SCF_MOUSE
ID SCF_MOUSE Reviewed; 273 AA.
AC P20826; P97332; Q3TNJ7; Q62524; Q64222; Q921N5;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Kit ligand;
DE AltName: Full=Hematopoietic growth factor KL;
DE AltName: Full=Mast cell growth factor;
DE Short=MGF;
DE AltName: Full=Steel factor;
DE AltName: Full=Stem cell factor;
DE Short=SCF;
DE AltName: Full=c-Kit ligand;
DE Contains:
DE RecName: Full=Soluble KIT ligand;
DE Short=sKITLG;
DE Flags: Precursor;
GN Name=Kitlg; Synonyms=Kitl, Mgf, Sl, Slf;
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 1).
RC STRAIN=WCB6F1;
RX PubMed=1698558; DOI=10.1016/0092-8674(90)90304-w;
RA Anderson D.M., Lyman S.D., Baird A., Wignall J.M., Eisenman J., Rauch C.,
RA March C.J., Boswell H.S., Gimpel S.D., Cosman D., Williams D.E.;
RT "Molecular cloning of mast cell growth factor, a hematopoietin that is
RT active in both membrane bound and soluble forms.";
RL Cell 63:235-243(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RX PubMed=1378327; DOI=10.1091/mbc.3.3.349;
RA Huang E.J., Nocka K.H., Buck J., Besmer P.;
RT "Differential expression and processing of two cell associated forms of the
RT kit-ligand: KL-1 and KL-2.";
RL Mol. Biol. Cell 3:349-362(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RC STRAIN=WCB6F1;
RX PubMed=1705866; DOI=10.1016/0092-8674(91)90326-t;
RA Flanagan J.G., Chan D.C., Leder P.;
RT "Transmembrane form of the kit ligand growth factor is determined by
RT alternative splicing and is missing in the Sld mutant.";
RL Cell 64:1025-1035(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX PubMed=1383087; DOI=10.1101/gad.6.10.1832;
RA Brannan C.I., Bedell M.A., Resnick J.L., Eppig J.J., Handel M.A.,
RA Williams D.E., Lyman S.D., Donovan P.J., Jenkins N.A., Copeland N.G.;
RT "Developmental abnormalities in Steel17H mice result from a splicing defect
RT in the steel factor cytoplasmic tail.";
RL Genes Dev. 6:1832-1842(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=8849898; DOI=10.1093/genetics/142.3.927;
RA Bedell M.A., Copeland N.G., Jenkins N.A.;
RT "Multiple pathways for Steel regulation suggested by genomic and sequence
RT analysis of the murine Steel gene.";
RL Genetics 142:927-934(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PRO-193 AND SER-207.
RC STRAIN=C3H/E1; TISSUE=Brain;
RX PubMed=8875893; DOI=10.1007/s003359900247;
RA Graw J., Loester J., Neuhaeuser-Klaus A., Pretsch W., Schmitt-John T.;
RT "Molecular analysis of two new Steel mutations in mice shows a transversion
RT or an insertion.";
RL Mamm. Genome 7:843-846(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-122; PRO-193 AND
RP SER-207.
RC STRAIN=102/E1 X C3H/E1;
RX PubMed=9360640; DOI=10.1016/s1383-5726(97)00005-8;
RA Graw J., Neuhauser-Klaus A., Pretsch W.;
RT "Detection of a point mutation (A to G) in exon 5 of the murine Mgf gene
RT defines a novel allele at the Steel locus with a weak phenotype.";
RL Mutat. Res. 382:75-78(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-207.
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 [10]
RP NUCLEOTIDE SEQUENCE OF 1-270 (ISOFORM 1), AND PROTEIN SEQUENCE OF 26-65.
RX PubMed=1698557; DOI=10.1016/0092-8674(90)90303-v;
RA Huang E., Nocka K., Beier D.R., Chu T.Y., Buck J., Lahm H.W., Wellner D.,
RA Leder P., Besmer P.;
RT "The hematopoietic growth factor KL is encoded by the Sl locus and is the
RT ligand of the c-kit receptor, the gene product of the W locus.";
RL Cell 63:225-233(1990).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-201.
RX PubMed=1698556; DOI=10.1016/0092-8674(90)90302-u;
RA Zsebo K.M., Williams D.A., Geissler E.N., Broudy V.C., Martin F.H.,
RA Atkins H.L., Hsu R.-Y., Birkett N.C., Okino K.H., Murdock D.C.,
RA Jacobsen F.W., Langley K.E., Smith K.A., Takeishi T., Cattanach B.M.,
RA Galli S.J., Suggs S.V.;
RT "Stem cell factor is encoded at the Sl locus of the mouse and is the ligand
RT for the c-kit tyrosine kinase receptor.";
RL Cell 63:213-224(1990).
RN [12]
RP PROTEIN SEQUENCE OF 26-53.
RX PubMed=1698554; DOI=10.1016/0092-8674(90)90298-s;
RA Copeland N.G., Gilbert D.J., Cho B.C., Donovan P.J., Jenkins N.A.,
RA Cosman D., Anderson D., Lyman S.D., Williams D.E.;
RT "Mast cell growth factor maps near the steel locus on mouse chromosome 10
RT and is deleted in a number of steel alleles.";
RL Cell 63:175-183(1990).
RN [13]
RP PROTEIN SEQUENCE OF 26-78.
RX PubMed=1698553; DOI=10.1016/0092-8674(90)90297-r;
RA Williams D.E., Eisenman J., Baird A., Rauch C., van Ness K., March C.J.,
RA Park L.S., Martin U., Mochizuki D.Y., Boswell H.S., Burgess G.S.,
RA Cosman D., Lyman S.D.;
RT "Identification of a ligand for the c-kit proto-oncogene.";
RL Cell 63:167-174(1990).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=26522471; DOI=10.1016/j.ajhg.2015.09.011;
RG Baylor-Hopkins Center for Mendelian Genomics;
RA Zazo Seco C., Serrao de Castro L., van Nierop J.W., Morin M., Jhangiani S.,
RA Verver E.J., Schraders M., Maiwald N., Wesdorp M., Venselaar H.,
RA Spruijt L., Oostrik J., Schoots J., van Reeuwijk J., Lelieveld S.H.,
RA Huygen P.L., Insenser M., Admiraal R.J., Pennings R.J., Hoefsloot L.H.,
RA Arias-Vasquez A., de Ligt J., Yntema H.G., Jansen J.H., Muzny D.M.,
RA Huls G., van Rossum M.M., Lupski J.R., Moreno-Pelayo M.A., Kunst H.P.,
RA Kremer H.;
RT "Allelic Mutations of KITLG, Encoding KIT Ligand, Cause Asymmetric and
RT Unilateral Hearing Loss and Waardenburg Syndrome Type 2.";
RL Am. J. Hum. Genet. 97:647-660(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 28-166 ALONE AND IN COMPLEX WITH
RP KIT, SUBUNIT, AND DISULFIDE BONDS.
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).
CC -!- FUNCTION: Ligand for the receptor-type protein-tyrosine kinase KIT.
CC Plays an essential role in the regulation of cell survival and
CC proliferation, hematopoiesis, stem cell maintenance, gametogenesis,
CC mast cell development, migration and function, and in melanogenesis.
CC KITLG/SCF binding can activate several signaling pathways. Promotes
CC phosphorylation of PIK3R1, the regulatory subunit of
CC phosphatidylinositol 3-kinase, and subsequent activation of the kinase
CC AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation
CC of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1.
CC KITLG/SCF and KIT promote activation of STAT family members STAT1,
CC STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading
CC to the production of the cellular signaling molecules diacylglycerol
CC and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with
CC other cytokines, probably interleukins.
CC -!- SUBUNIT: Homodimer, non-covalently linked (Probable). Heterotetramer
CC with KIT, binding two KIT molecules; thereby mediates KIT dimerization
CC and subsequent activation by autophosphorylation.
CC {ECO:0000269|PubMed:17255936, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250}; Single-
CC pass type I membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000250|UniProtKB:P21583}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Cell membrane {ECO:0000250|UniProtKB:P21583}; Single-pass type I
CC membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P21583}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P21583}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:P21583}.
CC -!- SUBCELLULAR LOCATION: [Soluble KIT ligand]: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=KL-1;
CC IsoId=P20826-1; Sequence=Displayed;
CC Name=2; Synonyms=KL-2;
CC IsoId=P20826-2; Sequence=VSP_006023;
CC -!- TISSUE SPECIFICITY: Expressed in the cochlea.
CC {ECO:0000269|PubMed:26522471}.
CC -!- DEVELOPMENTAL STAGE: Acts in the early stages of hematopoiesis.
CC -!- PTM: A soluble form is produced by proteolytic processing of isoform 1
CC in the extracellular domain.
CC -!- SIMILARITY: Belongs to the SCF family. {ECO:0000305}.
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DR EMBL; M59915; AAA40095.1; -; mRNA.
DR EMBL; M57647; AAA39538.1; -; mRNA.
DR EMBL; S40534; AAB22555.2; -; mRNA.
DR EMBL; X68989; CAA48778.1; -; mRNA.
DR EMBL; U44724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U44725; AAC52447.1; -; mRNA.
DR EMBL; X95381; CAA64667.1; -; mRNA.
DR EMBL; X99322; CAA67698.1; -; mRNA.
DR EMBL; Y10287; CAA71329.1; -; mRNA.
DR EMBL; AK018777; BAB31402.1; -; mRNA.
DR EMBL; AK134301; BAE22091.1; -; mRNA.
DR EMBL; AK165233; BAE38091.1; -; mRNA.
DR EMBL; BC011322; AAH11322.1; -; mRNA.
DR EMBL; S40364; AAB22554.2; -; mRNA.
DR EMBL; M59912; AAA39539.1; -; mRNA.
DR CCDS; CCDS36046.1; -. [P20826-1]
DR CCDS; CCDS83751.1; -. [P20826-2]
DR PIR; A35971; A35971.
DR PIR; A37934; A37934.
DR PIR; B35971; B35971.
DR PIR; S65801; S65801.
DR RefSeq; NP_001334085.1; NM_001347156.1. [P20826-2]
DR RefSeq; NP_038626.1; NM_013598.3. [P20826-1]
DR PDB; 2O26; X-ray; 2.50 A; A/B/E/F=28-166.
DR PDB; 2O27; X-ray; 2.20 A; A/B=28-166.
DR PDBsum; 2O26; -.
DR PDBsum; 2O27; -.
DR AlphaFoldDB; P20826; -.
DR SMR; P20826; -.
DR BioGRID; 201412; 1.
DR STRING; 10090.ENSMUSP00000100920; -.
DR GlyGen; P20826; 4 sites.
DR PhosphoSitePlus; P20826; -.
DR MaxQB; P20826; -.
DR PaxDb; P20826; -.
DR PeptideAtlas; P20826; -.
DR PRIDE; P20826; -.
DR ProteomicsDB; 255488; -. [P20826-1]
DR ProteomicsDB; 255489; -. [P20826-2]
DR Antibodypedia; 3883; 890 antibodies from 46 providers.
DR DNASU; 17311; -.
DR Ensembl; ENSMUST00000020129; ENSMUSP00000020129; ENSMUSG00000019966. [P20826-2]
DR Ensembl; ENSMUST00000105283; ENSMUSP00000100920; ENSMUSG00000019966. [P20826-1]
DR GeneID; 17311; -.
DR KEGG; mmu:17311; -.
DR UCSC; uc007gxp.1; mouse. [P20826-1]
DR UCSC; uc007gxq.1; mouse. [P20826-2]
DR CTD; 17311; -.
DR MGI; MGI:96974; Kitl.
DR VEuPathDB; HostDB:ENSMUSG00000019966; -.
DR eggNOG; ENOG502QTGT; Eukaryota.
DR GeneTree; ENSGT00390000018272; -.
DR HOGENOM; CLU_090207_0_0_1; -.
DR InParanoid; P20826; -.
DR OMA; CWISVMV; -.
DR OrthoDB; 1083457at2759; -.
DR PhylomeDB; P20826; -.
DR TreeFam; TF330811; -.
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; 17311; 4 hits in 72 CRISPR screens.
DR EvolutionaryTrace; P20826; -.
DR PRO; PR:P20826; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P20826; protein.
DR Bgee; ENSMUSG00000019966; Expressed in habenula and 308 other tissues.
DR ExpressionAtlas; P20826; baseline and differential.
DR Genevisible; P20826; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005173; F:stem cell factor receptor binding; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IGI:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI.
DR GO; GO:0035162; P:embryonic hemopoiesis; ISO:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0007281; P:germ cell development; TAS:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0033024; P:mast cell apoptotic process; IDA:MGI.
DR GO; GO:0097531; P:mast cell migration; IDA:MGI.
DR GO; GO:0070662; P:mast cell proliferation; IDA:MGI.
DR GO; GO:0097324; P:melanocyte migration; IDA:MGI.
DR GO; GO:0002573; P:myeloid leukocyte differentiation; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
DR GO; GO:0033026; P:negative regulation of mast cell apoptotic process; IDA:MGI.
DR GO; GO:0001755; P:neural crest cell migration; IDA:MGI.
DR GO; GO:0001541; P:ovarian follicle development; ISO:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:1901534; P:positive regulation of hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IDA:MGI.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IDA:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IGI:MGI.
DR GO; GO:0070668; P:positive regulation of mast cell proliferation; IDA:MGI.
DR GO; GO:0045636; P:positive regulation of melanocyte differentiation; IDA:MGI.
DR GO; GO:0002763; P:positive regulation of myeloid leukocyte differentiation; IGI:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:MGI.
DR GO; GO:0042098; P:T cell proliferation; IDA:MGI.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR003452; SCF.
DR PANTHER; PTHR11574; PTHR11574; 1.
DR Pfam; PF02404; SCF; 1.
DR PIRSF; PIRSF015599; SCF; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor; Membrane; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:1698553,
FT ECO:0000269|PubMed:1698554, ECO:0000269|PubMed:1698557"
FT CHAIN 26..273
FT /note="Kit ligand"
FT /id="PRO_0000031914"
FT CHAIN 26..190
FT /note="Soluble KIT ligand"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403392"
FT TOPO_DOM 26..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 190..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..114
FT /evidence="ECO:0000269|PubMed:17255936"
FT DISULFID 68..163
FT /evidence="ECO:0000269|PubMed:17255936"
FT VAR_SEQ 174..202
FT /note="DSRVSVTKPFMLPPVAASSLRNDSSSSNR -> G (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006023"
FT VARIANT 122
FT /note="N -> S (in MGFSL-3NEU)"
FT /evidence="ECO:0000269|PubMed:9360640"
FT VARIANT 193
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:8875893,
FT ECO:0000269|PubMed:9360640"
FT VARIANT 207
FT /note="A -> S"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8875893, ECO:0000269|PubMed:9360640"
FT CONFLICT 215
FT /note="W -> L (in Ref. 2; AAB22555/AAB22554)"
FT /evidence="ECO:0000305"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:2O26"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:2O27"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2O27"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:2O27"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2O27"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:2O27"
FT HELIX 97..118
FT /evidence="ECO:0007829|PDB:2O27"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2O27"
FT HELIX 137..151
FT /evidence="ECO:0007829|PDB:2O27"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:2O26"
SQ SEQUENCE 273 AA; 30645 MW; A7FC899B592A7967 CRC64;
MKKTQTWIIT CIYLQLLLFN PLVKTKEICG NPVTDNVKDI TKLVANLPND YMITLNYVAG
MDVLPSHCWL RDMVIQLSLS LTTLLDKFSN ISEGLSNYSI IDKLGKIVDD LVLCMEENAP
KNIKESPKRP ETRSFTPEEF FSIFNRSIDA FKDFMVASDT SDCVLSSTLG PEKDSRVSVT
KPFMLPPVAA SSLRNDSSSS NRKAAKAPED SGLQWTAMAL PALISLVIGF AFGALYWKKK
QSSLTRAVEN IQINEEDNEI SMLQQKEREF QEV
