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P42703 (LIFR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leukemia inhibitory factor receptor
Short name=LIF receptor
Short name=LIF-R
Alternative name(s):
D-factor/LIF receptor
CD_antigen=CD118
Gene names
Name:Lifr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1092 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells.

Subunit structure

Heterodimer composed of LIFR and IL6ST. The heterodimer formed by LIFR and IL6ST interacts with the complex formed by CNTF and CNTFR By similarity.

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein.

Isoform 2: Secreted.

Tissue specificity

Placenta, liver, kidney, heart, lung, brain, and embryos. The liver may be the primary site of synthesis of the secreted form.

Domain

The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.

The box 1 motif is required for JAK interaction and/or activation.

Sequence similarities

Belongs to the type I cytokine receptor family. Type 2 subfamily.

Contains 6 fibronectin type-III domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P42703-1)

Also known as: Membrane;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P42703-2)

Also known as: Secreted;

The sequence of this isoform differs from the canonical sequence as follows:
     718-719: AP → EA
     720-1092: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4343 Potential
Chain44 – 10921049Leukemia inhibitory factor receptor
PRO_0000010903

Regions

Topological domain44 – 828785Extracellular Potential
Transmembrane829 – 85325Helical; Potential
Topological domain854 – 1092239Cytoplasmic Potential
Domain45 – 12682Fibronectin type-III 1
Domain327 – 42397Fibronectin type-III 2
Domain428 – 52295Fibronectin type-III 3
Domain530 – 62091Fibronectin type-III 4
Domain622 – 71493Fibronectin type-III 5
Domain719 – 824106Fibronectin type-III 6
Motif514 – 5185WSXWS motif
Motif864 – 8729Box 1 motif

Amino acid modifications

Modified residue9221Phosphoserine By similarity
Glycosylation1641N-linked (GlcNAc...) Ref.8
Glycosylation1991N-linked (GlcNAc...) Ref.8
Glycosylation2381N-linked (GlcNAc...) Ref.8
Glycosylation2611N-linked (GlcNAc...) Ref.8
Glycosylation3851N-linked (GlcNAc...) Ref.5 Ref.6 Ref.7 Ref.8
Glycosylation4021N-linked (GlcNAc...) Ref.5 Ref.8
Glycosylation4211N-linked (GlcNAc...) Ref.8
Glycosylation4401N-linked (GlcNAc...) Ref.8
Glycosylation4531N-linked (GlcNAc...) Ref.8
Glycosylation4761N-linked (GlcNAc...) Potential
Glycosylation5671N-linked (GlcNAc...) Potential
Glycosylation6471N-linked (GlcNAc...) Potential
Glycosylation6581N-linked (GlcNAc...) Ref.6
Glycosylation6751N-linked (GlcNAc...) Ref.5
Glycosylation7241N-linked (GlcNAc...) Potential
Glycosylation7821N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 63 Ref.8
Disulfide bond80 ↔ 88 Ref.8
Disulfide bond208 ↔ 265 Ref.8
Disulfide bond336 ↔ 346 Ref.8
Disulfide bond461 ↔ 506 Ref.8

Natural variations

Alternative sequence718 – 7192AP → EA in isoform 2.
VSP_001686
Alternative sequence720 – 1092373Missing in isoform 2.
VSP_001687

Secondary structure

1 ......................................................................... 1092
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Membrane) [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 6F02BBC8E154DE70

FASTA1,092122,574
        10         20         30         40         50         60 
MAAYSWWRQP SWMVDNKRSR MTPNLPWLLS ALTLLHLTMH ANGLKRGVQD LKCTTNNMRV 

        70         80         90        100        110        120 
WDCTWPAPLG VSPGTVKDIC IKDRFHSCHP LETTNVKIPA LSPGDHEVTI NYLNGFQSKF 

       130        140        150        160        170        180 
TLNEKDVSLI PETPEILDLS ADFFTSSLLL KWNDRGSALP HPSNATWEIK VLQNPRTEPV 

       190        200        210        220        230        240 
ALVLLNTMLS GKDTVQHWNW TSDLPLQCAT HSVSIRWHID SPHFSGYKEW SDWSPLKNIS 

       250        260        270        280        290        300 
WIRNTETNVF PQDKVVLAGS NMTICCMSPT KVLSGQIGNT LRPLIHLYGQ TVAIHILNIP 

       310        320        330        340        350        360 
VSENSGTNII FITDDDVYGT VVFAGYPPDV PQKLSCETHD LKEIICSWNP GRITGLVGPR 

       370        380        390        400        410        420 
NTEYTLFESI SGKSAVFHRI EGLTNETYRL GVQMHPGQEI HNFTLTGRNP LGQAQSAVVI 

       430        440        450        460        470        480 
NVTERVAPHD PTSLKVKDIN STVVTFSWYL PGNFTKINLL CQIEICKANS KKEVRNATIR 

       490        500        510        520        530        540 
GAEDSTYHVA VDKLNPYTAY TFRVRCSSKT FWKWSRWSDE KRHLTTEATP SKGPDTWREW 

       550        560        570        580        590        600 
SSDGKNLIVY WKPLPINEAN GKILSYNVSC SLNEETQSVL EIFDPQHRAE IQLSKNDYII 

       610        620        630        640        650        660 
SVVARNSAGS SPPSKIASME IPNDDITVEQ AVGLGNRIFL TWRHDPNMTC DYVIKWCNSS 

