SCF_BOVIN
ID SCF_BOVIN Reviewed; 274 AA.
AC Q28132; Q9TU74;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
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;
GN Name=KITLG; Synonyms=SCF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Spleen;
RX PubMed=7520283; DOI=10.1016/0167-4889(94)90084-1;
RA Zhou J., Hikono H., Ohtaki M., Kubota T., Sakurai M.;
RT "Cloning and characterization of cDNAs encoding two normal isoforms of
RT bovine stem cell factor.";
RL Biochim. Biophys. Acta 1223:148-150(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Kudo T.;
RT "Bovine counterpart of stem cell factor.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-239, AND VARIANT ASP-218.
RC STRAIN=Belgian blue;
RX PubMed=10384045; DOI=10.1007/s003359901076;
RA Seitz J.J., Schmutz S.M., Thue T.D., Buchanan F.C.;
RT "A missense mutation in the bovine MGF gene is associated with the roan
RT phenotype in Belgian Blue and Shorthorn cattle.";
RL Mamm. Genome 10:710-712(1999).
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: [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}. 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;
CC IsoId=Q28132-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q28132-2; Sequence=VSP_006020;
CC -!- PTM: A soluble form is produced by proteolytic processing of isoform 1
CC in the extracellular domain. {ECO:0000250}.
CC -!- POLYMORPHISM: The roan locus is responsible for the coat coloration of
CC Belgian Blue and Shorthorn cattle. The solid-colored and white animals
CC are homozygotes, and the roan animals, with intermingled colored and
CC white hairs, are heterozygous. The roan phenotype is due to the Asp-218
CC mutation.
CC -!- SIMILARITY: Belongs to the SCF family. {ECO:0000305}.
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DR EMBL; D28934; BAA06061.1; -; mRNA.
DR EMBL; AB033716; BAA94808.1; -; mRNA.
DR EMBL; AF120154; AAD55355.1; -; Genomic_DNA.
DR PIR; S47571; S47571.
DR RefSeq; NP_776800.1; NM_174375.2. [Q28132-1]
DR AlphaFoldDB; Q28132; -.
DR SMR; Q28132; -.
DR STRING; 9913.ENSBTAP00000023349; -.
DR PaxDb; Q28132; -.
DR PRIDE; Q28132; -.
DR Ensembl; ENSBTAT00000065938; ENSBTAP00000055628; ENSBTAG00000017549. [Q28132-2]
DR Ensembl; ENSBTAT00000074582; ENSBTAP00000062180; ENSBTAG00000017549. [Q28132-1]
DR GeneID; 281885; -.
DR KEGG; bta:281885; -.
DR CTD; 4254; -.
DR VEuPathDB; HostDB:ENSBTAG00000017549; -.
DR eggNOG; ENOG502QTGT; Eukaryota.
DR GeneTree; ENSGT00390000018272; -.
DR HOGENOM; CLU_090207_0_0_1; -.
DR InParanoid; Q28132; -.
DR OMA; CWISVMV; -.
DR OrthoDB; 1083457at2759; -.
DR TreeFam; TF330811; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000017549; Expressed in intramuscular adipose tissue and 100 other tissues.
DR ExpressionAtlas; Q28132; 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 GO; GO:0009893; P:positive regulation of metabolic process; IEA:UniProt.
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 Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Disulfide bond; Glycoprotein; Growth factor;
KW Membrane; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..274
FT /note="Kit ligand"
FT /id="PRO_0000031908"
FT CHAIN 26..191
FT /note="Soluble KIT ligand"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403386"
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 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 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 VAR_SEQ 175..203
FT /note="DSRVSVTKPFMLPPVAASSLRNDSSSSNR -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7520283"
FT /id="VSP_006020"
FT VARIANT 218
FT /note="A -> D (in allele roan)"
FT /evidence="ECO:0000269|PubMed:10384045"
SQ SEQUENCE 274 AA; 31015 MW; D6C1DDB77B0CB12B CRC64;
MKKTQTWIIT CIYLQLLLFN PLVHTQGICS NRVTDDVKDV TKLVANLPKD YMITLKYVPG
MDVLPSHCWI SEMVEQLSVS LTDLLDKFSN ISEGLSNYCI IDKLVKIVDD LVECMEEHSS
ENVKKSSKSP EPRQFTPEKF FGIFNKSIDA FKDLEIVASK MSECVISSTS SPEKDSRVSV
TKPFMLPPVA ASSLRNDSSS SNRKASNSIE DSSLQWAAVA LPAFFSLVIG FAFGAFYWKK
KQPNLTRTVE NRQINEEDNE ISMLQEKERE FQEV
