SCF_NEOVI
ID SCF_NEOVI Reviewed; 274 AA.
AC Q95N18; Q95MN5;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Neovison vison (American mink) (Mustela vison).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Neogale.
OX NCBI_TaxID=452646;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Bennett R.D., Murphy B.D.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q95N18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95N18-2; Sequence=VSP_006024;
CC -!- PTM: A soluble form is produced by proteolytic processing of isoform 1
CC in the extracellular domain. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SCF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY013712; AAG37434.1; -; mRNA.
DR EMBL; AF323757; AAK73366.1; -; mRNA.
DR AlphaFoldDB; Q95N18; -.
DR SMR; Q95N18; -.
DR Proteomes; UP000694425; 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 Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Disulfide bond; Glycoprotein; Growth factor;
KW Membrane; Reference proteome; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..274
FT /note="Kit ligand"
FT /id="PRO_0000031915"
FT CHAIN 26..191
FT /note="Soluble KIT ligand"
FT /id="PRO_0000292276"
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 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|Ref.1"
FT /id="VSP_006024"
FT CONFLICT 65
FT /note="S -> P (in Ref. 1; AAK73366)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="S -> N (in Ref. 1; AAK73366)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..274
FT /note="EREFQEV -> RESFKRCNCGFYHTVLSYLGG (in Ref. 1;
FT AAK73366)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 31035 MW; 5AC1619014AE5E72 CRC64;
MKKTQTWIIT CIYLQLLLFN PLVRTKGICR NRVTDDVKDV TKLVANLPKD YKIALNYVPG
MDVLSSHCWI RVMVEQLSVS LTDLLDKFSN ISEGLSNYSI IDKLVKIVDD LVECMEEHSS
ENVKKSPKNP EPRHFAPEDF FRIFNRSIDA LKDLETVASK TSECVLPSTL SPEKDSRVSV
TKPFMLPPVA ASSLRNDSSS SNRKAANPLG DSNLQWAAMA LPAFFSLVIG FAFGALYWKK
KQPNLTRTAE NIQINEEDNE ISMLQEKERE FQEV
