SCF_CAPHI
ID SCF_CAPHI Reviewed; 274 AA.
AC Q95M19;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=SCF;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Shiba; TISSUE=Brain;
RA Yanagisawa N., Tanaka S., Yamanouchi K., Tojo H., Tachi C.;
RT "Identification of splicing isoforms of caprine stem cell factor (gSCF)
RT transcripts and expression patterns of the two major isoforms, gSCF825 and
RT gSCF741, in the brain and the skin of adult and fetal Shiba goats, Capra
RT hircus.";
RL Submitted (MAR-1997) 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; AB002152; BAB71753.1; -; mRNA.
DR RefSeq; NP_001272599.1; NM_001285670.1.
DR AlphaFoldDB; Q95M19; -.
DR SMR; Q95M19; -.
DR STRING; 9925.ENSCHIP00000030559; -.
DR GeneID; 100860807; -.
DR KEGG; chx:100860807; -.
DR CTD; 4254; -.
DR OrthoDB; 1083457at2759; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
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..274
FT /note="Kit ligand"
FT /id="PRO_0000031910"
FT CHAIN 26..191
FT /note="Soluble KIT ligand"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403388"
FT CHAIN 26..?
FT /note="Processed kit ligand"
FT /id="PRO_0000292274"
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 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"
SQ SEQUENCE 274 AA; 31053 MW; BBFE669A509EF65D CRC64;
MKKTQTWIIT CIYLQLLLFN PLVHSQGICR NRVTDDVKDV TKLVANLPKD YMITLKYVPG
MDVLPSHCWI SEMVEQLSVS LTDLLDKFSN ISEGLSNYSI IDKLVKIVDD LVECMEEHSF
ENVKKSSKSP EPRQFTPEKF FGIFNKSIDA FKDLEIVAST MSECVISSTS SPEKDSRVSV
TKPFMLPPVA ASSLRNDSSS SNRKASNSIE DSSLQWAAVA LPAFFSLVIG FAFGALYWKK
KQPNLTRTVE NRQINEEDNE ISMLQEKERE FQEV
