0000313|Ensembl:ENSP00000509704.1};
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:ALS55361.1};
RN [1] {ECO:0000313|Ensembl:ENSP00000509704.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11237011; DOI=10.1038/35057062;
RG International Human Genome Sequencing Consortium;
RA Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J.,
RA Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K.,
RA Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P.,
RA McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J.,
RA Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C.,
RA Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J.,
RA Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C.,
RA Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I.,
RA Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S.,
RA Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S.,
RA Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S.,
RA Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A.,
RA Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R.,
RA Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A.,
RA Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W.,
RA Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T.,
RA Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E.,
RA Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B.,
RA Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L.,
RA Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y.,
RA Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C.,
RA Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W.,
RA Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P.,
RA Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M.,
RA Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A.,
RA Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A.,
RA Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M.,
RA Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R.,
RA Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A.,
RA Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J.,
RA Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N.,
RA Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L.,
RA Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G.,
RA Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R.,
RA Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G.,
RA Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W.,
RA Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J.,
RA Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M.,
RA McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J.,
RA Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E.,
RA Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J.,
RA Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F.,
RA Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A.,
RA Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K.,
RA Shizuya H., Choi S., Chen Y.J.;
RT "Initial sequencing and analysis of the human genome.";
RL Nature 409:860-921(2001).
RN [2] {ECO:0000313|Ensembl:ENSP00000509704.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496913; DOI=10.1038/nature03001;
RG International Human Genome Sequencing Consortium;
RT "Finishing the euchromatic sequence of the human genome.";
RL Nature 431:931-945(2004).
RN [3] {ECO:0000313|Ensembl:ENSP00000509704.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.M., Maupin R., Latreille P., Wendl M.C., Yang S.P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4] {ECO:0000313|EMBL:ALS55361.1}
RP NUCLEOTIDE SEQUENCE.
RA Osman I., Vega y Saenz de Miera E.C.;
RT "Novel CKIT Alternative Splice Variant Expressed in Melanoma and
RT Melanocytes.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Ensembl:ENSP00000509704.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-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 ECO:0000256|PIRNR:PIRNR500951};
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|PIRNR:PIRNR500951, ECO:0000256|RuleBase:RU000311}.
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DR EMBL; AC006552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF510866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KT326922; ALS55361.1; -; mRNA.
DR RefSeq; NP_001372215.1; NM_001385286.1.
DR AlphaFoldDB; A0A0U2N547; -.
DR SMR; A0A0U2N547; -.
DR DNASU; 3815; -.
DR Ensembl; ENST00000686011.1; ENSP00000509704.1; ENSG00000157404.17.
DR GeneID; 3815; -.
DR CTD; 3815; -.
DR DisGeNET; 3815; -.
DR HGNC; HGNC:6342; KIT.
DR OpenTargets; ENSG00000157404; -.
DR GeneTree; ENSGT00940000155626; -.
DR OrthoDB; 6077854at2759; -.
DR BioGRID-ORCS; 3815; 9 hits in 1192 CRISPR screens.
DR ChiTaRS; KIT; human.
DR Proteomes; UP000005640; Chromosome 4.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019955; F:cytokine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016477; P:cell migration; IEA:UniProtKB-ARBA.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-ARBA.
DR GO; GO:0038093; P:Fc receptor signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0008406; P:gonad development; IEA:UniProtKB-ARBA.
DR GO; GO:0030097; P:hemopoiesis; IEA:UniProtKB-ARBA.
DR GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
DR GO; GO:0045321; P:leukocyte activation; IEA:UniProtKB-ARBA.
DR GO; GO:0070662; P:mast cell proliferation; IEA:UniProtKB-ARBA.
DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; IEA:UniProtKB-ARBA.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR GO; GO:0050793; P:regulation of developmental process; IEA:UniProtKB-ARBA.
DR CDD; cd00096; Ig; 2.
DR CDD; cd05860; IgI_4_SCFR; 1.
DR CDD; cd05104; PTKc_Kit; 1.
DR FunFam; 1.10.510.10:FF:000177; Mast/stem cell growth factor receptor; 1.
DR FunFam; 2.60.40.10:FF:000422; Mast/stem cell growth factor receptor; 1.
DR FunFam; 2.60.40.10:FF:000429; Mast/stem cell growth factor receptor; 1.
DR FunFam; 2.60.40.10:FF:000469; Mast/stem cell growth factor receptor; 1.
DR FunFam; 2.60.40.10:FF:000544; Mast/stem cell growth factor receptor; 1.
DR FunFam; 2.60.40.10:FF:000815; 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; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin_dom.
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; PF00047; ig; 1.
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; 3.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
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 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR500951};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR500951};
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR500951};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR500951};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR500951};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR500951};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR500951};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0U2N547,
KW ECO:0007829|ProteomicsDB:A0A0U2N547};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR500951};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR500951};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR500951};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR500951};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR500951};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR500951};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT CHAIN 26..971
FT /note="Mast/stem cell growth factor receptor"
FT /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT /id="PRO_5044535594"
FT TRANSMEM 521..544
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT DOMAIN 212..308
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 585..932
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 787
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 564
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 592..599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 667..673
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 791
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 792
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 805
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 931
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 971 AA; 109364 MW; A21E66B450878E1C CRC64;
MRGARGAWDF LCVLLLLLRV QTGSSQPSVS PGEPSPPSIH PGKSDLIVRV GDEIRLLCTD
PGFVKWTFEI LDETNENKQN EWITEKAEAT NTGKYTCTNK HGLSNSIYVF VRDPAKLFLV
DRSLYGKEDN DTLVRCPLTD PEVTNYSLKG CQGKPLPKDL RFIPDPKAGI MIKSVKRAYH
RLCLHCSVDQ EGKSVLSEKF ILKVRPAFKA VPVVSVSKAS YLLREGEEFT VTCTIKDVSS
SVYSTWKREN SQTKLQEKYN SWHHGDFNYE RQATLTISSA RVNDSGVFMC YANNTFGSAN
VTTTLEVVDK GFINIFPMIN TTVFVNDGEN VDLIVEYEAF PKPEHQQWIY MNRTFTDKWE
DYPKSENESN IRYVSELHLT RLKGTEGGTY TFLVSNSDVN AAIAFNVYVN TKPEILTYDR
LVNGMLQCVA AGFPEPTIDW YFCPGTEQRC SASVLPVDVQ TLNSSGPPFG KLVVQSSIDS
SAFKHNGTVE CKAYNDVGKT SAYFNFAFKE QIHPHTLFTP LLIGFVIVAG MMCIIVMILT
YKYLQKPMYE VQWKVVEEIN GNNYVYIDPT QLPYDHKWEF PRNRLSFGKT LGAGAFGKVV
EATAYGLIKS DAAMTVAVKM LKPSAHLTER EALMSELKVL SYLGNHMNIV NLLGACTIGG
PTLVITEYCC YGDLLNFLRR KRDSFICSKQ EDHAEAALYK NLLHSKESSC DSTNEYMDMK
PGVSYVVPTK ADKRRSVRIG SYIERDVTPA IMEDDELALD LEDLLSFSYQ VAKGMAFLAS
KNCIHRDLAA RNILLTHGRI TKICDFGLAR DIKNDSNYVV KGNARLPVKW MAPESIFNCV
YTFESDVWSY GIFLWELFSL GSSPYPGMPV DSKFYKMIKE GFRMLSPEHA PAEMYDIMKT
CWDADPLKRP TFKQIVQLIE KQISESTNHI YSNLANCSPN RQKPVVDHSV RINSVGSTAS
SSQPLLVHDD V
//
