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Mast/stem cell growth factor receptor kita (SCFR) (EC 2.7.10.1) (Tyrosine-protein kinase Kit)

 KITA_DANRE              Reviewed;         976 AA.
Q8JFR5; Q5RID5; Q9W755;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 2.
20-JUN-2018, entry version 124.
RecName: Full=Mast/stem cell growth factor receptor kita;
Short=SCFR;
EC=2.7.10.1;
AltName: Full=Tyrosine-protein kinase Kit;
Flags: Precursor;
Name=kita; Synonyms=kit, sparse;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
DISRUPTION PHENOTYPE.
PubMed=10393121;
Parichy D.M., Rawls J.F., Pratt S.J., Whitfield T.T., Johnson S.L.;
"Zebrafish sparse corresponds to an orthologue of c-kit and is
required for the morphogenesis of a subpopulation of melanocytes, but
is not essential for hematopoiesis or primordial germ cell
development.";
Development 126:3425-3436(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
-!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface
receptor for the cytokine kitlg/scf and plays a role in the
regulation of cell survival and proliferation, hematopoiesis, stem
cell maintenance, gametogenesis, and in mast cell development,
migration and function. Required for the migration of cells in the
melanocyte lineage and the survival of embryonic melanocytes.
Required for the differentiation of some, but not all,
melanocytes. Not essential for hematopoiesis or primordial germ
cell development. {ECO:0000269|PubMed:10393121}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in cells of the neural crest-
melanocyte lineage. In the embryo, also expressed in mesodermal
cells that give rise to hematopoietic precursors, notochord,
neural crest-derived cells of the branchial arches, pineal gland,
retina and mechanoreceptive sensory cells of lateral line
neuromasts. Not detected in primordial germ cells or larval gut.
{ECO:0000269|PubMed:10393121}.
-!- PTM: Ubiquitinated. Rapidly ubiquitinated after
autophosphorylation induced by kitlg/scf binding, leading to
internalization and degradation. {ECO:0000250}.
-!- PTM: Autophosphorylated on tyrosine residues. Phosphorylated
tyrosine residues are important for interaction with specific
binding partners (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Defects in the number and distribution of
melanocytes. {ECO:0000269|PubMed:10393121}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; AF153446; AAD41890.1; -; mRNA.
EMBL; AL691516; CAD43458.1; -; Genomic_DNA.
EMBL; BX248242; CAD43458.1; JOINED; Genomic_DNA.
EMBL; BX248242; CAI11525.1; -; Genomic_DNA.
EMBL; AL691516; CAI11525.1; JOINED; Genomic_DNA.
EMBL; BX276114; CAI11666.1; -; Genomic_DNA.
RefSeq; NP_571128.1; NM_131053.1.
UniGene; Dr.81312; -.
ProteinModelPortal; Q8JFR5; -.
SMR; Q8JFR5; -.
STRING; 7955.ENSDARP00000099069; -.
PaxDb; Q8JFR5; -.
PRIDE; Q8JFR5; -.
Ensembl; ENSDART00000011135; ENSDARP00000024170; ENSDARG00000043317.
GeneID; 30256; -.
KEGG; dre:30256; -.
CTD; 30256; -.
ZFIN; ZDB-GENE-980526-464; kita.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000112008; -.
HOVERGEN; HBG004335; -.
InParanoid; Q8JFR5; -.
KO; K05091; -.
OMA; PTFKQIV; -.
Reactome; R-DRE-1257604; PIP3 activates AKT signaling.
Reactome; R-DRE-1433557; Signaling by SCF-KIT.
Reactome; R-DRE-1433559; Regulation of KIT signaling.
Reactome; R-DRE-5673001; RAF/MAP kinase cascade.
Reactome; R-DRE-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
PRO; PR:Q8JFR5; -.
Proteomes; UP000000437; Chromosome 20.
Bgee; ENSDARG00000043317; -.
ExpressionAtlas; Q8JFR5; baseline.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019955; F:cytokine binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0048066; P:developmental pigmentation; IMP:ZFIN.
GO; GO:0038093; P:Fc receptor signaling pathway; IEA:InterPro.
GO; GO:0014831; P:gastro-intestinal system smooth muscle contraction; IMP:ZFIN.
GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
GO; GO:1902362; P:melanocyte apoptotic process; IMP:ZFIN.
GO; GO:0030318; P:melanocyte differentiation; IMP:ZFIN.
GO; GO:0097324; P:melanocyte migration; IMP:ZFIN.
GO; GO:0043473; P:pigmentation; IMP:ZFIN.
GO; GO:0048865; P:stem cell fate commitment; IMP:ZFIN.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR027263; SCGF_receptor.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500951; SCGF_recepter; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 3.
SMART; SM00220; S_TKc; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 4.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
2: Evidence at transcript level;
ATP-binding; Cell membrane; Complete proteome; Differentiation;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase;
Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 976 Mast/stem cell growth factor receptor
kita.
/FTId=PRO_0000248880.
TOPO_DOM 22 515 Extracellular. {ECO:0000255}.
TRANSMEM 516 536 Helical. {ECO:0000255}.
TOPO_DOM 537 976 Cytoplasmic. {ECO:0000255}.
DOMAIN 23 105 Ig-like C2-type 1.
DOMAIN 100 199 Ig-like C2-type 2.
DOMAIN 206 301 Ig-like C2-type 3.
DOMAIN 308 402 Ig-like C2-type 4.
DOMAIN 399 504 Ig-like C2-type 5.
DOMAIN 580 922 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 587 594 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 662 668 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 777 777 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
METAL 559 559 Magnesium. {ECO:0000250}.
METAL 782 782 Magnesium. {ECO:0000250}.
METAL 795 795 Magnesium. {ECO:0000250}.
BINDING 614 614 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 781 781 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 559 559 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 561 561 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 691 691 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 707 707 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 808 808 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 921 921 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 315 315 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 449 449 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 477 477 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 89 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 131 180 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 146 177 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 228 285 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 422 488 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 168 168 E -> Q (in Ref. 1; AAD41890).
{ECO:0000305}.
CONFLICT 460 460 V -> L (in Ref. 2; CAD43458/CAI11525).
{ECO:0000305}.
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


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