SCF_COTJA
ID SCF_COTJA Reviewed; 287 AA.
AC Q90314; Q90315;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Flags: Precursor;
GN Name=KITLG; Synonyms=SCF;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX PubMed=8679698; DOI=10.1016/0167-4781(96)00062-0;
RA Petitte J.N., Kulik M.J.;
RT "Cloning and characterization of cDNAs encoding two forms of avian stem
RT cell factor.";
RL Biochim. Biophys. Acta 1307:149-151(1996).
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. Acts
CC 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}. Secreted {ECO:0000250}.
CC Note=Also exists as a secreted soluble form (isoform 1 only).
CC {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q90314-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q90314-2; Sequence=VSP_006026;
CC -!- PTM: A soluble form is produced by proteolytic processing of isoform 1
CC in the extracellular domain.
CC -!- SIMILARITY: Belongs to the SCF family. {ECO:0000305}.
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DR EMBL; U43078; AAC59933.1; -; mRNA.
DR EMBL; U43079; AAC59934.1; -; Genomic_DNA.
DR PIR; S70367; S70367.
DR AlphaFoldDB; Q90314; -.
DR SMR; Q90314; -.
DR Proteomes; UP000694412; 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:0000255"
FT CHAIN 26..287
FT /note="Kit ligand"
FT /id="PRO_0000031920"
FT TOPO_DOM 26..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..117
FT /evidence="ECO:0000250"
FT DISULFID 68..167
FT /evidence="ECO:0000250"
FT VAR_SEQ 179..213
FT /note="DSRVAVTKTISFPPVAASSLRNDSIGSNTSSNSNK -> E (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:8679698"
FT /id="VSP_006026"
SQ SEQUENCE 287 AA; 32455 MW; ABA81AEA422A702E CRC64;
MKKAQTWIIT CFCLQLLLLN PLVKTQSSCG NPVTDDVNDI AKLVGNLPND YLITLKYVPK
MDSLPNHCWL HLMVPEFSRS LHNLLQKFVD ISDMSDVLSN YSIINNLTRI INDLMACLAF
DKNKDFIKEN GHLYEEDRFI PENFFRLFNR TIEVYKEFAD SLDKNDCIMP STVETPENDS
RVAVTKTISF PPVAASSLRN DSIGSNTSSN SNKEALGFIS SSSLQGISIA LTSLLSLLIG
FILGVIYWKK THPKSRPESN ETTQCHGCQE ENEISMLQQK EKEHLQV
