GenomeNet

Database: UniProt
Entry: P15018
LinkDB: P15018
Original site: P15018 
ID   LIF_HUMAN               Reviewed;         202 AA.
AC   P15018; B2RCW7; B5MC23; Q52LZ2;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   07-OCT-2020, entry version 202.
DE   RecName: Full=Leukemia inhibitory factor;
DE            Short=LIF;
DE   AltName: Full=Differentiation-stimulating factor;
DE            Short=D factor;
DE   AltName: Full=Melanoma-derived LPL inhibitor;
DE            Short=MLPLI;
DE   AltName: INN=Emfilermin;
DE   Flags: Precursor;
GN   Name=LIF; Synonyms=HILDA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3143918; DOI=10.1038/336690a0;
RA   Moreau J.-F., Donaldson D.D., Bennett F., Witek-Giannotti J., Clark S.C.,
RA   Wong G.G.;
RT   "Leukaemia inhibitory factor is identical to the myeloid growth factor
RT   human interleukin for DA cells.";
RL   Nature 336:690-692(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2475312; DOI=10.1089/dna.1.1989.8.351;
RA   Lowe D.G., Nunes W., Bombara M., McCabe S., Ranges G.E., Henzel W.,
RA   Tomida M., Yamamoto-Yamaguchi Y., Hozumi M., Goeddel D.V.;
RT   "Genomic cloning and heterologous expression of human differentiation-
RT   stimulating factor.";
RL   DNA 8:351-359(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic stem cell;
RX   PubMed=15146197; DOI=10.1038/nbt971;
RA   Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., Li Y.,
RA   Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., Lebkowski J.,
RA   Stanton L.W.;
RT   "Transcriptome characterization elucidates signaling networks that control
RT   human ES cell growth and differentiation.";
RL   Nat. Biotechnol. 22:707-716(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1692837;
RA   Stahl J., Gearing D.P., Willson T.A., Brown M.A., King J.A., Gough N.M.;
RT   "Structural organization of the genes for murine and human leukemia
RT   inhibitory factor. Evolutionary conservation of coding and non-coding
RT   regions.";
RL   J. Biol. Chem. 265:8833-8841(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-202.
RX   PubMed=3128791; DOI=10.1073/pnas.85.8.2623;
RA   Gough N.M., Gearing D.P., King J.A., Willson T.A., Hilton D.J.,
RA   Nicola N.A., Metcalf D.;
RT   "Molecular cloning and expression of the human homologue of the murine gene
RT   encoding myeloid leukemia-inhibitory factor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:2623-2627(1988).
RN   [10]
RP   PROTEIN SEQUENCE OF 23-39.
RX   PubMed=2730639; DOI=10.1016/s0006-291x(89)80114-7;
RA   Mori M., Yamaguchi K., Abe K.;
RT   "Purification of a lipoprotein lipase-inhibiting protein produced by a
RT   melanoma cell line associated with cancer cachexia.";
RL   Biochem. Biophys. Res. Commun. 160:1085-1092(1989).
RN   [11]
RP   DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-31; ASN-56; ASN-85; ASN-95;
RP   ASN-118 AND ASN-138.
RX   PubMed=8489250; DOI=10.1006/abbi.1993.1243;
RA   Schmelzer C.H., Harris R.J., Butler D., Yedinak C.M., Wagner K.L.,
RA   Burton L.E.;
RT   "Glycosylation pattern and disulfide assignments of recombinant human
RT   differentiation-stimulating factor.";
RL   Arch. Biochem. Biophys. 302:484-489(1993).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-202 IN COMPLEX WITH IL6ST.
RX   PubMed=14527405; DOI=10.1016/s1097-2765(03)00365-4;
RA   Boulanger M.J., Bankovich A.J., Kortemme T., Baker D., Garcia K.C.;
RT   "Convergent mechanisms for recognition of divergent cytokines by the shared
RT   signaling receptor gp130.";
RL   Mol. Cell 12:577-589(2003).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 23-202 IN COMPLEX WITH MOUSE LIFR.
RX   PubMed=17652170; DOI=10.1073/pnas.0705577104;
RA   Huyton T., Zhang J.G., Luo C.S., Lou M.Z., Hilton D.J., Nicola N.A.,
RA   Garrett T.P.;
RT   "An unusual cytokine:Ig-domain interaction revealed in the crystal
RT   structure of leukemia inhibitory factor (LIF) in complex with the LIF
RT   receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12737-12742(2007).
CC   -!- FUNCTION: LIF has the capacity to induce terminal differentiation in
CC       leukemic cells. Its activities include the induction of hematopoietic
CC       differentiation in normal and myeloid leukemia cells, the induction of
CC       neuronal cell differentiation, and the stimulation of acute-phase
CC       protein synthesis in hepatocytes.
CC   -!- INTERACTION:
CC       P15018; O60760: HPGDS; NbExp=3; IntAct=EBI-1037189, EBI-10187349;
CC       P15018; P40189: IL6ST; NbExp=2; IntAct=EBI-1037189, EBI-1030834;
CC       P15018; Q15323: KRT31; NbExp=3; IntAct=EBI-1037189, EBI-948001;
CC       P15018; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-1037189, EBI-11953334;
CC       P15018; P61601: NCALD; NbExp=3; IntAct=EBI-1037189, EBI-749635;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P15018-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P15018-2; Sequence=VSP_045551, VSP_045552;
CC   -!- PHARMACEUTICAL: In phase II clinical trial. The drug is being developed
CC       by Amrad to assist embryo implantation in women who have failed to
CC       become pregnant despite assisted reproductive technologies (ART).
CC   -!- SIMILARITY: Belongs to the LIF/OSM family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Leukemia inhibitory factor entry;
CC       URL="https://en.wikipedia.org/wiki/Leukemia_inhibitory_factor";
DR   EMBL; X13967; CAA32147.1; -; mRNA.
DR   EMBL; M27053; AAA53188.1; -; Genomic_DNA.
DR   EMBL; M27052; AAA53188.1; JOINED; Genomic_DNA.
DR   EMBL; AC004264; AAC05174.1; -; Genomic_DNA.
DR   EMBL; M63420; AAA51699.1; -; Genomic_DNA.
DR   EMBL; CN409468; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK315310; BAG37714.1; -; mRNA.
DR   EMBL; CH471095; EAW59863.1; -; Genomic_DNA.
DR   EMBL; BC069540; AAH69540.1; -; mRNA.
DR   EMBL; BC093733; AAH93733.1; -; mRNA.
DR   EMBL; BC093735; AAH93735.1; -; mRNA.
DR   EMBL; J03261; AAA59517.1; -; Genomic_DNA.
DR   CCDS; CCDS13872.1; -. [P15018-1]
DR   CCDS; CCDS58799.1; -. [P15018-2]
DR   PIR; B36282; B36282.
DR   RefSeq; NP_001244064.1; NM_001257135.1. [P15018-2]
DR   RefSeq; NP_002300.1; NM_002309.4. [P15018-1]
DR   PDB; 1EMR; X-ray; 3.50 A; A=44-202.
DR   PDB; 1PVH; X-ray; 2.50 A; B/D=34-202.
DR   PDB; 2Q7N; X-ray; 4.00 A; B/D=23-202.
DR   PDBsum; 1EMR; -.
DR   PDBsum; 1PVH; -.
DR   PDBsum; 2Q7N; -.
DR   SMR; P15018; -.
DR   BioGRID; 110164; 5.
DR   CORUM; P15018; -.
DR   DIP; DIP-5769N; -.
DR   IntAct; P15018; 8.
DR   MINT; P15018; -.
DR   STRING; 9606.ENSP00000249075; -.
DR   GlyGen; P15018; 6 sites.
DR   iPTMnet; P15018; -.
DR   BioMuta; LIF; -.
DR   DMDM; 126279; -.
DR   EPD; P15018; -.
DR   MassIVE; P15018; -.
DR   PaxDb; P15018; -.
DR   PeptideAtlas; P15018; -.
DR   PRIDE; P15018; -.
DR   ProteomicsDB; 53100; -. [P15018-1]
DR   ProteomicsDB; 5976; -.
DR   Antibodypedia; 10647; 581 antibodies.
DR   Ensembl; ENST00000249075; ENSP00000249075; ENSG00000128342. [P15018-1]
DR   Ensembl; ENST00000403987; ENSP00000384450; ENSG00000128342. [P15018-2]
DR   GeneID; 3976; -.
DR   KEGG; hsa:3976; -.
DR   UCSC; uc003agz.3; human. [P15018-1]
DR   CTD; 3976; -.
DR   DisGeNET; 3976; -.
DR   EuPathDB; HostDB:ENSG00000128342.4; -.
DR   GeneCards; LIF; -.
DR   HGNC; HGNC:6596; LIF.
DR   HPA; ENSG00000128342; Tissue enhanced (gallbladder).
DR   MIM; 159540; gene.
DR   neXtProt; NX_P15018; -.
DR   OpenTargets; ENSG00000128342; -.
DR   PharmGKB; PA30370; -.
DR   eggNOG; ENOG502S3JD; Eukaryota.
DR   GeneTree; ENSGT00390000000059; -.
DR   HOGENOM; CLU_117011_0_0_1; -.
DR   InParanoid; P15018; -.
DR   KO; K05419; -.
DR   OMA; CNKYHVA; -.
DR   OrthoDB; 1240691at2759; -.
DR   PhylomeDB; P15018; -.
DR   TreeFam; TF336245; -.
DR   PathwayCommons; P15018; -.
DR   Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR   Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR   Reactome; R-HSA-6788467; IL-6-type cytokine receptor ligand interactions.
DR   SignaLink; P15018; -.
DR   SIGNOR; P15018; -.
