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SCF_PIG
ID   SCF_PIG                 Reviewed;         274 AA.
AC   Q29030; Q2WG86;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 112.
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=MGF;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Uterus;
RX   PubMed=7508758; DOI=10.1095/biolreprod50.1.95;
RA   Zhang Z., Anthony R.V.;
RT   "Porcine stem cell factor/c-kit ligand: its molecular cloning and
RT   localization within the uterus.";
RL   Biol. Reprod. 50:95-102(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-124; ASN-149 AND ALA-248.
RC   TISSUE=Kidney;
RX   PubMed=16441305; DOI=10.1111/j.1365-2052.2005.01404.x;
RA   Okumura N., Hayashi T., Sekikawa H., Matsumoto T., Mikawa A., Hamasima N.,
RA   Awata T.;
RT   "Sequencing, mapping and nucleotide variation of porcine coat color genes
RT   EDNRB, MYO5A, KITLG, SLC45A2, RAB27A, SILV and MITF.";
RL   Anim. Genet. 37:80-82(2006).
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   -!- 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; L07786; AAA53670.1; -; mRNA.
DR   EMBL; AB209954; BAE48720.1; -; mRNA.
DR   PIR; I46575; I46575.
DR   RefSeq; NP_999434.2; NM_214269.2.
DR   RefSeq; XP_013853552.1; XM_013998098.1.
DR   AlphaFoldDB; Q29030; -.
DR   SMR; Q29030; -.
DR   STRING; 9823.ENSSSCP00000000985; -.
DR   PaxDb; Q29030; -.
DR   GeneID; 397509; -.
DR   KEGG; ssc:397509; -.
DR   CTD; 4254; -.
DR   eggNOG; ENOG502QTGT; Eukaryota.
DR   InParanoid; Q29030; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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: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   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:0000250"
FT   CHAIN           26..274
FT                   /note="Kit ligand"
FT                   /id="PRO_0000031916"
FT   CHAIN           26..191
FT                   /note="Soluble KIT ligand"
FT                   /id="PRO_0000292277"
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"
FT   VARIANT         124
FT                   /note="K -> R"
FT                   /evidence="ECO:0000269|PubMed:16441305"
FT   VARIANT         149
FT                   /note="D -> N"
FT                   /evidence="ECO:0000269|PubMed:16441305"
FT   VARIANT         248
FT                   /note="T -> A"
FT                   /evidence="ECO:0000269|PubMed:16441305"
SQ   SEQUENCE   274 AA;  31119 MW;  FF3C87114D7BA6A6 CRC64;
     MKKTQTWIIT CIYLQLLLFN PLVRTQGICR NRVTDDVKDV TKLVANLPKD YKITLKYVPG
     MDVLPSHCWI SEMVEQLSVS LTDLLDKFSN ISEGLSNYSI IDKLVKIVDD LVECMEEHSF
     ENVKKSSKSP EPRLFTPEKF FGIFNRSIDA FKDLEMVAPK TSECVISSTL TPEKDSRVSV
     TKPFMLPPVA ASSLRNDSSS SNRKASDSIE DSSLQWAAVA LPAFFSLVIG FAFGALYWKK
     KQPNLTRTVE NIQINEEDNE ISMLQEKERE FQEV
 
 
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