KITA_DANRE
ID KITA_DANRE Reviewed; 976 AA.
AC Q8JFR5; Q5RID5; Q9W755;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Mast/stem cell growth factor receptor kita;
DE Short=SCFR;
DE EC=2.7.10.1;
DE AltName: Full=Tyrosine-protein kinase Kit;
DE Flags: Precursor;
GN Name=kita; Synonyms=kit, sparse;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10393121; DOI=10.1242/dev.126.15.3425;
RA Parichy D.M., Rawls J.F., Pratt S.J., Whitfield T.T., Johnson S.L.;
RT "Zebrafish sparse corresponds to an orthologue of c-kit and is required for
RT the morphogenesis of a subpopulation of melanocytes, but is not essential
RT for hematopoiesis or primordial germ cell development.";
RL Development 126:3425-3436(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC for the cytokine kitlg/scf and plays a role in the regulation of cell
CC survival and proliferation, hematopoiesis, stem cell maintenance,
CC gametogenesis, and in mast cell development, migration and function.
CC Required for the migration of cells in the melanocyte lineage and the
CC survival of embryonic melanocytes. Required for the differentiation of
CC some, but not all, melanocytes. Not essential for hematopoiesis or
CC primordial germ cell development. {ECO:0000269|PubMed:10393121}.
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:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in cells of the neural crest-melanocyte
CC lineage. In the embryo, also expressed in mesodermal cells that give
CC rise to hematopoietic precursors, notochord, neural crest-derived cells
CC of the branchial arches, pineal gland, retina and mechanoreceptive
CC sensory cells of lateral line neuromasts. Not detected in primordial
CC germ cells or larval gut. {ECO:0000269|PubMed:10393121}.
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 -!- DISRUPTION PHENOTYPE: Defects in the number and distribution of
CC melanocytes. {ECO:0000269|PubMed:10393121}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AF153446; AAD41890.1; -; mRNA.
DR EMBL; AL691516; CAD43458.1; -; Genomic_DNA.
DR EMBL; BX248242; CAD43458.1; JOINED; Genomic_DNA.
DR EMBL; BX248242; CAI11525.1; -; Genomic_DNA.
DR EMBL; AL691516; CAI11525.1; JOINED; Genomic_DNA.
DR EMBL; BX276114; CAI11666.1; -; Genomic_DNA.
DR RefSeq; NP_571128.1; NM_131053.1.
DR AlphaFoldDB; Q8JFR5; -.
DR SMR; Q8JFR5; -.
DR STRING; 7955.ENSDARP00000099069; -.
DR PaxDb; Q8JFR5; -.
DR ABCD; Q8JFR5; 1 sequenced antibody.
DR Ensembl; ENSDART00000011135; ENSDARP00000024170; ENSDARG00000043317.
DR GeneID; 30256; -.
DR KEGG; dre:30256; -.
DR CTD; 30256; -.
DR ZFIN; ZDB-GENE-980526-464; kita.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000155626; -.
DR HOGENOM; CLU_000288_49_0_1; -.
DR InParanoid; Q8JFR5; -.
DR OMA; HWILLFV; -.
DR Reactome; R-DRE-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DRE-1433557; Signaling by SCF-KIT.
DR Reactome; R-DRE-1433559; Regulation of KIT signaling.
DR Reactome; R-DRE-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DRE-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR SignaLink; Q8JFR5; -.
DR PRO; PR:Q8JFR5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000043317; Expressed in pigment cell and 45 other tissues.
DR ExpressionAtlas; Q8JFR5; baseline.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
DR GO; GO:0048066; P:developmental pigmentation; IMP:ZFIN.
DR GO; GO:0038093; P:Fc receptor signaling pathway; IEA:InterPro.
DR GO; GO:0014831; P:gastro-intestinal system smooth muscle contraction; IMP:ZFIN.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
DR GO; GO:0038109; P:Kit signaling pathway; IBA:GO_Central.
