KIT_CHICK
ID KIT_CHICK Reviewed; 960 AA.
AC Q08156;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mast/stem cell growth factor receptor Kit;
DE Short=SCFR;
DE EC=2.7.10.1;
DE AltName: Full=Proto-oncogene c-Kit;
DE AltName: Full=Tyrosine-protein kinase Kit;
DE Flags: Precursor;
GN Name=KIT;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Brain;
RX PubMed=7685729; DOI=10.1016/0378-1119(93)90571-j;
RA Sasaki E., Okamura H., Chikamune T., Kanai Y., Watanabe M., Naito M.,
RA Sakurai M.;
RT "Cloning and expression of the chicken c-kit proto-oncogene.";
RL Gene 128:257-261(1993).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC for the cytokine KITLG/SCF and plays an essential role in the
CC regulation of cell survival and proliferation, hematopoiesis, stem cell
CC maintenance, gametogenesis, mast cell development, migration and
CC function, and in melanogenesis. In response to KITLG/SCF binding, KIT
CC can activate several signaling pathways. Promotes phosphorylation of
CC PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and
CC subsequent activation of the kinase AKT1. Activated KIT also transmits
CC signals via GRB2 and activation of RAS, RAF1 and the MAP kinases
CC MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family
CC members STAT1, STAT3, STAT5A and STAT5B. KIT promotes activation of
CC PLCG1, leading to the production of the cellular signaling molecules
CC diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is
CC modulated by protein phosphatases, and by rapid internalization and
CC degradation of the receptor (By similarity). {ECO:0000250}.
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; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: High in the brain and testes and also present in
CC the bursa of Fabricus, heart, kidney, lung, spleen thymus and ovary.
CC -!- PTM: Ubiquitinated. KIT is rapidly ubiquitinated after
CC autophosphorylation induced by KITLG/SCF binding, leading to
CC internalization and degradation. {ECO:0000250}.
CC -!- PTM: Autophosphorylated on tyrosine residues. KITLG/SCF binding
CC promotes autophosphorylation. Phosphorylated tyrosine residues are
CC important for interaction with specific binding partners (By
CC similarity). {ECO:0000250}.
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; D13225; BAA02506.1; -; mRNA.
DR PIR; JN0677; JN0677.
DR RefSeq; NP_989692.1; NM_204361.1.
DR AlphaFoldDB; Q08156; -.
DR SMR; Q08156; -.
DR STRING; 9031.ENSGALP00000022531; -.
DR PaxDb; Q08156; -.
DR Ensembl; ENSGALT00000047850; ENSGALP00000051217; ENSGALG00000038634.
DR GeneID; 378783; -.
DR KEGG; gga:378783; -.
DR CTD; 3815; -.
DR VEuPathDB; HostDB:geneid_378783; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000155626; -.
DR HOGENOM; CLU_000288_49_0_1; -.
DR InParanoid; Q08156; -.
DR OMA; KSSAYFN; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; Q08156; -.
DR BRENDA; 2.7.10.1; 1306.
DR PRO; PR:Q08156; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000038634; Expressed in lung and 11 other tissues.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0005020; F:stem cell factor receptor activity; IEA:Ensembl.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IEA:Ensembl.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0038162; P:erythropoietin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0038093; P:Fc receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
DR GO; GO:0035701; P:hematopoietic stem cell migration; IEA:Ensembl.
DR GO; GO:0002327; P:immature B cell differentiation; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0038109; P:Kit signaling pathway; IBA:GO_Central.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0002320; P:lymphoid progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0002551; P:mast cell chemotaxis; IEA:Ensembl.
DR GO; GO:0043303; P:mast cell degranulation; IEA:Ensembl.
DR GO; GO:0060374; P:mast cell differentiation; IEA:Ensembl.
DR GO; GO:0070662; P:mast cell proliferation; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR GO; GO:0097326; P:melanocyte adhesion; IEA:Ensembl.
DR GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
DR GO; GO:0097324; P:melanocyte migration; IEA:Ensembl.
DR GO; GO:0002318; P:myeloid progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0051093; P:negative regulation of developmental process; IEA:Ensembl.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IEA:Ensembl.
DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
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:0032765; P:positive regulation of mast cell cytokine production; IEA:Ensembl.
DR GO; GO:0070668; P:positive regulation of mast cell proliferation; IEA:Ensembl.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:1905065; P:positive regulation of vascular associated smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
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; 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 Pfam; PF00047; ig; 1.
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; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF56112; SSF56112; 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..960
FT /note="Mast/stem cell growth factor receptor Kit"
FT /id="PRO_0000016756"
FT TOPO_DOM 25..511
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..960
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..102
FT /note="Ig-like C2-type 1"
FT DOMAIN 111..194
FT /note="Ig-like C2-type 2"
FT DOMAIN 201..294
FT /note="Ig-like C2-type 3"
FT DOMAIN 303..396
FT /note="Ig-like C2-type 4"
FT DOMAIN 399..497
FT /note="Ig-like C2-type 5"
FT DOMAIN 575..913
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 777
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 554
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 582..589
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 609
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 657..663
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 554
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 556
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 689
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 706
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 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 126..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 141..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 222..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 414..481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 960 AA; 107312 MW; 0E93850527AB68F6 CRC64;
MEGAHLAWEL AHAVLLLSLI PAGGSVPHEE SSLVVNKGEE LRLKCNEEGP VTWNFQNSDP
SAKTRISNEK EWHTKNATIR DIGRYECKSK GSIVNSFYVF VKDPNVLFLV DSLIYGKEDS
DILLVCPLTD PDVLNFTLRK CDGKPLPKNM TFIPNPQKGI IIKNVQRSFK GCYQCLAKHN
GVEKISEHIF LNVRPVHKAL PVITLSKSYE LLKEGEEFEV TCIITDVDSS VKASWISYKS
AIVTSKSRNL GDYGYERKLT LNIRSVGVND SGEFTCQAEN PFGKTNATVT LKALAKGFVR
LFATMNTTID INAGQNGNLT VEYEAYPKPK EEVWMYMNET LQNSSDHYVK FKTVGNNSYT
SELHLTRLKG TEGGIYTFFV SNSDASSSVT FNVYVKTKPE ILTLDMLGND ILQCVATGFP
APTIYWYFCP GTEQRCLDSP TISPMDVKVS YTNSSVPSFE RILVESTVNA SMFKSTGTIC
CEASSNGDKS SVFFNFAIKE QIRTHTLFTP LLIAFGVAAG LMCIIVMILV YIYLQKPKYE
VQWKVVEEIN GNNYVYIDPT QLPYDHKWEF PRNRLSFGKT LGAGAFGKVV EATAYGLFKS
DAAMTVAVKM LKPSAHLTER EALMSELKVL SYLGNHINIV NLLGACTIGG PTLVITEYCC
YGDLLNFLRR KRDSFICPKH EEHAEAAVYE NLLHQAEPTA DAVNEYMDMK PGVSYAVPPK
ADKKRPVKSG SYTDQDVTLS MLEDDELALD VEDLLSFSYQ VAKGMSFLAS KNCIHRDLAA
RNILLTHGRI TKICDFGLAR DIRNDSNYVV KGNARLPVKW MAPESIFNCV YTFESDVWSY
GILLWELFSL GSSPYPGMPV DSKFYKMIKE GYRMFSPECS PPEMYDIMKS CWDADPLQRP
TFKQIVQLIE QQLSDNAPRV YANFSTPPST QGNATDHSVR INSVGSSASS TQPLLVREDV
