| IED ID | IndEnz0016000153 |
| Enzyme Type ID | tyrosinase000153 |
| Protein Name |
Kit ligand Mast cell growth factor MGF Stem cell factor SCF c-Kit ligand Cleaved into: Soluble KIT ligand sKITLG |
| Gene Name | KITLG MGF SCF |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MKKTQTWILTCIYLQLLLFNPLVKTEGICRNRVTNNVKDVTKLVANLPKDYMITLKYVPGMDVLPSHCWISEMVVQLSDSLTDLLDKFSNISEGLSNYSIIDKLVNIVDDLVECVKENSSKDLKKSFKSPEPRLFTPEEFFRIFNRSIDAFKDFVVASETSDCVVSSTLSPEKDSRVSVTKPFMLPPVAASSLRNDSSSSNRKAKNPPGDSSLHWAAMALPALFSLIIGFAFGALYWKKRQPSLTRAVENIQINEEDNEISMLQEKEREFQEV |
| Enzyme Length | 273 |
| Uniprot Accession Number | P21583 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (3); Beta strand (5); Chain (2); Disulfide bond (2); Glycosylation (7); Helix (6); Natural variant (6); Sequence conflict (6); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1); Turn (2) |
| Keywords | 3D-structure;Alternative splicing;Cell adhesion;Cell membrane;Cell projection;Cytoplasm;Cytoskeleton;Deafness;Direct protein sequencing;Disease variant;Disulfide bond;Glycoprotein;Growth factor;Membrane;Non-syndromic deafness;Reference proteome;Secreted;Signal;Transmembrane;Transmembrane helix |
| Interact With | P10721 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:26522471}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:26522471}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, lamellipodium {ECO:0000269|PubMed:26522471}. Cell projection, filopodium {ECO:0000269|PubMed:26522471}.; SUBCELLULAR LOCATION: [Soluble KIT ligand]: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: A soluble form (sKITLG) is produced by proteolytic processing of isoform 1 in the extracellular domain. {ECO:0000269|PubMed:1381905}.; PTM: Found in two differentially glycosylated forms, LMW-SCF and HMW-SCF. LMW-SCF is fully N-glycosylated at Asn-145, partially N-glycosylated at Asn-90, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97 or Asn-118. HMW-SCF is N-glycosylated at Asn-118, Asn-90 and Asn-145, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97. {ECO:0000269|PubMed:1381905}.; PTM: A soluble form exists as a cleavage product of the extracellular domain. {ECO:0000269|PubMed:1381905}. |
| Signal Peptide | SIGNAL 1..25 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1EXZ; 1SCF; 2E9W; |
| Mapped Pubmed ID | 10022833; 10358045; 10374881; 10377264; 10523831; 10523834; 10679268; 11069563; 11395417; 11435302; 11494148; 11520784; 11707405; 11809791; 11905054; 11994499; 12002675; 12062105; 12062186; 12123753; 12192036; 12297464; 12393703; 12429808; 12444928; 12445210; 12556557; 12637332; 12660731; 12666065; 12753403; 12824176; 12829027; 12878163; 1371879; 1375232; 1381360; 14628073; 14654075; 14662725; 14691917; 14707129; 14985355; 15024050; 15140230; 15143187; 15145934; 15217825; 15308671; 15337769; 15378028; 15474101; 15475566; 15504546; 15504551; 15526978; 15576295; 15728521; 15781331; 15834429; 15866728; 16015044; 16129412; 16181409; 16213778; 16479403; 16483568; 16616334; 16647110; 16647379; 16709604; 16737840; 16780420; 16780589; 16873377; 16905672; 17115933; 17175329; 17191042; 17213284; 1721591; 17255936; 17344430; 17410437; 17556598; 17687495; 17855052; 17904548; 18026739; 18042633; 18083106; 18166170; 18239612; 18339685; 18372228; 18499891; 18588518; 18602222; 18606717; 18617639; 18684968; 18697750; 18754654; 18829560; 18830255; 18834862; 18928604; 19001805; 19074504; 19196101; 19197368; 19285034; 19342032; 19411071; 19416273; 19480722; 19481739; 19483681; 19483682; 19492092; 19570824; 19644473; 19675587; 19805105; 19897599; 19912360; 19913121; 20028869; 20117079; 20131076; 20237496; 20304997; 20305142; 20337985; 20353940; 20384797; 20396801; 20522708; 20596251; 20608808; 20628086; 20713702; 20857409; 21030588; 21094786; 21102635; 21161069; 21257825; 21281800; 21317208; 21320746; 21368164; 21368769; 21372320; 21617256; 21636540; 21668414; 21763396; 21799876; 21827948; 21976531; 22004924; 22072546; 22140272; 22188813; 22194441; 22204707; 22279057; 22349512; 22467521; 22533504; 22588880; 22802530; 22833529; 23060556; 23125456; 23185384; 23273644; 23303910; 23662587; 23680593; 23703692; 24083421; 24116170; 24120139; 24449920; 24745671; 24790137; 24897070; 24937142; 24944064; 24999927; 25061857; 25086759; 25161061; 25213795; 25220285; 25241372; 25241761; 25401222; 25418470; 25457384; 25514101; 25766327; 25799412; 25962936; 26049754; 26177551; 26179221; 26188365; 26666817; 26704889; 26791471; 26853551; 26909822; 27536065; 27762658; 27859606; 28064312; 28153790; 28285567; 28290616; 28370370; 28456630; 28551414; 28714970; 28880927; 28954236; 29112292; 29631773; 29704617; 30091263; 30142893; 30298755; 30388134; 30617299; 31138788; 31530062; 31612386; 31870114; 32189379; 32203862; 32223088; 32327564; 32336682; 32463597; 32578480; 32736659; 33407466; 34450114; 34716665; 35023029; 7506952; 7509796; 7523381; 7526158; 7536744; 7680037; 7684496; 8611693; 8636116; 8647802; 8657148; 8695790; 8774734; 8950973; 9038210; 9045650; 9111318; 9256427; 9341198; 9355737; 9446650; 9528781; 9788619; 9799234; 9872323; |
| Motif | |
| Gene Encoded By | |
| Mass | 30,899 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |