Leukemia inhibitory factor precursor

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P09056 (LIF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Leukemia inhibitory factor
Short name=LIF

Alternative name(s):
Differentiation-stimulating factor
Short name=D factor

Gene names

Name:

Lif

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	203 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes.
Subcellular location	Secreted.
Sequence similarities	Belongs to the LIF/OSM family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Cytokine Growth factor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood vessel remodeling Inferred from genetic interaction PubMed 16691571. Source: MGI decidualization Inferred from direct assay PubMed 1522892. Source: MGI embryo implantation Inferred from direct assay PubMed 1522892. Source: MGI immune response Inferred from electronic annotation. Source: InterPro leukemia inhibitory factor signaling pathway Inferred from electronic annotation. Source: Compara lung alveolus development Inferred from genetic interaction PubMed 16691571. Source: MGI lung lobe morphogenesis Inferred from genetic interaction PubMed 16691571. Source: MGI lung vasculature development Inferred from genetic interaction PubMed 16691571. Source: MGI muscle organ morphogenesis Inferred from mutant phenotype PubMed 15716414. Source: MGI negative regulation of ERK1 and ERK2 cascade Inferred from genetic interaction PubMed 16691571. Source: MGI negative regulation of cell proliferation Inferred from genetic interaction PubMed 16691571. Source: MGI negative regulation of hormone secretion Inferred from electronic annotation. Source: Compara negative regulation of meiosis Inferred from direct assay PubMed 11203703. Source: MGI neuron development Inferred from genetic interaction PubMed 15716414. Source: MGI positive regulation of MAPK cascade Inferred from electronic annotation. Source: Compara positive regulation of astrocyte differentiation Inferred from direct assay PubMed 10486560. Source: MGI positive regulation of cell proliferation Inferred from mutant phenotype PubMed 1522892. Source: MGI positive regulation of macrophage differentiation Inferred from electronic annotation. Source: Compara positive regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-serine phosphorylation of STAT protein Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 16691571. Source: MGI positive regulation of tyrosine phosphorylation of Stat1 protein Inferred from electronic annotation. Source: Compara positive regulation of tyrosine phosphorylation of Stat3 protein Inferred from electronic annotation. Source: Compara regulation of metanephric nephron tubule epithelial cell differentiation Inferred from electronic annotation. Source: Compara spongiotrophoblast differentiation Inferred from genetic interaction PubMed 16258063. Source: MGI stem cell maintenance Inferred from direct assay PubMed 15358627. Source: MGI trophoblast giant cell differentiation Inferred from genetic interaction PubMed 16258063. Source: MGI tyrosine phosphorylation of Stat3 protein Inferred from direct assay PubMed 15012602. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara extracellular space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cytokine activity Inferred from direct assay PubMed 15012602 PubMed 1522892. Source: MGI growth factor activity Inferred from mutant phenotype PubMed 1522892. Source: MGI leukemia inhibitory factor receptor binding Inferred from sequence orthology PubMed 7957045. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

Ref.6

Chain

24 – 203

180

Leukemia inhibitory factor

PRO_0000017716

Amino acid modifications

Glycosylation

N-linked (GlcNAc...)

Glycosylation

N-linked (GlcNAc...)

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

119

N-linked (GlcNAc...)

Glycosylation

139

N-linked (GlcNAc...)

Disulfide bond

Disulfide bond

Disulfide bond

Secondary structure

203

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P09056 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: F5C65EF11A67A835
Show »

FASTA

203

22,287

        10         20         30         40         50         60 
MKVLAAGIVP LLLLVLHWKH GAGSPLPITP VNATCAIRHP CHGNLMNQIK NQLAQLNGSA 

        70         80         90        100        110        120 
NALFISYYTA QGEPFPNNVE KLCAPNMTDF PSFHGNGTEK TKLVELYRMV AYLSASLTNI 

       130        140        150        160        170        180 
TRDQKVLNPT AVSLQVKLNA TIDVMRGLLS NVLCRLCNKY RVGHVDVPPV PDHSDKEAFQ 

       190        200 
RKKLGCQLLG TYKQVISVVV QAF

« Hide

References

[1]	"Complete sequence of murine myeloid leukaemia inhibitory factor (LIF)." Gough N.M., Gearing D.P., King J.A. Nucleic Acids Res. 16:9857-9857(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural organization of the genes for murine and human leukemia inhibitory factor. Evolutionary conservation of coding and non-coding regions." Stahl J., Gearing D.P., Willson T.A., Brown M.A., King J.A., Gough N.M. J. Biol. Chem. 265:8833-8841(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence polymorphisms in the chemokines Scya1 (TCA-3), Scya2 (monocyte chemoattractant protein (MCP)-1), and Scya12 (MCP-5) are candidates for eae7, a locus controlling susceptibility to monophasic remitting/nonrelapsing experimental allergic encephalomyelitis." Teuscher C., Butterfield R.J., Ma R.Z., Zachary J.F., Doerge R.W., Blankenhorn E.P. J. Immunol. 163:2262-2266(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: B10.S/J and SJL/J. Tissue: Spleen.
[4]	"Molecular cloning and expression of cDNA encoding a murine myeloid leukaemia inhibitory factor (LIF)." Gearing D.P., Gough N.M., King J.A., Hilton D.J., Nicola N.A., Simpson R.J., Nice E.C., Kelso A., Metcalf D. EMBO J. 6:3995-4002(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-203, PROTEIN SEQUENCE OF 195-203.
[5]	"Biochemical characterization of murine leukaemia inhibitory factor produced by Krebs ascites and by yeast cells." Gough N.M., Hilton D.J., Gearing D.P., Willson T.A., King J.A., Nicola N.A., Metcalf D. Blood Cells 14:431-442(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 178-203.
[6]	"Genomic cloning and heterologous expression of human differentiation-stimulating factor." Lowe D.G., Nunes W., Bombara M., McCabe S., Ranges G.E., Henzel W., Tomida M., Yamamoto-Yamaguchi Y., Hozumi M., Goeddel D.V. DNA 8:351-359(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-81 AND 108-176.
[7]	"The disulfide bond arrangement of leukemia inhibitory factor: homology to oncostatin M and structural implications." Nicola N.A., Cross B., Simpson R.J. Biochem. Biophys. Res. Commun. 190:20-26(1993) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS.
[8]	"The crystal structure and biological function of leukemia inhibitory factor: implications for receptor binding." Robinson R.C., Grey L.M., Staunton D., Vankelecom H., Vernallis A.B., Moreau J.-F., Stuart D.I., Heath J.K., Jones E.Y. Cell 77:1101-1116(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[9]	"Solution dynamics and secondary structure of murine leukemia inhibitory factor: a four-helix cytokine with a rigid CD loop." Purvis D.H., Mabbutt B.C. Biochemistry 36:10146-10154(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[10]	"Solution structure of leukemia inhibitory factor." Hinds M.G., Maurer T., Zhang J.G., Nicola N.A., Norton R.S. J. Biol. Chem. 273:13738-13745(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF HUMAN-MOUSE CHIMERA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12810 mRNA. Translation: CAA31299.1.
X06381 mRNA. Translation: CAA29680.1.
AF065917 mRNA. Translation: AAC17912.1.
AF065918 mRNA. Translation: AAC17913.1.
M63419 Genomic DNA. Translation: AAA37211.1.
M57691 mRNA. Translation: AAA63388.1.

IPI

IPI00132476.

PIR

A36282.

RefSeq

NP_032527.1. NM_008501.2.

UniGene

Mm.4964.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A7M	NMR	-	A	24-203	[»]
1LKI	X-ray	2.00	A	24-203	[»]

ProteinModelPortal

P09056.

SMR

P09056. Positions 32-203.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5771N.

STRING

10090.ENSMUSP00000105579.

Proteomic databases

PRIDE

P09056.

Protocols and materials databases

DNASU

16878.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000066283; ENSMUSP00000067066; ENSMUSG00000034394.

GeneID

16878.

KEGG

mmu:16878.

Organism-specific databases

CTD

3976.

MGI

MGI:96787. Lif.

Phylogenomic databases

eggNOG

NOG45686.

GeneTree

ENSGT00390000000059.

HOGENOM

HOG000059647.

HOVERGEN

HBG006267.

InParanoid

P09056.

K05419.

OMA

KYHVAHV.

OrthoDB

EOG4RXZ18.

Gene expression databases

ArrayExpress

P09056.

Bgee

P09056.

CleanEx

MM_LIF.

Genevestigator

P09056.

GermOnline

ENSMUSG00000034394. Mus musculus.

Family and domain databases

Gene3D

1.20.1250.10. 1 hit.

InterPro

IPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR003624. Leukemia_IF.
IPR001581. Leukemia_IF/oncostatin.
IPR019827. Leukemia_IF/oncostatin_CS.
[Graphical view]

PANTHER

PTHR10633. PTHR10633. 1 hit.

Pfam

PF01291. LIF_OSM. 1 hit.
[Graphical view]

PRINTS

PR01883. LEUKAEMIAIF.

SMART

SM00080. LIF_OSM. 1 hit.
[Graphical view]

SUPFAM

SSF47266. 4_helix_cytokine. 1 hit.

PROSITE

PS00590. LIF_OSM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P09056.

NextBio

290872.

SOURCE

Search...

Entry information

Entry name

LIF_MOUSE

Accession

Primary (citable) accession number: P09056

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	April 3, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents