SCF_SHEEP
ID SCF_SHEEP Reviewed; 267 AA.
AC P79368; Q28591;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Kit ligand;
DE AltName: Full=Mast cell growth factor;
DE Short=MGF;
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; Fragment;
GN Name=KITLG; Synonyms=SCF;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-267.
RC TISSUE=Ovarian follicle;
RX PubMed=8662240; DOI=10.1007/s003359900142;
RA Tisdall D.J., Quirke L.D., Galloway S.M.;
RT "Ovine stem cell factor gene is located within a syntenic group on
RT chromosome 3 conserved across mammalian species.";
RL Mamm. Genome 7:472-473(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-202.
RX PubMed=10328863; DOI=10.1006/cyto.1998.0430;
RA McInnes C.J., Deane D., Thomson J., Broad A., Haig D.M.;
RT "The cloning and expression of the cDNA for ovine stem cell factor (kit-
RT ligand) and characterization of its in vitro haematopoietic activity.";
RL Cytokine 11:249-256(1999).
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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21583}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane
CC {ECO:0000250|UniProtKB:P21583}; Single-pass type I membrane protein
CC {ECO:0000250}. 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 -!- PTM: A soluble form is produced by proteolytic processing of the
CC extracellular domain. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SCF family. {ECO:0000305}.
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DR EMBL; U89874; AAB49491.1; -; mRNA.
DR EMBL; Z50743; CAA90620.1; -; mRNA.
DR PIR; S58313; S58313.
DR AlphaFoldDB; P79368; -.
DR SMR; P79368; -.
DR STRING; 9940.ENSOARP00000016728; -.
DR eggNOG; ENOG502QTGT; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005173; F:stem cell factor receptor binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Disulfide bond; Glycoprotein; Growth factor; Membrane;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..>267
FT /note="Kit ligand"
FT /id="PRO_0000031918"
FT CHAIN 26..191
FT /note="Soluble KIT ligand"
FT /id="PRO_0000292278"
FT TOPO_DOM 26..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..>267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 26
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P21581"
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 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..114
FT /evidence="ECO:0000250"
FT DISULFID 68..164
FT /evidence="ECO:0000250"
FT NON_TER 267
SQ SEQUENCE 267 AA; 30149 MW; 9D9D959E4B9EC841 CRC64;
MKKTQTWIIT CIYLQLLLFN PLVHTQGICR NRVTDDVKDV TKLVANLPKD YMITLKYVPG
MDVLPSHCWI SEMVEQLSVS LTDLLDKFSN ISEGLSNYSI IDKLVKIVDD LVECMEEHSF
ENVKKSSKSP EPRQFTPEKF FGIFNKSIDA FKDLEIVAST MSECVISSTS SPEKDSRVSV
TKPFMLPPVA ASSLRNDSSS SNRKASNSIE DSSLQWAAVA LPAFFSLVIG FAFGALYWKK
KQPNLTRTVE NRQINEEDNE ISMLQEK
