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Kit ligand (Mast cell growth factor) (MGF) (Stem cell factor) (SCF) (c-Kit ligand) [Cleaved into: Soluble KIT ligand (sKITLG)]

 SCF_HUMAN               Reviewed;         273 AA.
P21583; A0AV09; A8K2Q4; B7ZLM4; Q16487; Q68DZ2; Q7M4N8; Q9UQK7;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
27-SEP-2017, entry version 169.
RecName: Full=Kit ligand;
AltName: Full=Mast cell growth factor;
Short=MGF;
AltName: Full=Stem cell factor;
Short=SCF;
AltName: Full=c-Kit ligand;
Contains:
RecName: Full=Soluble KIT ligand;
Short=sKITLG;
Flags: Precursor;
Name=KITLG; Synonyms=MGF, SCF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2208279; DOI=10.1016/0092-8674(90)90301-T;
Martin F.H., Suggs S.V., Langley K.E., Lu H.S., Ting J., Okino K.H.,
Morris C.F., McNiece I.K., Jacobsen F.W., Mendiaz E.A., Birkett N.C.,
Smith K.A., Johnson M.J., Parker V.P., Flores J.C., Patel A.C.,
Fisher E.F., Erjavec H.O., Herrera C.J., Wypych J., Sachdev R.K.,
Pope J.A., Leslie I., Wen D., Lin C.-H., Cupples R.L., Zsebo K.M.;
"Primary structure and functional expression of rat and human stem
cell factor DNAs.";
Cell 63:203-211(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1724381;
Anderson D.M., Williams D.E., Tushinski R., Gimpel S., Eisenman J.,
Cannizzaro L.A., Aronson M., Croce C.M., Huebner K., Cosman D.;
"Alternate splicing of mRNAs encoding human mast cell growth factor
and localization of the gene to chromosome 12q22-q24.";
Cell Growth Differ. 2:373-378(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10049787; DOI=10.1006/bbrc.1999.0260;
Blair H.C., Julian B.A., Cao X., Jordan S.E., Dong S.S.;
"Parathyroid hormone-regulated production of stem cell factor in human
osteoblasts and osteoblast-like cells.";
Biochem. Biophys. Res. Commun. 255:778-784(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Han C., Peng X., Yuan J., Qiang B.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Tongue, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 26-40; 64-79; 87-102; 110-149 AND 154-190 (ISOFORM
1), DISULFIDE BONDS, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND
GLYCOSYLATION AT ASN-90; ASN-118; ASN-145; SER-167; THR-168 AND
THR-180.
PubMed=1381905; DOI=10.1016/0003-9861(92)90106-7;
Lu H.S., Clogston C.L., Wypych J., Parker V.P., Lee T.D., Swiderek K.,
Baltera R.F. Jr., Patel A.C., Chang D.C., Brankow D.W., Liu X.-D.,
Ogden S.G., Karkare S.B., Hu S.S., Zsebo K.M., Langley K.E.;
"Post-translational processing of membrane-associated recombinant
human stem cell factor expressed in Chinese hamster ovary cells.";
Arch. Biochem. Biophys. 298:150-158(1992).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 167-248 (ISOFORM 2).
PubMed=1379846;
Toyota M., Hinoda Y., Itoh F., Tsujisaki M., Imai K., Yachi A.;
"Expression of two types of kit ligand mRNAs in human tumor cells.";
Int. J. Hematol. 55:301-304(1992).
[11]
REVIEW.
PubMed=10582791; DOI=10.1093/humupd/5.5.535;
Mauduit C., Hamamah S., Benahmed M.;
"Stem cell factor/c-kit system in spermatogenesis.";
Hum. Reprod. Update 5:535-545(1999).
[12]
REVIEW.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[13]
REVIEW.
PubMed=15625120; DOI=10.1634/stemcells.2004-0117;
Lennartsson J., Jelacic T., Linnekin D., Shivakrupa R.;
"Normal and oncogenic forms of the receptor tyrosine kinase kit.";
Stem Cells 23:16-43(2005).
[14]
INVOLVEMENT IN SHEP7.
PubMed=17952075; DOI=10.1038/ng.2007.13;
Sulem P., Gudbjartsson D.F., Stacey S.N., Helgason A., Rafnar T.,
Magnusson K.P., Manolescu A., Karason A., Palsson A., Thorleifsson G.,
Jakobsdottir M., Steinberg S., Palsson S., Jonasson F.,
Sigurgeirsson B., Thorisdottir K., Ragnarsson R.,
Benediktsdottir K.R., Aben K.K., Kiemeney L.A., Olafsson J.H.,
Gulcher J., Kong A., Thorsteinsdottir U., Stefansson K.;
"Genetic determinants of hair, eye and skin pigmentation in
Europeans.";
Nat. Genet. 39:1443-1452(2007).
[15]
POLYMORPHISM LINKED TO BLOND HAIR COLOR.
PubMed=24880339; DOI=10.1038/ng.2991;
Guenther C.A., Tasic B., Luo L., Bedell M.A., Kingsley D.M.;
"A molecular basis for classic blond hair color in Europeans.";
Nat. Genet. 46:748-752(2014).
[16]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND DISULFIDE BONDS.
PubMed=10880433; DOI=10.1093/emboj/19.13.3192;
Jiang X., Gurel O., Mendiaz E.A., Stearns G.W., Clogston C.L.,
Lu H.S., Osslund T.D., Syed R.S., Langley K.E., Hendrickson W.A.;
"Structure of the active core of human stem cell factor and analysis
of binding to its receptor kit.";
EMBO J. 19:3192-3203(2000).
[17]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-166, AND DISULFIDE BONDS.
PubMed=10884405; DOI=10.1073/pnas.97.14.7732;
Zhang Z., Zhang R., Joachimiak A., Schlessinger J., Kong X.P.;
"Crystal structure of human stem cell factor: implication for stem
cell factor receptor dimerization and activation.";
Proc. Natl. Acad. Sci. U.S.A. 97:7732-7737(2000).
[18]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 26-166 IN COMPLEX WITH KIT,
AND DISULFIDE BONDS.
PubMed=17662946; DOI=10.1016/j.cell.2007.05.055;
Yuzawa S., Opatowsky Y., Zhang Z., Mandiyan V., Lax I.,
Schlessinger J.;
"Structural basis for activation of the receptor tyrosine kinase KIT
by stem cell factor.";
Cell 130:323-334(2007).
[19]
VARIANT FPHH SER-36, AND CHARACTERIZATION OF VARIANT FPHH SER-36.
PubMed=19375057; DOI=10.1016/j.ajhg.2009.03.019;
Wang Z.-Q., Si L., Tang Q., Lin D., Fu Z., Zhang J., Cui B., Zhu Y.,
Kong X., Deng M., Xia Y., Xu H., Le W., Hu L., Kong X.;
"Gain-of-function mutation of KIT ligand on melanin synthesis causes
familial progressive hyperpigmentation.";
Am. J. Hum. Genet. 84:672-677(2009).
[20]
VARIANT DCUA 67-HIS-CYS-68 DELINS ARG, CHARACTERIZATION OF VARIANT
DCUA 67-HIS-CYS-68 DELINS ARG, INVOLVEMENT IN DCUA, VARIANT VAL-104,
CHARACTERIZATION OF VARIANT VAL-104, AND SUBCELLULAR LOCATION (ISOFORM
2).
PubMed=26522471; DOI=10.1016/j.ajhg.2015.09.011;
Baylor-Hopkins Center for Mendelian Genomics;
Zazo Seco C., Serrao de Castro L., van Nierop J.W., Morin M.,
Jhangiani S., Verver E.J., Schraders M., Maiwald N., Wesdorp M.,
Venselaar H., Spruijt L., Oostrik J., Schoots J., van Reeuwijk J.,
Lelieveld S.H., Huygen P.L., Insenser M., Admiraal R.J.,
Pennings R.J., Hoefsloot L.H., Arias-Vasquez A., de Ligt J.,
Yntema H.G., Jansen J.H., Muzny D.M., Huls G., van Rossum M.M.,
Lupski J.R., Moreno-Pelayo M.A., Kunst H.P., Kremer H.;
"Allelic Mutations of KITLG, Encoding KIT Ligand, Cause Asymmetric and
Unilateral Hearing Loss and Waardenburg Syndrome Type 2.";
Am. J. Hum. Genet. 97:647-660(2015).
-!- FUNCTION: Ligand for the receptor-type protein-tyrosine kinase
KIT. Plays an essential role in the regulation of cell survival
and proliferation, hematopoiesis, stem cell maintenance,
gametogenesis, mast cell development, migration and function, and
in melanogenesis. KITLG/SCF binding can activate several signaling
pathways. Promotes phosphorylation of PIK3R1, the regulatory
subunit of phosphatidylinositol 3-kinase, and subsequent
activation of the kinase AKT1. KITLG/SCF and KIT also transmit
signals via GRB2 and activation of RAS, RAF1 and the MAP kinases
MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation
of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT
promote activation of PLCG1, leading to the production of the
cellular signaling molecules diacylglycerol and inositol 1,4,5-
trisphosphate. KITLG/SCF acts synergistically with other
cytokines, probably interleukins.