DR   BioGRID-ORCS; 3976; 5 hits in 869 CRISPR screens.
DR   EvolutionaryTrace; P15018; -.
DR   GeneWiki; Leukemia_inhibitory_factor; -.
DR   GenomeRNAi; 3976; -.
DR   Pharos; P15018; Tbio.
DR   PRO; PR:P15018; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; P15018; protein.
DR   Bgee; ENSG00000128342; Expressed in left coronary artery and 163 other tissues.
DR   Genevisible; P15018; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
DR   GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL.
DR   GO; GO:0005146; F:leukemia inhibitory factor receptor binding; IDA:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR   GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0048861; P:leukemia inhibitory factor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR   GO; GO:0060463; P:lung lobe morphogenesis; IEA:Ensembl.
DR   GO; GO:0060426; P:lung vasculature development; IEA:Ensembl.
DR   GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR   GO; GO:0048644; P:muscle organ morphogenesis; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0046888; P:negative regulation of hormone secretion; IDA:MGI.
DR   GO; GO:0045835; P:negative regulation of meiotic nuclear division; IEA:Ensembl.
DR   GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR   GO; GO:0048711; P:positive regulation of astrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IMP:CACAO.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR   GO; GO:1901676; P:positive regulation of histone H3-K27 acetylation; IDA:BHF-UCL.
DR   GO; GO:0045651; P:positive regulation of macrophage differentiation; IDA:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR   GO; GO:0072108; P:positive regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; IDA:BHF-UCL.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IDA:BHF-UCL.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
DR   GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR   GO; GO:0072307; P:regulation of metanephric nephron tubule epithelial cell differentiation; IDA:BHF-UCL.
DR   GO; GO:1903025; P:regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0060708; P:spongiotrophoblast differentiation; IEA:Ensembl.
DR   GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
DR   GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
DR   GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR003624; Leukemia_IF.
DR   InterPro; IPR001581; Leukemia_IF/oncostatin.
DR   InterPro; IPR019827; Leukemia_IF/oncostatin_CS.
DR   PANTHER; PTHR10633; PTHR10633; 1.
DR   Pfam; PF01291; LIF_OSM; 1.
DR   PRINTS; PR01883; LEUKAEMIAIF.
DR   SMART; SM00080; LIF_OSM; 1.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00590; LIF_OSM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytokine; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Growth factor; Pharmaceutical;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:2730639"
FT   CHAIN           23..202
FT                   /note="Leukemia inhibitory factor"
FT                   /id="PRO_0000017715"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8489250"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8489250"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8489250"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8489250"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8489250"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8489250"
FT   DISULFID        34..156
FT                   /evidence="ECO:0000269|PubMed:8489250"
FT   DISULFID        40..153
FT                   /evidence="ECO:0000269|PubMed:8489250"
FT   DISULFID        82..185
FT                   /evidence="ECO:0000269|PubMed:8489250"
FT   VAR_SEQ         7..88
FT                   /note="GVVPLLLVLHWKHGAGSPLPITPVNATCAIRHPCHNNLMNQIRSQLAQLNGS
FT                   ANALFILYYTAQGEPFPNNLDKLCGPNVTD -> VHSPGGAVPQQPGQAMWPQRDGLPA
FT                   LPRQRHGEGQAGGAVPHSRVPWHLPGQHHPGPEDPQPQCPQPPQQAQRHRRHPARPP
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15146197"
FT                   /id="VSP_045551"
FT   VAR_SEQ         89..202
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15146197"
FT                   /id="VSP_045552"
FT   HELIX           44..70
FT                   /evidence="ECO:0000244|PDB:1PVH"
FT   TURN            72..77
FT                   /evidence="ECO:0000244|PDB:1PVH"
FT   HELIX           78..81
FT                   /evidence="ECO:0000244|PDB:1PVH"
FT   STRAND          82..84
FT                   /evidence="ECO:0000244|PDB:1EMR"
FT   STRAND          94..96
FT                   /evidence="ECO:0000244|PDB:1EMR"
FT   HELIX           98..126
FT                   /evidence="ECO:0000244|PDB:1PVH"
FT   HELIX           131..157
FT                   /evidence="ECO:0000244|PDB:1PVH"
FT   HELIX           177..199
FT                   /evidence="ECO:0000244|PDB:1PVH"
SQ   SEQUENCE   202 AA;  22008 MW;  634CD10BFF67A217 CRC64;
     MKVLAAGVVP LLLVLHWKHG AGSPLPITPV NATCAIRHPC HNNLMNQIRS QLAQLNGSAN
     ALFILYYTAQ GEPFPNNLDK LCGPNVTDFP PFHANGTEKA KLVELYRIVV YLGTSLGNIT
     RDQKILNPSA LSLHSKLNAT ADILRGLLSN VLCRLCSKYH VGHVDVTYGP DTSGKDVFQK
     KKLGCQLLGK YKQIIAVLAQ AF
//
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