SCF_HORSE
ID SCF_HORSE Reviewed; 274 AA.
AC Q95MD2; O62765; Q95MG7; Q95MG8; Q9N1Y5;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 105.
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 Contains:
DE RecName: Full=Processed kit ligand;
DE Flags: Precursor;
GN Name=KITLG; Synonyms=MGF, SCF;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE OF 4-264.
RA Terry R.R., Mickelson J.R., Schmutz S., Cothran E.G., Bailey E.;
RT "Equus caballus mast cell growth factor (MGF).";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE OF 12-267.
RC TISSUE=Skin;
RA Rieder S., Checa-Cortes M.L., Joerg H., Stranzinger G.;
RT "An equine sequence homologous to stem cell factor (KIT-ligand).";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 107-202 AND 227-274.
RA Terry R.R., Bailey E.F., Cothran E.G.;
RT "Evaluation of MGF as the candidate gene for Appaloosa spotting.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE OF 147-197.
RA Caetano A.R., Shiue Y.-L., Lyons L.A., Laughlin T.F., O'Brien S.J.,
RA Murray J.D., Bowling A.T.;
RT "A primary Human-Horse comparative gene map.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Stimulates the proliferation of mast cells. Able to augment
CC the proliferation of both myeloid and lymphoid hematopoietic
CC progenitors in bone marrow culture. Mediates also cell-cell adhesion.
CC Acts synergistically with other cytokines, probably interleukins (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer, non-covalently linked. {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: [Processed kit ligand]: Secreted {ECO:0000250}.
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; AF401625; AAK94474.1; -; mRNA.
DR EMBL; AF053498; AAC97076.1; -; mRNA.
DR EMBL; AF367704; AAK63249.1; -; Genomic_DNA.
DR EMBL; AF367706; AAK63250.1; -; Genomic_DNA.
DR EMBL; AF130770; AAF36716.1; -; Genomic_DNA.
DR RefSeq; NP_001157434.1; NM_001163962.1.
DR AlphaFoldDB; Q95MD2; -.
DR SMR; Q95MD2; -.
DR STRING; 9796.ENSECAP00000000163; -.
DR PaxDb; Q95MD2; -.
DR Ensembl; ENSECAT00000034663; ENSECAP00000030330; ENSECAG00000000152.
DR GeneID; 100034127; -.
DR KEGG; ecb:100034127; -.
DR CTD; 4254; -.
DR VGNC; VGNC:49477; KITLG.
DR GeneTree; ENSGT00390000018272; -.
DR HOGENOM; CLU_090207_0_0_1; -.
DR InParanoid; Q95MD2; -.
DR OrthoDB; 1083457at2759; -.
DR Proteomes; UP000002281; Chromosome 28.
DR Bgee; ENSECAG00000000152; Expressed in epithelium of bronchus and 21 other tissues.
DR ExpressionAtlas; Q95MD2; baseline.
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:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005173; F:stem cell factor receptor binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
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; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..274
FT /note="Kit ligand"
FT /id="PRO_0000031912"
FT CHAIN 26..191
FT /note="Soluble KIT ligand"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403390"
FT CHAIN 26..?
FT /note="Processed kit ligand"
FT /id="PRO_0000292275"
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..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 CARBOHYD 207
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 CONFLICT 15
FT /note="Q -> P (in Ref. 2; AAC97076)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="Missing (in Ref. 3; AAK63250)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 31217 MW; 96C1D4C9059132F2 CRC64;
MKKTQTWIIT CIYLQLLLFN PLVKTKGICE NRVTDDVKDV TKLVANLPKD YKITLKYVPG
MDVLPSHCWI SEMVQHLSVS LTDLLEKFSN ISEGLSNYSI IDKLVKIVDD LVECMEEHSS
ENVKKSYKSQ ESRLFTPEEF FRIFNRSIDA FKDLEMVVSK TSECVVSSTL SPEKDSRVSV
TKPFMLPPVA ASSLRNDSSS SNRKASNFTG DSNLQWAAMA LPAFFSLVIG FAFGALYWKK
KQPNLTRAVE NIQINEEDNE ISMLQEKERE FQEV