       670        680        690        700        710        720 
RSEPCLLDWR KVPSNSTETV IESDQFQPGV RYNFYLYGCT NQGYQLLRSI IGYVEELAPI 

       730        740        750        760        770        780 
VAPNFTVEDT SADSILVKWD DIPVEELRGF LRGYLFYFQK GERDTPKTRS LEPHHSDIKL 

       790        800        810        820        830        840 
KNITDISQKT LRIADLQGKT SYHLVLRAYT HGGLGPEKSM FVVTKENSVG LIIAILIPVA 

       850        860        870        880        890        900 
VAVIVGVVTS ILCYRKREWI KETFYPDIPN PENCKALQFQ KSVCEGSNAL KTLEMNPCTP 

       910        920        930        940        950        960 
NNVEVLESRS IVPKIEDTEI ISPVAERPGE RSEVDPENHV VVSYCPPIIE EEITNPAADE 

       970        980        990       1000       1010       1020 
VGGASQVVYI DVQSMYQPQA KAEEEQDVDP VVVAGYKPQM RLPISPAVED TAAEDEEGKT 

      1030       1040       1050       1060       1070       1080 
AGYRPQANVN TWNLVSPDSP RSTDSNNEVV SFGSPCSINS RQFLIPPKDE DSPKSNGGGW 

      1090 
SFTNFFQNKP ND

« Hide

Isoform 2 (Secreted) [UniParc].

Checksum: 4DF1779816B06D2B
Show »

FASTA71981,287

References

« Hide 'large scale' references
[1]"Leukemia inhibitory factor receptor is structurally related to the IL-6 signal transducer, gp130."
Gearing D.P., Thut C.J., Vanden Bos T., Gimpel S.D., Delaney P.B., King J., Price V., Cosman D., Beckmann M.P.
EMBO J. 10:2839-2848(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Pregnancy associated increase in mRNA for soluble D-factor/LIF receptor in mouse liver."
Tomida M., Yamamoto-Yamaguchi Y., Hozumi M.
FEBS Lett. 334:193-197(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: ICR.
Tissue: Liver.
[3]"Three different cDNAs encoding mouse D-factor/LIF receptor."
Tomida M., Yamamoto-Yamaguchi Y., Hozumi M.
J. Biochem. 115:557-562(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: FVB/N.
Tissue: Liver.
[5]"Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385; ASN-402 AND ASN-675, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Plasma.
[6]"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
Bernhard O.K., Kapp E.A., Simpson R.J.
J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385 AND ASN-658, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Plasma.
[7]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385, MASS SPECTROMETRY.
[8]"An unusual cytokine:Ig-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor."
Huyton T., Zhang J.G., Luo C.S., Lou M.Z., Hilton D.J., Nicola N.A., Garrett T.P.
Proc. Natl. Acad. Sci. U.S.A. 104:12737-12742(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 49-529 IN COMPLEX WITH HUMAN LIF, DISULFIDE BOND, GLYCOSYLATION AT ASN-164; ASN-199; ASN-238; ASN-261; ASN-385; ASN-402; ASN-421; ASN-440 AND ASN-453.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S73496 mRNA. Translation: AAC60698.1.
S73495 mRNA. Translation: AAC60697.1.
D26177 mRNA. Translation: BAA05165.1.
D17444 mRNA. Translation: BAA04258.1.
BC031929 mRNA. Translation: AAH31929.1.
IPIIPI00119299.
IPI00407541.
PIRJX0312.
RefSeqNP_001106857.1. NM_001113386.1.
NP_038612.1. NM_013584.2.
UniGeneMm.149720.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q7NX-ray4.00A/C50-529[»]
ProteinModelPortalP42703.
SMRP42703. Positions 50-817.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5772N.
MINTMINT-4100386.

PTM databases

PhosphoSiteP42703.

Proteomic databases

PaxDbP42703.
PRIDEP42703.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067190; ENSMUSP00000064551; ENSMUSG00000054263.
ENSMUST00000164529; ENSMUSP00000131434; ENSMUSG00000054263.
ENSMUST00000171588; ENSMUSP00000126137; ENSMUSG00000054263.
GeneID16880.
KEGGmmu:16880.
UCSCuc007vdw.2. mouse.
uc007vdx.2. mouse.

Organism-specific databases

CTD3977.
MGIMGI:96788. Lifr.

Phylogenomic databases

eggNOGNOG147644.
GeneTreeENSGT00550000074436.
HOGENOMHOG000113324.
HOVERGENHBG006266.
InParanoidQ5I0Y2.
KOK05058.
OMAIKETFYP.
OrthoDBEOG4G7BXJ.

Gene expression databases

BgeeP42703.
CleanExMM_LIFR.
GenevestigatorP42703.
GermOnlineENSMUSG00000054263. Mus musculus.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR003961. Fibronectin_type3.
IPR003529. Hematopoietin_rcpt_Gp130_CS.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF00041. fn3. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 5 hits.
[Graphical view]
SUPFAMSSF49265. FN_III-like. 5 hits.
PROSITEPS50853. FN3. 5 hits.
PS01353. HEMATOPO_REC_L_F2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP42703.
NextBio290878.
SOURCESearch...

Entry information

Entry nameLIFR_MOUSE
AccessionPrimary (citable) accession number: P42703
Secondary accession number(s): Q5I0Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 29, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents