KIT_MOUSE
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 03-AUG-2022, entry version 223.
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.
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 VARIANTS W37 LYS-586; WV MET-664 AND W41 MET-835.
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 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.
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}.
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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 GlyGen; P05532; 8 sites.
DR iPTMnet; P05532; -.
DR PhosphoSitePlus; P05532; -.
DR MaxQB; P05532; -.
DR PaxDb; P05532; -.
DR PRIDE; P05532; -.
DR ProteomicsDB; 263611; -. [P05532-1]
DR ProteomicsDB; 263612; -. [P05532-2]
DR ProteomicsDB; 263613; -. [P05532-3]
DR ABCD; P05532; 1 sequenced antibody.
DR Antibodypedia; 1392; 5458 antibodies from 57 providers.
DR DNASU; 16590; -.
DR Ensembl; ENSMUST00000005815; ENSMUSP00000005815; ENSMUSG00000005672. [P05532-1]
DR Ensembl; ENSMUST00000144270; ENSMUSP00000116465; ENSMUSG00000005672. [P05532-2]
DR GeneID; 16590; -.
DR KEGG; mmu:16590; -.
DR UCSC; uc008xug.2; mouse. [P05532-1]
DR UCSC; uc012dxj.1; mouse. [P05532-2]
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; KSSAYFN; -.
DR OrthoDB; 236292at2759; -.
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; 1 hit in 75 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 304 other tissues.
DR Genevisible; P05532; MM.
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:0005737; C:cytoplasm; ISO: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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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:0031532; P:actin cytoskeleton reorganization; 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:0097067; P:cellular response to thyroid hormone stimulus; IDA:UniProtKB.
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:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
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:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IGI: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:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA: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:0048103; P:somatic stem cell division; ISO: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:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0008542; P:visual learning; ISO:MGI.
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; 4.
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 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 spotting; impaired protein stability
FT and loss of kinase activity)"
FT /evidence="ECO:0000269|PubMed:1693331,
FT ECO:0000269|PubMed:1714377"
FT VARIANT 664
FT /note="T -> M (in Wv spotting)"
FT /evidence="ECO:0000269|PubMed:1693331"
FT VARIANT 794
FT /note="D -> N (in W42 spotting; loss of kinase activity and
FT impaired 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 spotting; 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