-!- SUBUNIT: Homodimer, non-covalently linked (Probable).
Heterotetramer with KIT, binding two KIT molecules; thereby
mediates KIT dimerization and subsequent activation by
autophosphorylation. {ECO:0000269|PubMed:17662946, ECO:0000305}.
-!- INTERACTION:
P10721:KIT; NbExp=2; IntAct=EBI-1379527, EBI-1379503;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:26522471}. Cytoplasm, cytoskeleton
{ECO:0000250}. Cell membrane {ECO:0000269|PubMed:26522471};
Single-pass type I membrane protein {ECO:0000250}. Cell
projection, lamellipodium {ECO:0000269|PubMed:26522471}. Cell
projection, filopodium {ECO:0000269|PubMed:26522471}.
-!- SUBCELLULAR LOCATION: Soluble KIT ligand: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=SCF248;
IsoId=P21583-1; Sequence=Displayed;
Name=2; Synonyms=SCF220;
IsoId=P21583-2; Sequence=VSP_006022;
Name=3;
IsoId=P21583-3; Sequence=VSP_032762, VSP_032763;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: Acts in the early stages of hematopoiesis.
-!- PTM: A soluble form (sKITLG) is produced by proteolytic processing
of isoform 1 in the extracellular domain.
{ECO:0000269|PubMed:1381905}.
-!- PTM: Found in two differentially glycosylated forms, LMW-SCF and
HMW-SCF. LMW-SCF is fully N-glycosylated at Asn-145, partially N-
glycosylated at Asn-90, O-glycosylated at Ser-167, Thr-168 and
Thr-180, and not glycosylated at Asn-97 or Asn-118. HMW-SCF is N-
glycosylated at Asn-118, Asn-90 and Asn-145, O-glycosylated at
Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97.
{ECO:0000269|PubMed:1381905}.
-!- PTM: A soluble form exists as a cleavage product of the
extracellular domain. {ECO:0000269|PubMed:1381905}.
-!- POLYMORPHISM: Genetic variants in KITLG define the skin/hair/eye
pigmentation variation locus 7 (SHEP7) [MIM:611664]. Hair, eye and
skin pigmentation are among the most visible examples of human
phenotypic variation, with a broad normal range that is subject to
substantial geographic stratification. In the case of skin,
individuals tend to have lighter pigmentation with increasing
distance from the equator. By contrast, the majority of variation
in human eye and hair color is found among individuals of European
ancestry, with most other human populations fixed for brown eyes
and black hair.
-!- POLYMORPHISM: A non-coding SNP (dbSNP:rs12821256) has been shown
to be associated with classic blond hair color in Europeans. This
SNP is located 350 kb upstream from KITLG, in an enhancer
specifically active in the hair follicle environment. It alters a
LEF1 binding site, reducing LEF1 responsiveness in cultured
keratinocytes. This SNP is not associated with eye pigmentation.
It is most prevalent in Northern Europe (PubMed:24880339).
{ECO:0000269|PubMed:24880339}.
-!- DISEASE: Hyperpigmentation with or without hypopigmentation,
familial progressive (FPHH) [MIM:145250]: A disorder characterized
by hyperpigmented patches in the skin, present in early infancy
and increasing in size and number with age. Hyperpigmentation has
variable intensity, and sometimes is associated with cafe-au-lait
macules and larger hypopigmented ash-leaf macules.
{ECO:0000269|PubMed:19375057}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Deafness, congenital, unilateral or asymmetric (DCUA)
[MIM:616697]: An autosomal dominant form of non-syndromic,
sensorineural deafness characterized by inability to hear
affecting one ear. Some patients suffers from asymmetric,
bilateral hearing loss. {ECO:0000269|PubMed:26522471}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the SCF family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MGFID142.html";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=two's company - Issue
163 of August 2014;
URL="http://web.expasy.org/spotlight/back_issues/163/";
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EMBL; M59964; AAA85450.1; -; mRNA.
EMBL; AF119835; AAD22048.1; -; mRNA.
EMBL; AF400436; AAK92485.1; -; mRNA.
EMBL; AF400437; AAK92486.1; -; mRNA.
EMBL; AK290319; BAF83008.1; -; mRNA.
EMBL; AK293002; BAF85691.1; -; mRNA.
EMBL; CR749222; CAH18078.1; -; mRNA.
EMBL; CH471054; EAW97417.1; -; Genomic_DNA.
EMBL; BC069733; AAH69733.1; -; mRNA.
EMBL; BC069783; AAH69783.1; -; mRNA.
EMBL; BC069797; AAH69797.1; -; mRNA.
EMBL; BC074725; AAH74725.1; -; mRNA.
EMBL; BC126166; AAI26167.1; -; mRNA.
EMBL; BC143899; AAI43900.1; -; mRNA.
EMBL; S42571; AAB22846.2; -; mRNA.
CCDS; CCDS31867.1; -. [P21583-2]
CCDS; CCDS31868.1; -. [P21583-1]
PIR; A35974; A35974.
PIR; B61190; B61190.
PIR; S29052; S29052.
RefSeq; NP_000890.1; NM_000899.4. [P21583-1]
RefSeq; NP_003985.2; NM_003994.5. [P21583-2]
UniGene; Hs.1048; -.
UniGene; Hs.661108; -.
PDB; 1EXZ; X-ray; 2.30 A; A/B/C/D=26-166.
PDB; 1SCF; X-ray; 2.20 A; A/B/C/D=1-273.
PDB; 2E9W; X-ray; 3.50 A; C/D=26-166.
PDBsum; 1EXZ; -.
PDBsum; 1SCF; -.
PDBsum; 2E9W; -.
DisProt; DP00917; -.
ProteinModelPortal; P21583; -.
SMR; P21583; -.
BioGrid; 110410; 9.
IntAct; P21583; 2.
STRING; 9606.ENSP00000228280; -.
BindingDB; P21583; -.
ChEMBL; CHEMBL2346489; -.
iPTMnet; P21583; -.
PhosphoSitePlus; P21583; -.
BioMuta; KITLG; -.
DMDM; 134289; -.
MaxQB; P21583; -.
PaxDb; P21583; -.
PeptideAtlas; P21583; -.
PRIDE; P21583; -.
DNASU; 4254; -.
Ensembl; ENST00000228280; ENSP00000228280; ENSG00000049130. [P21583-1]
Ensembl; ENST00000347404; ENSP00000054216; ENSG00000049130. [P21583-2]
GeneID; 4254; -.
KEGG; hsa:4254; -.
UCSC; uc001tav.4; human. [P21583-1]
CTD; 4254; -.
DisGeNET; 4254; -.
EuPathDB; HostDB:ENSG00000049130.13; -.
GeneCards; KITLG; -.
HGNC; HGNC:6343; KITLG.
HPA; HPA070395; -.
MalaCards; KITLG; -.
MIM; 145250; phenotype.
MIM; 184745; gene.
MIM; 611664; phenotype.
MIM; 616697; phenotype.
neXtProt; NX_P21583; -.
OpenTargets; ENSG00000049130; -.
Orphanet; 280628; Familial progressive hyper- and hypopigmentation.
Orphanet; 79146; Familial progressive hyperpigmentation.
Orphanet; 363494; Testicular non seminomatous germ cell tumor.
PharmGKB; PA30129; -.
eggNOG; ENOG410IF3Y; Eukaryota.
eggNOG; ENOG410XYQR; LUCA.
GeneTree; ENSGT00390000018272; -.
HOVERGEN; HBG036146; -.
InParanoid; P21583; -.
KO; K05461; -.
OMA; VKTKGIC; -.
OrthoDB; EOG091G0I23; -.
PhylomeDB; P21583; -.
TreeFam; TF330811; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1433559; Regulation of KIT signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SIGNOR; P21583; -.
ChiTaRS; KITLG; human.
EvolutionaryTrace; P21583; -.
GeneWiki; Stem_cell_factor; -.
GenomeRNAi; 4254; -.
PMAP-CutDB; P21583; -.
PRO; PR:P21583; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000049130; -.
CleanEx; HS_KITLG; -.
ExpressionAtlas; P21583; baseline and differential.
Genevisible; P21583; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005125; F:cytokine activity; IEA:Ensembl.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005173; F:stem cell factor receptor binding; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
GO; GO:0035162; P:embryonic hemopoiesis; IDA:DFLAT.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0033026; P:negative regulation of mast cell apoptotic process; IEA:Ensembl.
GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL.
GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0070668; P:positive regulation of mast cell proliferation; IEA:Ensembl.
GO; GO:0045636; P:positive regulation of melanocyte differentiation; IEA:Ensembl.
GO; GO:0002763; P:positive regulation of myeloid leukocyte differentiation; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:Ensembl.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR003452; SCF.
PANTHER; PTHR11574; PTHR11574; 1.
Pfam; PF02404; SCF; 1.
PIRSF; PIRSF015599; SCF; 1.
