ID KIT_MOUSE Reviewed; 979 AA. AC P05532; Q61415; Q61416; Q61417; Q6LEE9; Q6QJB7; Q6QJB8; Q7TS86; Q8C8K9; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 3. DT 27-MAR-2024, entry version 232. 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 AltName: CD_antigen=CD117; DE Flags: Precursor; GN Name=Kit; Synonyms=Sl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT GLU-207. RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=2456920; DOI=10.1002/j.1460-2075.1988.tb02907.x; RA Qiu F., Ray P., Brown K., Barker P.E., Jhanwar S., Ruddle F.H., Besmer P.; RT "Primary structure of c-kit: relationship with the CSF-1/PDGF receptor RT kinase family -- oncogenic activation of v-kit involves deletion of RT extracellular domain and C-terminus."; RL EMBO J. 7:1003-1011(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata; RX PubMed=1709486; DOI=10.1093/nar/19.6.1267; RA Hayashi S., Kunisada T., Ogawa M., Yamaguchi K., Nishikawa S.; RT "Exon skipping by mutation of an authentic splice site of c-kit gene in W/W RT mouse."; RL Nucleic Acids Res. 19:1267-1271(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), AND TISSUE RP SPECIFICITY. RC STRAIN=ICR; RX PubMed=1378413; DOI=10.1016/0012-1606(92)90172-d; RA Rossi P., Marziali G., Albanesi C., Charlesworth A., Geremia R., RA Sorrentino V.; RT "A novel c-kit transcript, potentially encoding a truncated receptor, RT originates within a kit gene intron in mouse spermatids."; RL Dev. Biol. 152:203-207(1992). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND MUTAGENESIS OF PHE-860. RC STRAIN=C57BL/6J; RX PubMed=15731517; DOI=10.1534/genetics.104.027177; RA Ruan H.B., Zhang N., Gao X.; RT "Identification of a novel point mutation of mouse proto-oncogene c-kit RT through N-ethyl-N-nitrosourea mutagenesis."; RL Genetics 169:819-831(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. RC STRAIN=BALB/cJ; RX PubMed=7682073; DOI=10.1006/bbrc.1993.1301; RA Yasuda H., Galli S.J., Geissler E.N.; RT "Cloning and functional analysis of the mouse c-kit promoter."; RL Biochem. Biophys. Res. Commun. 191:893-901(1993). RN [8] RP FUNCTION, AND SUBUNIT. RX PubMed=1698611; DOI=10.1002/j.1460-2075.1990.tb07528.x; RA Tan J.C., Buck J., Levi E., Besmer P.; RT "Candidate ligand for the c-kit transmembrane kinase receptor: KL, a RT fibroblast derived growth factor stimulates mast cells and erythroid RT progenitors."; RL EMBO J. 9:3287-3294(1990). RN [9] RP FUNCTION IN ACTIVATION OF PLCG1, INTERACTION WITH PLCG1, ALTERNATIVE RP SPLICING, PHOSPHORYLATION, GLYCOSYLATION, AND CHARACTERIZATION OF VARIANTS RP W37 LYS-586 AND W41 MET-835. RX PubMed=1714377; DOI=10.1002/j.1460-2075.1991.tb07784.x; RA Reith A.D., Ellis C., Lyman S.D., Anderson D.M., Williams D.E., RA Bernstein A., Pawson T.; RT "Signal transduction by normal isoforms and W mutant variants of the Kit RT receptor tyrosine kinase."; RL EMBO J. 10:2451-2459(1991). RN [10] RP INTERACTION WITH PIK3R1, AND FUNCTION IN PHOSPHORYLATION OF PIK3R1. RX PubMed=7509796; DOI=10.1016/s0021-9258(17)37564-6; RA Serve H., Hsu Y.C., Besmer P.; RT "Tyrosine residue 719 of the c-kit receptor is essential for binding of the RT P85 subunit of phosphatidylinositol (PI) 3-kinase and for c-kit-associated RT PI 3-kinase activity in COS-1 cells."; RL J. Biol. Chem. 269:6026-6030(1994). RN [11] RP UBIQUITINATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, PHOSPHORYLATION RP AT TYR-825, INTERACTION WITH PIK3R1, CHARACTERIZATION OF VARIANT W42 RP ASN-794, MUTAGENESIS OF TYR-723, AND TISSUE SPECIFICITY. RX PubMed=7527401; DOI=10.1016/s0021-9258(18)31793-9; RA Yee N.S., Hsiau C.W., Serve H., Vosseller K., Besmer P.; RT "Mechanism of down-regulation of c-kit receptor. Roles of receptor tyrosine RT kinase, phosphatidylinositol 3'-kinase, and protein kinase C."; RL J. Biol. Chem. 269:31991-31998(1994). RN [12] RP ALTERNATIVE SPLICING, AND FUNCTION IN ACTIVATION OF PLCG1. RX PubMed=9722617; DOI=10.1083/jcb.142.4.1063; RA Sette C., Bevilacqua A., Geremia R., Rossi P.; RT "Involvement of phospholipase Cgamma1 in mouse egg activation induced by a RT truncated form of the C-kit tyrosine kinase present in spermatozoa."; RL J. Cell Biol. 142:1063-1074(1998). RN [13] RP INTERACTION WITH PTPN6/SHP-1 AND PTPN11/SHP-2, FUNCTION IN PHOSPHORYLATION RP OF PTPN6/SHP-1, AND MUTAGENESIS OF TYR-571 AND TYR-573. RX PubMed=9528781; DOI=10.1128/mcb.18.4.2089; RA Kozlowski M., Larose L., Lee F., Le D.M., Rottapel R., Siminovitch K.A.; RT "SHP-1 binds and negatively modulates the c-Kit receptor by interaction RT with tyrosine 569 in the c-Kit juxtamembrane domain."; RL Mol. Cell. Biol. 18:2089-2099(1998). RN [14] RP REVIEW ON ROLE IN SPERMATOGENESIS AND FERTILITY. RX PubMed=12558531; DOI=10.1046/j.1439-0272.2003.00539.x; RA Rossi P., Dolci S., Sette C., Geremia R.; RT "Molecular mechanisms utilized by alternative c-kit gene products in the RT control of spermatogonial proliferation and sperm-mediated egg RT activation."; RL Andrologia 35:71-78(2003). RN [15] RP INTERACTION WITH FES/FPS. RX PubMed=17595334; DOI=10.1182/blood-2007-02-076471; RA Voisset E., Lopez S., Dubreuil P., De Sepulveda P.; RT "The tyrosine kinase FES is an essential effector of KITD816V proliferation RT signal."; RL Blood 110:2593-2599(2007). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-571; TYR-573; TYR-706 AND RP TYR-938, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Mast cell; RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864; RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., RA Kawakami T., Salomon A.R.; RT "Quantitative time-resolved phosphoproteomic analysis of mast cell RT signaling."; RL J. Immunol. 179:5864-5876(2007). RN [17] RP FUNCTION IN MAST CELL MIGRATION, AND IN SIGNALING VIA FYN. RX PubMed=18725415; DOI=10.1074/jbc.m804077200; RA Samayawardhena L.A., Pallen C.J.; RT "Protein-tyrosine phosphatase alpha regulates stem cell factor-dependent c- RT Kit activation and migration of mast cells."; RL J. Biol. Chem. 283:29175-29185(2008). RN [18] RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX PubMed=18447649; DOI=10.1089/scd.2007.0101; RA Zayas J., Spassov D.S., Nachtman R.G., Jurecic R.; RT "Murine hematopoietic stem cells and multipotent progenitors express RT truncated intracellular form of c-kit receptor."; RL Stem Cells Dev. 17:343-353(2008). RN [19] RP FUNCTION IN MAST CELL DEGRANULATION. RX PubMed=21037083; DOI=10.2353/ajpath.2010.100369; RA Chen S., Burgin S., McDaniel A., Li X., Yuan J., Chen M., Khalaf W., RA Clapp D.W., Yang F.C.; RT "Nf1-/- Schwann cell-conditioned medium modulates mast cell degranulation RT by c-Kit-mediated hyperactivation of phosphatidylinositol 3-kinase."; RL Am. J. Pathol. 177:3125-3132(2010). RN [20] RP INTERACTION WITH IL1RL1 AND IL1RAP, AND SUBUNIT. RX PubMed=20200353; DOI=10.1182/blood-2009-10-247411; RA Drube S., Heink S., Walter S., Loehn T., Grusser M., Gerbaulet A., RA Berod L., Schons J., Dudeck A., Freitag J., Grotha S., Reich D., RA Rudeschko O., Norgauer J., Hartmann K., Roers A., Kamradt T.; RT "The receptor tyrosine kinase c-Kit controls IL-33 receptor signaling in RT mast cells."; RL Blood 115:3899-3906(2010). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Lung, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [22] RP VARIANT GLU-207. RA Jawad-Alam J.; RL Unpublished observations (APR-2010). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-314 IN COMPLEX WITH KITLG/SCF, RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-296 AND ASN-303. RX PubMed=17255936; DOI=10.1038/sj.emboj.7601545; RA Liu H., Chen X., Focia P.J., He X.; RT "Structural basis for stem cell factor-KIT signaling and activation of RT class III receptor tyrosine kinases."; RL EMBO J. 26:891-901(2007). RN [24] RP VARIANT W42 ASN-794, AND INVOLVEMENT IN WHITE-SPOTTING PHENOTYPE. RX PubMed=1688471; DOI=10.1126/science.1688471; RA Tan J.C., Nocka K., Ray P., Traktman P., Besmer P.; RT "The dominant W42 spotting phenotype results from a missense mutation in RT the c-kit receptor kinase."; RL Science 247:209-212(1990). RN [25] RP VARIANT W37 LYS-586, VARIANT WV MET-664, VARIANT W41 MET-835, AND RP INVOLVEMENT IN WHITE-SPOTTING PHENOTYPE. RX PubMed=1693331; DOI=10.1002/j.1460-2075.1990.tb08305.x; RA Nocka K., Tan J.C., Chiu E., Chu T.Y., Ray P., Traktman P., Besmer P.; RT "Molecular bases of dominant negative and loss of function mutations at the RT murine c-kit/white spotting locus: W37, Wv, W41 and W."; RL EMBO J. 9:1805-1813(1990). CC -!- FUNCTION: Tyrosine-protein kinase that acts as a 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. Phosphorylates PIK3R1, PLCG1, CC SH2B2/APS and CBL. Activates the AKT1 signaling pathway by CC phosphorylation of PIK3R1, the regulatory subunit of CC phosphatidylinositol 3-kinase. Activated KIT also transmits signals via CC GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or CC MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, CC STAT5A and STAT5B. Activation of PLCG1 leads to the production of the CC cellular signaling molecules diacylglycerol and inositol 1,4,5- CC trisphosphate. KIT signaling is modulated by protein phosphatases, and CC by rapid internalization and degradation of the receptor. Activated KIT CC promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and CC PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and CC STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), CC LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1. CC {ECO:0000269|PubMed:1698611, ECO:0000269|PubMed:1714377, CC ECO:0000269|PubMed:18725415, ECO:0000269|PubMed:21037083, CC ECO:0000269|PubMed:7509796, ECO:0000269|PubMed:9528781, CC ECO:0000269|PubMed:9722617}. 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 ECO:0000269|PubMed:7527401}; CC -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence CC of bound ligand. KITLG/SCF binding leads to dimerization and activation CC by autophosphorylation. 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 the CC protein phosphatases PTPN6/SHP-1 (via SH2 domain), PTPN11/SHP-2 (via CC SH2 domain) and PTPRU. Interacts with DOK1 and TEC (By similarity). CC Interacts with the protein kinase FES/FPS. Interacts with PLCG1. CC Interacts (via phosphorylated tyrosine residues) with PIK3R1 and PIK3 CC catalytic subunit. Interacts (KITLG/SCF-bound) with IL1RL1. Interacts CC with IL1RAP (independent of stimulation with KITLG/SCF). A mast cell- CC specific KITLG/SCF-induced interleukin-33 signaling complex contains CC IL1RL1, IL1RAP, KIT and MYD88. {ECO:0000250|UniProtKB:P10721, CC ECO:0000269|PubMed:1698611, ECO:0000269|PubMed:1714377, CC ECO:0000269|PubMed:17255936, ECO:0000269|PubMed:17595334, CC ECO:0000269|PubMed:20200353, ECO:0000269|PubMed:7509796, CC ECO:0000269|PubMed:7527401, ECO:0000269|PubMed:9528781}. CC -!- INTERACTION: CC P05532; P26955: Csf2rb; NbExp=4; IntAct=EBI-8559255, EBI-1810026; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I CC membrane protein. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I CC membrane protein. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Note=Detected in the CC cytoplasm of spermatozoa, especially in the equatorial and subacrosomal CC region of the sperm head. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=GNNK(+), KitA(+); CC IsoId=P05532-1; Sequence=Displayed; CC Name=2; Synonyms=GNNK(-), Kit(+); CC IsoId=P05532-2; Sequence=VSP_041870; CC Name=3; Synonyms=Tr-kit, Truncated; CC IsoId=P05532-3; Sequence=VSP_041868, VSP_041869; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are detected in bone marrow CC cells, spermatogonia and spermatocytes, but not in round spermatids, CC elongating spermatids and spermatozoa. Isoform 3 is detected in round CC spermatids, elongating spermatids and spermatozoa, but not in CC spermatogonia and spermatocytes (at protein level). Isoform 1 is widely CC expressed and detected in fetal liver and bone marrow. Isoform 3 is CC detected in bone marrow cells enriched in hematopoietic stem cells. CC {ECO:0000269|PubMed:1378413, ECO:0000269|PubMed:18447649, CC ECO:0000269|PubMed:7527401}. CC -!- PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after CC autophosphorylation induced by KITLG/SCF binding, leading to CC internalization and degradation (By similarity). {ECO:0000250}. CC -!- PTM: Autophosphorylated on tyrosine residues. KITLG/SCF binding CC promotes autophosphorylation of isoform 1 and isoform 2. Isoform 1 CC shows low levels of tyrosine phosphorylation in the absence of added CC KITLG/SCF, while isoform 2 requires stimulation by KITLG/SCF for CC phosphorylation (in vitro). Phosphorylation of Tyr-573 is required for CC interaction with PTPN6/SHP-1. Phosphorylation of Tyr-571 is required CC for interaction with PTPN11/SHP-2. Phosphorylated tyrosine residues are CC important for interaction with specific binding partners. CC {ECO:0000269|PubMed:1714377, ECO:0000269|PubMed:7527401}. CC -!- DISEASE: Note=Defects in Kit are the cause of the white-spotting CC phenotype (W). White-spotting variants induces severe effects on CC pigmentation, gametogenesis and hematopoiesis. Mice homozygous for W42 CC die perinatally of macrocytic anemia. {ECO:0000269|PubMed:1688471, CC ECO:0000269|PubMed:1693331}. CC -!- MISCELLANEOUS: Numerous proteins are phosphorylated in response to KIT CC signaling, but it is not evident to determine which are directly CC phosphorylated by KIT under in vivo conditions. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y00864; CAA68772.1; -; mRNA. DR EMBL; AK046795; BAC32872.1; -; mRNA. DR EMBL; X65997; CAA46798.1; -; mRNA. DR EMBL; X65998; CAA46799.1; ALT_SEQ; Genomic_DNA. DR EMBL; X65998; CAA46800.1; -; Genomic_DNA. DR EMBL; AY536430; AAS45606.1; -; mRNA. DR EMBL; AY536431; AAS45607.1; -; mRNA. DR EMBL; AC013622; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC115853; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC052457; AAH52457.1; -; mRNA. DR EMBL; BC075716; AAH75716.1; -; mRNA. DR EMBL; L11358; AAA37420.1; -; Genomic_DNA. DR CCDS; CCDS51525.1; -. [P05532-1] DR CCDS; CCDS80302.1; -. [P05532-2] DR PIR; A44876; A44876. DR PIR; S00474; TVMSKT. DR PIR; S24667; S24667. DR PIR; S34435; S34435. DR RefSeq; NP_001116205.1; NM_001122733.1. [P05532-1] DR RefSeq; NP_066922.2; NM_021099.3. [P05532-2] DR PDB; 2O26; X-ray; 2.50 A; U/W/X/Y=25-314. DR PDBsum; 2O26; -. DR AlphaFoldDB; P05532; -. DR SMR; P05532; -. DR BioGRID; 200957; 36. DR CORUM; P05532; -. DR DIP; DIP-59622N; -. DR IntAct; P05532; 5. DR MINT; P05532; -. DR STRING; 10090.ENSMUSP00000005815; -. DR BindingDB; P05532; -. DR ChEMBL; CHEMBL2034798; -. DR DrugCentral; P05532; -. DR GlyCosmos; P05532; 8 sites, No reported glycans. DR GlyGen; P05532; 9 sites, 1 O-linked glycan (1 site). DR iPTMnet; P05532; -. DR PhosphoSitePlus; P05532; -. DR SwissPalm; P05532; -. DR MaxQB; P05532; -. DR PaxDb; 10090-ENSMUSP00000005815; -. DR ProteomicsDB; 263611; -. [P05532-1] DR ProteomicsDB; 263612; -. [P05532-2] DR ProteomicsDB; 263613; -. [P05532-3] DR ABCD; P05532; 1 sequenced antibody. DR Antibodypedia; 1392; 6193 antibodies from 58 providers. DR DNASU; 16590; -. DR Ensembl; ENSMUST00000005815.7; ENSMUSP00000005815.7; ENSMUSG00000005672.13. [P05532-1] DR Ensembl; ENSMUST00000144270.8; ENSMUSP00000116465.3; ENSMUSG00000005672.13. [P05532-2] DR GeneID; 16590; -. DR KEGG; mmu:16590; -. DR UCSC; uc008xug.2; mouse. [P05532-1] DR UCSC; uc012dxj.1; mouse. [P05532-2] DR AGR; MGI:96677; -. DR CTD; 3815; -. DR MGI; MGI:96677; Kit. DR VEuPathDB; HostDB:ENSMUSG00000005672; -. DR eggNOG; KOG0200; Eukaryota. DR GeneTree; ENSGT00940000155626; -. DR HOGENOM; CLU_000288_49_0_1; -. DR InParanoid; P05532; -. DR OMA; SSAYFNF; -. DR OrthoDB; 1614410at2759; -. DR TreeFam; TF325768; -. DR BRENDA; 2.7.10.1; 3474. DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling. DR Reactome; R-MMU-1433557; Signaling by SCF-KIT. DR Reactome; R-MMU-1433559; Regulation of KIT signaling. DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade. DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR BioGRID-ORCS; 16590; 2 hits in 80 CRISPR screens. DR ChiTaRS; Kit; mouse. DR EvolutionaryTrace; P05532; -. DR PRO; PR:P05532; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; P05532; Protein. DR Bgee; ENSMUSG00000005672; Expressed in cerebellum lobe and 308 other cell types or tissues. DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0005911; C:cell-cell junction; IDA:MGI. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0001650; C:fibrillar center; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. 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; ISS:UniProtKB. DR GO; GO:0019838; F:growth factor binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI. DR GO; GO:0042169; F:SH2 domain binding; IPI:BHF-UCL. DR GO; GO:0005020; F:stem cell factor receptor activity; IDA:MGI. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0030183; P:B cell differentiation; IBA:GO_Central. DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; TAS:MGI. DR GO; GO:0008283; P:cell population proliferation; IGI:MGI. DR GO; GO:0006935; P:chemotaxis; TAS:MGI. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI. DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:UniProtKB. DR GO; GO:0048066; P:developmental pigmentation; IMP:MGI. DR GO; GO:0048565; P:digestive tract development; IMP:UniProtKB. DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI. DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:UniProtKB. DR GO; GO:0050673; P:epithelial cell proliferation; ISO:MGI. DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB. DR GO; GO:0038162; P:erythropoietin-mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0038093; P:Fc receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0007281; P:germ cell development; TAS:MGI. DR GO; GO:0008354; P:germ cell migration; ISO:MGI. DR GO; GO:0006687; P:glycosphingolipid metabolic process; IMP:MGI. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central. DR GO; GO:0035701; P:hematopoietic stem cell migration; IMP:MGI. DR GO; GO:0030097; P:hemopoiesis; IMP:MGI. DR GO; GO:0002327; P:immature B cell differentiation; IMP:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; IDA:MGI. DR GO; GO:0038109; P:Kit signaling pathway; ISO:MGI. DR GO; GO:0030032; P:lamellipodium assembly; IDA:UniProtKB. DR GO; GO:0002320; P:lymphoid progenitor cell differentiation; IGI:MGI. DR GO; GO:0008584; P:male gonad development; IEA:Ensembl. DR GO; GO:0002551; P:mast cell chemotaxis; ISO:MGI. DR GO; GO:0043303; P:mast cell degranulation; ISS:UniProtKB. DR GO; GO:0060374; P:mast cell differentiation; IMP:UniProtKB. DR GO; GO:0070662; P:mast cell proliferation; IGI:MGI. DR GO; GO:0035855; P:megakaryocyte development; IMP:UniProtKB. DR GO; GO:0097326; P:melanocyte adhesion; IDA:UniProtKB. DR GO; GO:0030318; P:melanocyte differentiation; IMP:UniProtKB. DR GO; GO:0097324; P:melanocyte migration; IMP:UniProtKB. DR GO; GO:0002318; P:myeloid progenitor cell differentiation; IGI:MGI. DR GO; GO:0051093; P:negative regulation of developmental process; IMP:MGI. DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:MGI. DR GO; GO:2000242; P:negative regulation of reproductive process; IMP:MGI. DR GO; GO:0001541; P:ovarian follicle development; IMP:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0043473; P:pigmentation; IMP:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. DR GO; GO:1904343; P:positive regulation of colon smooth muscle contraction; ISO:MGI. DR GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI. DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISO:MGI. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI. DR GO; GO:0032765; P:positive regulation of mast cell cytokine production; ISS:UniProtKB. DR GO; GO:0070668; P:positive regulation of mast cell proliferation; IGI:MGI. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:MGI. DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:MGI. DR GO; GO:0120072; P:positive regulation of pyloric antrum smooth muscle contraction; ISO:MGI. DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI. DR GO; GO:1904349; P:positive regulation of small intestine smooth muscle contraction; ISO:MGI. DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI. DR GO; GO:1905065; P:positive regulation of vascular associated smooth muscle cell differentiation; ISO:MGI. DR GO; GO:0012501; P:programmed cell death; IGI:MGI. DR GO; GO:1904251; P:regulation of bile acid metabolic process; ISO:MGI. DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0009314; P:response to radiation; IMP:MGI. DR GO; GO:0035019; P:somatic stem cell population maintenance; ISO:MGI. DR GO; GO:0007286; P:spermatid development; IMP:MGI. DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB. DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB. DR GO; GO:0030217; P:T cell differentiation; IMP:UniProtKB. DR GO; GO:0043586; P:tongue development; IEA:Ensembl. DR GO; GO:0008542; P:visual learning; ISO:MGI. DR CDD; cd00096; Ig; 1. DR CDD; cd05860; IgI_4_SCFR; 1. DR CDD; cd05104; PTKc_Kit; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 5. 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. 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 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; 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; 3. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF48726; Immunoglobulin; 4. 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. DR Genevisible; P05532; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; KW Disease variant; Disulfide bond; Glycoprotein; Immunoglobulin domain; KW Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; KW Phosphoprotein; Proto-oncogene; Receptor; Reference proteome; Repeat; KW Signal; Transferase; Transmembrane; Transmembrane helix; KW Tyrosine-protein kinase; Ubl conjugation. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..979 FT /note="Mast/stem cell growth factor receptor Kit" FT /id="PRO_0000016755" FT TOPO_DOM 25..527 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 528..548 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 549..979 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 31..117 FT /note="Ig-like C2-type 1" FT DOMAIN 126..210 FT /note="Ig-like C2-type 2" FT DOMAIN 217..315 FT /note="Ig-like C2-type 3" FT DOMAIN 324..417 FT /note="Ig-like C2-type 4" FT DOMAIN 420..514 FT /note="Ig-like C2-type 5" FT DOMAIN 592..939 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 571..573 FT /note="Important for interaction with phosphotyrosine- FT binding proteins" FT /evidence="ECO:0000250" FT ACT_SITE 794 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 571 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 599..606 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 626 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 674..680 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 798 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 799 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 812 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT SITE 938 FT /note="Important for interaction with phosphotyrosine- FT binding proteins" FT /evidence="ECO:0000250" FT MOD_RES 550 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P10721" FT MOD_RES 556 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P10721" FT MOD_RES 571 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 573 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 706 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 720 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 723 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P10721" FT MOD_RES 732 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P10721" FT MOD_RES 743 FT /note="Phosphoserine; by PKC/PRKCA" FT /evidence="ECO:0000250|UniProtKB:P10721" FT MOD_RES 748 FT /note="Phosphoserine; by PKC/PRKCA" FT /evidence="ECO:0000250|UniProtKB:P10721" FT MOD_RES 823 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10721" FT MOD_RES 825 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:7527401" FT MOD_RES 893 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10721" FT MOD_RES 902 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P10721" FT MOD_RES 938 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 962 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10721" FT CARBOHYD 146 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 296 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:17255936" FT CARBOHYD 303 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:17255936" FT CARBOHYD 323 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 355 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 370 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 466 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 489 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 58..98 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:17255936" FT DISULFID 137..187 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:17255936" FT DISULFID 152..184 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:17255936" FT DISULFID 234..293 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:17255936" FT DISULFID 431..494 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1..12 FT /note="MRGARGAWDLLC -> MAVAVFPFLPQQ (in isoform 3)" FT /evidence="ECO:0000303|PubMed:1378413" FT /id="VSP_041868" FT VAR_SEQ 13..789 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:1378413" FT /id="VSP_041869" FT VAR_SEQ 512..515 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15731517, ECO:0000303|PubMed:2456920" FT /id="VSP_041870" FT VARIANT 207 FT /note="A -> E (loss-of-function mutation abolishing ligand FT binding)" FT /evidence="ECO:0000269|PubMed:2456920, ECO:0000269|Ref.22" FT VARIANT 586 FT /note="E -> K (in W37; impaired protein stability and loss FT of kinase activity)" FT /evidence="ECO:0000269|PubMed:1693331, FT ECO:0000269|PubMed:1714377" FT VARIANT 664 FT /note="T -> M (in Wv)" FT /evidence="ECO:0000269|PubMed:1693331" FT VARIANT 794 FT /note="D -> N (in W42; loss of kinase activity and impaired FT internalization after exposure to KITLG/SCF)" FT /evidence="ECO:0000269|PubMed:1688471, FT ECO:0000269|PubMed:7527401" FT VARIANT 835 FT /note="V -> M (in W41; decreased kinase activity)" FT /evidence="ECO:0000269|PubMed:1693331, FT ECO:0000269|PubMed:1714377" FT MUTAGEN 571 FT /note="Y->F: Abolishes interaction with PTPN11/SHP-2." FT /evidence="ECO:0000269|PubMed:9528781" FT MUTAGEN 573 FT /note="Y->F: Abolishes interaction with PTPN6/SHP-1." FT /evidence="ECO:0000269|PubMed:9528781" FT MUTAGEN 573 FT /note="Missing: Abolishes interaction with PTPN6/SHP-1." FT /evidence="ECO:0000269|PubMed:9528781" FT MUTAGEN 723 FT /note="Y->F: Abolishes interaction with PIK3R1." FT /evidence="ECO:0000269|PubMed:7527401" FT MUTAGEN 860 FT /note="F->S: Mice display white fur, hearing loss, anemia FT and mast cell deficiency, plus sterility in both males and FT females." FT /evidence="ECO:0000269|PubMed:15731517" FT CONFLICT 551 FT /note="L -> F (in Ref. 6; AAH52457)" FT /evidence="ECO:0000305" FT CONFLICT 781 FT /note="G -> A (in Ref. 1; CAA68772 and 2; CAA46799)" FT /evidence="ECO:0000305" FT CONFLICT 860 FT /note="F -> S (in Ref. 4; AAS45607)" FT /evidence="ECO:0000305" FT STRAND 38..41 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 43..49 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 54..59 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 63..69 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 80..85 FT /evidence="ECO:0007829|PDB:2O26" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 94..103 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 105..113 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 125..128 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 145..151 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 162..166 FT /evidence="ECO:0007829|PDB:2O26" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 170..175 FT /evidence="ECO:0007829|PDB:2O26" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 194..197 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 201..206 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 230..240 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 244..256 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 264..268 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 271..282 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 285..287 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 289..296 FT /evidence="ECO:0007829|PDB:2O26" FT STRAND 301..308 FT /evidence="ECO:0007829|PDB:2O26" SQ SEQUENCE 979 AA; 109343 MW; 03FB4D672248585E CRC64; MRGARGAWDL LCVLLVLLRG QTATSQPSAS PGEPSPPSIH PAQSELIVEA GDTLSLTCID PDFVRWTFKT YFNEMVENKK NEWIQEKAEA TRTGTYTCSN SNGLTSSIYV FVRDPAKLFL VGLPLFGKED SDALVRCPLT DPQVSNYSLI ECDGKSLPTD LTFVPNPKAG ITIKNVKRAY HRLCVRCAAQ RDGTWLHSDK FTLKVRAAIK AIPVVSVPET SHLLKKGDTF TVVCTIKDVS TSVNSMWLKM NPQPQHIAQV KHNSWHRGDF NYERQETLTI SSARVDDSGV FMCYANNTFG SANVTTTLKV VEKGFINISP VKNTTVFVTD GENVDLVVEY EAYPKPEHQQ WIYMNRTSAN KGKDYVKSDN KSNIRYVNQL RLTRLKGTEG GTYTFLVSNS DASASVTFNV YVNTKPEILT YDRLINGMLQ CVAEGFPEPT IDWYFCTGAE QRCTTPVSPV DVQVQNVSVS PFGKLVVQSS IDSSVFRHNG TVECKASNDV GKSSAFFNFA FKGNNKEQIQ AHTLFTPLLI GFVVAAGAMG IIVMVLTYKY LQKPMYEVQW KVVEEINGNN YVYIDPTQLP YDHKWEFPRN RLSFGKTLGA GAFGKVVEAT AYGLIKSDAA MTVAVKMLKP SAHLTEREAL MSELKVLSYL GNHMNIVNLL GACTVGGPTL VITEYCCYGD LLNFLRRKRD SFIFSKQEEQ AEAALYKNLL HSTEPSCDSS NEYMDMKPGV SYVVPTKTDK RRSARIDSYI ERDVTPAIME DDELALDLDD LLSFSYQVAK GMAFLASKNC IHRDLAARNI LLTHGRITKI CDFGLARDIR NDSNYVVKGN ARLPVKWMAP ESIFSCVYTF ESDVWSYGIF LWELFSLGSS PYPGMPVDSK FYKMIKEGFR MVSPEHAPAE MYDVMKTCWD ADPLKRPTFK QVVQLIEKQI SDSTKHIYSN LANCNPNPEN PVVVDHSVRV NSVGSSASST QPLLVHEDA //