ID A0A671DYY4_RHIFE Unreviewed; 972 AA.
AC A0A671DYY4;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 29.
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:ENSRFEP00010006085.1};
GN ORFNames=mRhiFer1_007374 {ECO:0000313|EMBL:KAF6371908.1};
OS Rhinolophus ferrumequinum (Greater horseshoe bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Rhinolophoidea;
OC Rhinolophidae; Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=59479 {ECO:0000313|Ensembl:ENSRFEP00010006085.1, ECO:0000313|Proteomes:UP000472240};
RN [1] {ECO:0000313|Ensembl:ENSRFEP00010006085.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25689317; DOI=10.1146/annurev-animal-090414-014900;
RA Koepfli K.P., Paten B., O'Brien S.J., Koepfli K.P., Paten B., Antunes A.,
RA Belov K., Bustamante C., Castoe T.A., Clawson H., Crawford A.J.,
RA Diekhans M., Distel D., Durbin R., Earl D., Fujita M.K., Gamble T.,
RA Georges A., Gemmell N., Gilbert M.T., Graves J.M., Green R.E., Hickey G.,
RA Jarvis E.D., Johnson W., Komissarov A., Korf I., Kuhn R., Larkin D.M.,
RA Lewin H., Lopez J.V., Ma J., Marques-Bonet T., Miller W., Murphy R.,
RA Pevzner P., Shapiro B., Steiner C., Tamazian G., Venkatesh B., Wang J.,
RA Wayne R., Wiley E., Yang H., Zhang G., Haussler D., Ryder O., O'Brien S.J.;
RT "The Genome 10K Project: a way forward.";
RL Annu Rev Anim Biosci 3:57-111(2015).
RN [2] {ECO:0000313|Ensembl:ENSRFEP00010006085.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=29166127; DOI=10.1146/annurev-animal-022516-022811;
RA Teeling E.C., Vernes S.C., Davalos L.M., Ray D.A., Gilbert M.T.P.,
RA Myers E.;
RT "Bat Biology, Genomes, and the Bat1K Project: To Generate Chromosome-Level
RT Genomes for All Living Bat Species.";
RL Annu Rev Anim Biosci 6:23-46(2018).
RN [3] {ECO:0000313|Ensembl:ENSRFEP00010006085.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Teeling E., Myers G., Vernes S., Pippel M., Winkler S., Fedrigo O.,
RA Rhie A., Koren S., Phillippy A., Lewin H., Damas J., Howe K.,
RA Mountcastle J., Jarvis E.D.;
RT "G10K-VGP greater horseshoe bat female genome, primary haplotype.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:KAF6371908.1, ECO:0000313|Proteomes:UP000585614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRhiFer1 {ECO:0000313|EMBL:KAF6371908.1};
RC TISSUE=Lung {ECO:0000313|EMBL:KAF6371908.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
RN [5] {ECO:0000313|Ensembl:ENSRFEP00010006085.1}
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; JACAGC010000004; KAF6371908.1; -; Genomic_DNA.
DR RefSeq; XP_032962311.1; XM_033106420.1.
DR AlphaFoldDB; A0A671DYY4; -.
DR Ensembl; ENSRFET00010006675.1; ENSRFEP00010006085.1; ENSRFEG00010004158.1.
DR GeneID; 117022389; -.
DR CTD; 3815; -.
DR GeneTree; ENSGT00940000155626; -.
DR OMA; CDSTNEY; -.
DR Proteomes; UP000472240; Chromosome 5.
DR Proteomes; UP000585614; Unassembled WGS sequence.
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; 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; 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; 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 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:UP000472240};
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..972
FT /note="Mast/stem cell growth factor receptor"
FT /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT /id="PRO_5044535961"
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 586..933
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 788
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 792
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 793
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 806
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 932
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 972 AA; 109066 MW; 6F84DDFBD33F65E5 CRC64;
MRGARGAWDF LCVLLLLLGL QTGSSQPSVS PGELSPPSIE PAKSELIVSV GDEIRLLCTD
PGFVKWTFET LGQLSEKTHN EWIMEKAEAT NTGNYTCTNE GGLSSSIYVF VRDPAKLFLI
DLPLYGKEGN DTLVRCPLTD PDVTDYSLTG CEGKPLPQDL TFVADPKAGI TIRNVKREYH
RLCLHCSAYK KGKSVLSKKF TLKVRAAIRA VPVVSVSKAS YLLREGEEFT VTCLIKDVSS
SVYSMWIKEN SQQTKAQVMS NSRHQGDFSF VRQERLTISS ARVNDSGVFM CYANNTFGSA
NVTTTLEVVD KGFINIFPMA NTTIFVNDGE NVDLIVEYEA YPKPDHQQWI YMNKTFTDKW
ENYPKSENES NIRYVTELHL TRLKGTEGGI YTFLVSNSDA NSSVTFNVYV NTKPEILIRE
RLMNGLLQCV AAGFPEPTID WYFCPGIEQR CSVPVGPVDR QMQNSSVSPF GKLVVQSSID
YNSFKFNGTV ECRAYNDVGK SSAFFNFAIK EQIHAHTLFT PLLIGFVIAA GMMCIIVMIL
TYKYLQKPMY EVQWKVVEEI NGNNYVYIDP TQLPYDHKWE FPRNRLSFGK TLGAGAFGKV
VEATAYGLIK SDAAMTVAVK MLKPSAHLTE REALMSELKV LSYLGNHMNI VNLLGACTIG
GPTLVITEYC CYGDLLNFLR RKRDSFICSK QEDHAEAALY KNLLHSKETS CDSTNEYMDM
KPGVSYVVPT KADKRRSARI GSYIERDVTP AIMEDDELAL DLEDLLSFSY QVAKGMAFLA
SKNCIHRDLA ARNILLTHGR ITKICDFGLA RDIKNDSNYV VKGNARLPVK WMAPESIFNC
VYTFESDVWS YGIFLWELFS LGSSPYPGMP VDSKFYKMIK EGFRMLSPEH APADMYDIMM
TCWDADPLKR PTFKQIVQLI EKQISDSTNH IYSNLANWSP NQDSTVVDHS VRINSVGSSA
SSTQPLLVHE DV
//