SUPFAM; SSF47266; SSF47266; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Deafness;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Growth factor; Membrane; Non-syndromic deafness;
Polymorphism; Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25
CHAIN 26 273 Kit ligand.
/FTId=PRO_0000031913.
CHAIN 26 190 Soluble KIT ligand.
/FTId=PRO_0000403391.
TOPO_DOM 26 214 Extracellular. {ECO:0000255}.
TRANSMEM 215 237 Helical. {ECO:0000255}.
TOPO_DOM 238 273 Cytoplasmic. {ECO:0000255}.
SITE 97 97 Not glycosylated.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:1381905}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:1381905}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1381905}.
CARBOHYD 167 167 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:1381905}.
CARBOHYD 168 168 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:1381905}.
CARBOHYD 180 180 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:1381905}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 29 114
DISULFID 68 163
VAR_SEQ 1 35 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_032762.
VAR_SEQ 36 43 NVKDVTKL -> MPSCLAAQ (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_032763.
VAR_SEQ 174 202 DSRVSVTKPFMLPPVAASSLRNDSSSSNR -> G (in
isoform 2). {ECO:0000303|PubMed:10049787,
ECO:0000303|PubMed:1379846,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1724381,
ECO:0000303|Ref.4}.
/FTId=VSP_006022.
VARIANT 36 36 N -> S (in FPHH; gain-of-function
mutation; sKITLG reveales that the mutant
Ser-36 sKITLG increases the content of
the melanin by 109% compared with the
wild-type sKITLG; tyrosinase activity is
significantly increased by the mutant
sKITLG compared to wild-type control;
dbSNP:rs121918653).
{ECO:0000269|PubMed:19375057}.
/FTId=VAR_063237.
VARIANT 54 54 T -> A (in dbSNP:rs3741457).
/FTId=VAR_042652.
VARIANT 67 68 HC -> R (in DCUA; loss of cell membrane
association).
{ECO:0000269|PubMed:26522471}.
/FTId=VAR_076222.
VARIANT 104 104 L -> V (found in a patient with
Waardenburg syndrome type 2 (WS2) and
hearing loss; unknown pathological
significance; reduces secretion;
dbSNP:rs864309655).
{ECO:0000269|PubMed:26522471}.
/FTId=VAR_076223.
VARIANT 210 210 D -> Y (in dbSNP:rs41283112).
/FTId=VAR_063238.
VARIANT 232 232 F -> Y (in dbSNP:rs12721563).
/FTId=VAR_042653.
CONFLICT 55 55 L -> S (in Ref. 3; AAD22048 and 4;
AAK92486). {ECO:0000305}.
CONFLICT 128 128 K -> R (in Ref. 3; AAD22048 and 4;
AAK92486). {ECO:0000305}.
CONFLICT 134 134 L -> F (in Ref. 3; AAD22048 and 4;
AAK92486). {ECO:0000305}.
HELIX 30 32 {ECO:0000244|PDB:2E9W}.
HELIX 37 46 {ECO:0000244|PDB:1SCF}.
STRAND 53 56 {ECO:0000244|PDB:1SCF}.
TURN 59 63 {ECO:0000244|PDB:1SCF}.
HELIX 66 68 {ECO:0000244|PDB:1SCF}.
HELIX 70 85 {ECO:0000244|PDB:1SCF}.
STRAND 92 94 {ECO:0000244|PDB:2E9W}.
HELIX 97 114 {ECO:0000244|PDB:1SCF}.
STRAND 120 122 {ECO:0000244|PDB:1EXZ}.
STRAND 132 135 {ECO:0000244|PDB:1SCF}.
HELIX 137 149 {ECO:0000244|PDB:1SCF}.
TURN 150 152 {ECO:0000244|PDB:1SCF}.
STRAND 157 160 {ECO:0000244|PDB:1SCF}.
SEQUENCE 273 AA; 30899 MW; 19FD362CB59C6607 CRC64;
MKKTQTWILT CIYLQLLLFN PLVKTEGICR NRVTNNVKDV TKLVANLPKD YMITLKYVPG
MDVLPSHCWI SEMVVQLSDS LTDLLDKFSN ISEGLSNYSI IDKLVNIVDD LVECVKENSS
KDLKKSFKSP EPRLFTPEEF FRIFNRSIDA FKDFVVASET SDCVVSSTLS PEKDSRVSVT
KPFMLPPVAA SSLRNDSSSS NRKAKNPPGD SSLHWAAMAL PALFSLIIGF AFGALYWKKR
QPSLTRAVEN IQINEEDNEI SMLQEKEREF QEV


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