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SCF_CANLF
ID   SCF_CANLF               Reviewed;         274 AA.
AC   Q06220; Q8SPM6;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 136.
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;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=T-cell;
RX   PubMed=1281786;
RA   Shull R.M., Suggs S.V., Langley K.E., Okino K.H., Jacobsen F.W.,
RA   Martin F.H.;
RT   "Canine stem cell factor (c-kit ligand) supports the survival of
RT   hematopoietic progenitors in long-term canine marrow culture.";
RL   Exp. Hematol. 20:1118-1124(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-274.
RC   TISSUE=Tail;
RA   Schmutz S.M., Berryere T.G.;
RT   "MGF sequencing in the dog aids in mapping to CFA15.";
RL   Submitted (APR-2002) 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.
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.
CC   -!- SUBCELLULAR LOCATION: [Soluble KIT ligand]: Secreted {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Acts in the early stages of hematopoiesis.
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; S53329; AAB24619.1; -; mRNA.
DR   EMBL; AY094361; AAM16280.1; -; mRNA.
DR   PIR; I46929; I46929.
DR   RefSeq; NP_001012753.1; NM_001012735.2.
DR   AlphaFoldDB; Q06220; -.
DR   SMR; Q06220; -.
DR   STRING; 9615.ENSCAFP00000066357; -.
DR   PaxDb; Q06220; -.
DR   Ensembl; ENSCAFT00030032992; ENSCAFP00030028782; ENSCAFG00030017725.
DR   Ensembl; ENSCAFT00040028995; ENSCAFP00040025188; ENSCAFG00040015574.
DR   Ensembl; ENSCAFT00845032796; ENSCAFP00845025667; ENSCAFG00845018506.
DR   GeneID; 403507; -.
DR   KEGG; cfa:403507; -.
DR   CTD; 4254; -.
DR   VEuPathDB; HostDB:ENSCAFG00845018506; -.
DR   eggNOG; ENOG502QTGT; Eukaryota.
DR   GeneTree; ENSGT00390000018272; -.
DR   HOGENOM; CLU_090207_0_0_1; -.
DR   InParanoid; Q06220; -.
DR   OMA; CWISVMV; -.
DR   OrthoDB; 1083457at2759; -.
DR   TreeFam; TF330811; -.
DR   Reactome; R-CFA-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-CFA-1433557; Signaling by SCF-KIT.
DR   Reactome; R-CFA-1433559; Regulation of KIT signaling.
DR   Reactome; R-CFA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-CFA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Proteomes; UP000002254; Chromosome 15.
DR   Bgee; ENSCAFG00000006091; Expressed in bone marrow and 44 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:0033024; P:mast cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0097531; P:mast cell migration; IEA:Ensembl.
DR   GO; GO:0070662; P:mast cell proliferation; IEA:Ensembl.
DR   GO; GO:0097324; P:melanocyte migration; IEA:Ensembl.
DR   GO; GO:0002573; P:myeloid leukocyte differentiation; IEA:Ensembl.
DR   GO; GO:0033026; P:negative regulation of mast cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:1901534; P:positive regulation of hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR   GO; GO:0070668; P:positive regulation of mast cell proliferation; IEA:Ensembl.
DR   GO; GO:0045636; P:positive regulation of melanocyte differentiation; IEA:Ensembl.
DR   GO; GO:0002763; P:positive regulation of myeloid leukocyte differentiation; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:Ensembl.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR   GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR   GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
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:0000250"
FT   CHAIN           26..274
FT                   /note="Kit ligand"
FT                   /id="PRO_0000031909"
FT   CHAIN           26..191
FT                   /note="Soluble KIT ligand"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000403387"
FT   CHAIN           26..?
FT                   /note="Processed kit ligand"
FT                   /id="PRO_0000292273"
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"
SQ   SEQUENCE   274 AA;  30870 MW;  4182BE9AED00793B CRC64;
     MKKTQTWIIT CIYLQLLLFN PLVKTKGICG KRVTDDVKDV TKLVANLPKD YKIALKYVPG
     MDVLPSHCWI SVMVEQLSVS LTDLLDKFSN ISEGLSNYSI IDKLVKIVDD LVECTEGYSF
     ENVKKAPKSP ELRLFTPEEF FRIFNRSIDA FKDLETVASK SSECVVSSTL SPDKDSRVSV
     TKPFMLPPVA ASSLRNDSSS SNRKASNSIG DSNLQWAAMA LPAFFSLVIG FAFGALYWKK
     KQPNLTRTVE NIQINEEDNE ISMLQEKERE FQEV
 
 
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