ID A0A8C6EB80_MOSMO Unreviewed; 973 AA.
AC A0A8C6EB80;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 21.
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|Ensembl:ENSMMSP00000028315.1};
OS Moschus moschiferus (Siberian musk deer) (Moschus sibiricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Moschidae;
OC Moschus.
OX NCBI_TaxID=68415 {ECO:0000313|Ensembl:ENSMMSP00000028315.1, ECO:0000313|Proteomes:UP000694544};
RN [1] {ECO:0000313|Ensembl:ENSMMSP00000028315.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSMMSP00000028315.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SUBUNIT: Monomer in the absence of bound KITLG/SCF. Homodimer in the
CC presence of bound KITLG/SCF, forming a heterotetramer with two
CC KITLG/SCF molecules. Interacts (via phosphorylated tyrosine residues)
CC with the adapter proteins GRB2 and GRB7 (via SH2 domain), and
CC SH2B2/APS. Interacts (via C-terminus) with MPDZ (via the tenth PDZ
CC domain). Interacts (via phosphorylated tyrosine residues) with PIK3R1
CC and PIK3CD. Interacts (via phosphorylated tyrosine) with CRK (isoform
CC Crk-II), FYN, SHC1 and MATK/CHK (via SH2 domain). Interacts with LYN
CC and FES/FPS. Interacts (via phosphorylated tyrosine residues) with the
CC protein phosphatases PTPN6/SHP-1 (via SH2 domain), PTPN11/SHP-2 (via
CC SH2 domain) and PTPRU. Interacts with PLCG1. Interacts with DOK1 and
CC TEC. Interacts with IL1RAP (independent of stimulation with KITLG/SCF).
CC A mast cell-specific KITLG/SCF-induced interleukin-33 signaling complex
CC contains IL1RL1, IL1RAP, KIT and MYD88.
CC {ECO:0000256|ARBA:ARBA00065309}.
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 AlphaFoldDB; A0A8C6EB80; -.
DR Ensembl; ENSMMST00000031193.1; ENSMMSP00000028315.1; ENSMMSG00000021225.1.
DR GeneTree; ENSGT00940000155626; -.
DR Proteomes; UP000694544; Unplaced.
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:0043235; C:receptor complex; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019955; F:cytokine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019838; F:growth factor binding; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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:0030036; P:actin cytoskeleton organization; 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:UniProtKB-UniRule.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IEA:Ensembl.
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: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; IEA:TreeGrafter.
DR GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1905065; P:positive regulation of vascular associated smooth muscle cell differentiation; 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 CDD; cd00096; Ig; 1.
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; 4.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 3: Inferred from homology;
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 Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR500951};
KW Reference proteome {ECO:0000313|Proteomes:UP000694544};
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..973
FT /note="Mast/stem cell growth factor receptor"
FT /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT /id="PRO_5034399436"
FT TRANSMEM 522..545
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT DOMAIN 212..309
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 427..508
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 586..934
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 789
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 565
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 593..600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 668..674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 793
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 794
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 807
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 933
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 973 AA; 109361 MW; BD8296019F8BF4D3 CRC64;
MRGARGAWDF LFVLQLLLRV QTGSSQPSVS PGELSLPSIH PAKSELIVSV GDEIRLLCTD
PGFVKWTFEI LGQLSEKTNP EWITEKAEAT NTGNYTCTNK GGLSSSIYVF VRDPEKLFLI
DLPLYGKEEN DTLVRCPLTD PEVTDYSLTG CEGKPLPKDL TFVADPKAGI TIRNVKREYH
RLCLHCSASQ RGKSMLSKKF TLKVRAAIKA VPVVSVSKTS YLLREGEEFA VTCLIKDVSS
SVDSMWIKEN SQQTKAQTKK NSWHQGDFSY LRQERLTISS ARVNDSGVFM CYANNTFGSA
NVTTTLEVVD KGFINIFPMM NTTVFVNDGE NVDLVVEYEA YPKPEHRQWI YMNRTSTDKW
DDYPKSENES NIRYVNELHL TRLKGTEGGT YTFHVSNSDV NSSVTFNVYV NTKPEILTHD
RLVNGMLQCV AAGFPEPTID WYFCPGTEQR CSVPVGPVDV QIQNSSVSPF GKLVVYSTID
DSTFKHNGTV ECRAYNDVGK SSASFNFAFK EQIHAHTLFT PLLIGFVIAA GLMCIFVMIL
TYKYLQKPMY EVQWKVVEEI NGNNYVYIDP TQLPYDHKWE FPRNRLSFGK TLGAGAFGKV
VEATAYGLIK SDAAMTVAVK MLKPSAHLTE REALMSELKV LSYLGNHMNI VNLLGACTIG
GPTLVITEYC CYGDLLNFLR RKRDSFICSK QEDHAEVALY KNLLHSKESS CNDSTNEYMD
MKPGVSYVVP TKADKRRSAR IGSYIERDVT PAIMEDDELA LDLEDLLSFS YQVAKGMAFL
ASKNCIHRDL AARNILLTHG RITKICDFGL ARDIKNDSNY VVKGNARLPV KWMAPESIFN
CVYTFESDVW SYGIFLWELF SLGSSPYPGM PVDSKFYKMI KEGFRMLSPE HAPAEMYDIM
KTCWDADPLK RPTFKQIVQL IEKQISESTN HIYSNLANCS PHRENPAVDH SVRINSVGSS
ASSTQPLLVH EDV
//