DR GO; GO:1902362; P:melanocyte apoptotic process; IMP:ZFIN.
DR GO; GO:0030318; P:melanocyte differentiation; IMP:ZFIN.
DR GO; GO:0097324; P:melanocyte migration; IMP:ZFIN.
DR GO; GO:0043473; P:pigmentation; IMP:ZFIN.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0048865; P:stem cell fate commitment; IMP:ZFIN.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 5.
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; 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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500951; SCGF_recepter; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Differentiation; 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..976
FT /note="Mast/stem cell growth factor receptor kita"
FT /id="PRO_0000248880"
FT TOPO_DOM 22..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..976
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..105
FT /note="Ig-like C2-type 1"
FT DOMAIN 100..199
FT /note="Ig-like C2-type 2"
FT DOMAIN 206..301
FT /note="Ig-like C2-type 3"
FT DOMAIN 308..402
FT /note="Ig-like C2-type 4"
FT DOMAIN 399..504
FT /note="Ig-like C2-type 5"
FT DOMAIN 580..922
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 929..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 777
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 559
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 587..594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 662..668
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 781
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 782
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 795
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 559
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 561
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 691
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 808
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 921
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 131..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 146..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 228..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 422..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 168
FT /note="E -> Q (in Ref. 1; AAD41890)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="V -> L (in Ref. 2; CAD43458/CAI11525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 976 AA; 109280 MW; A56921FA4ED2A90D CRC64;
MEYHCVLFTV LLQLIIQPGR SRPTITPEGP RLTVPLYSNF SLHCQSNSTV RWQHENRPMR
TLKEEQRQGQ QTILKVNRAG PQHLGKYSCR EEKTGEKSSI YVYVKDPENP FRRTIVFDIV
AAEGDTTVIP CLATDPDMKN LNLQKCDGQP LPNSLRYSAS LETGVSVEKV RKEFEGCYVC
VGTLDAATVK SGRYQLTVRL VPDAPPPITL GQPQRVLLTQ GEKLSLSCST SNVNSDIAVK
WKAPNGVNPS VHQNSHLLTE PITHVRTAIL SLSSVTMQDA GNYSCEAINE KGTTAKPVWV
NIYEKGFINI TSVDNSTRRV RAGESLSLRV VMNAYPKPHT FSWSYSGVKL TNTTDHVITS
RTHGNSYTSE LKLVRLKVSE SGIYTFSCLN RDATIRQTFE VHVISKPQIV SYEGPIDGQV
RCVAEGYPTP QIKWYYCDLP HSRCSNLLNA TQEEEDVVTV TMTNPPFGKG AVESRLNITK
NNYATLECVA SANGEIVYTL FSISENTVPH ELFTPLLIGF VAAAVILVLI LIVLTYKYMQ
KPKYQIQWKV IEGIHGNNYV YIDPTQLPYD HQWEFPRDKL RFGKTLGSGA FGKVVEATAY
GMSKADTVMT VAVKMLKPSA HATEKEALMS ELKVLSYLGN HINIVNLLGA CTVGGPTLVI
TEYCCFGDLL NFLRRRRVYF YYTTLGEDAY YRNVMMQSEP NDSRNGYMTM KPSVLGILSS
ENRRSLNKGD SYSDSDAVSE ILQEDGLTLD TEDLLSFSYQ VAKGMDFLAS KNCIHRDLAA
RNILLTQGRV AKICDFGLAR DITTDSNYVV KGNARLPVKW MSPESIFECV YTFESDVWSY
GILLWEIFSL GSSPYPGMPV DSKFYKMIKE GYRMESPEFS PSEMYDIMHS CWDADPVKRP
SFSKIVEKIE QQISDSTKHI YLNFSSRLPA APGPREESSS HVHRLNSVGS HSTATQPLLS
SNDVFLDRSS PSHPVV
