LIFR_MOUSE
ID LIFR_MOUSE Reviewed; 1092 AA.
AC P42703; Q5I0Y2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Leukemia inhibitory factor receptor;
DE Short=LIF receptor;
DE Short=LIF-R;
DE AltName: Full=D-factor/LIF receptor;
DE AltName: CD_antigen=CD118;
DE Flags: Precursor;
GN Name=Lifr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1915266; DOI=10.1002/j.1460-2075.1991.tb07833.x;
RA Gearing D.P., Thut C.J., Vanden Bos T., Gimpel S.D., Delaney P.B., King J.,
RA Price V., Cosman D., Beckmann M.P.;
RT "Leukemia inhibitory factor receptor is structurally related to the IL-6
RT signal transducer, gp130.";
RL EMBO J. 10:2839-2848(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=ICR; TISSUE=Liver;
RX PubMed=7901054; DOI=10.1016/0014-5793(93)81710-h;
RA Tomida M., Yamamoto-Yamaguchi Y., Hozumi M.;
RT "Pregnancy associated increase in mRNA for soluble D-factor/LIF receptor in
RT mouse liver.";
RL FEBS Lett. 334:193-197(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=8056772; DOI=10.1093/oxfordjournals.jbchem.a124375;
RA Tomida M., Yamamoto-Yamaguchi Y., Hozumi M.;
RT "Three different cDNAs encoding mouse D-factor/LIF receptor.";
RL J. Biochem. 115:557-562(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Liver;
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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385; ASN-402 AND ASN-675.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385 AND ASN-658.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 49-529 IN COMPLEX WITH HUMAN LIF,
RP DISULFIDE BOND, AND GLYCOSYLATION AT ASN-164; ASN-199; ASN-238; ASN-261;
RP ASN-385; ASN-402; ASN-421; ASN-440 AND ASN-453.
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: Signal-transducing molecule. May have a common pathway with
CC IL6ST. The soluble form inhibits the biological activity of LIF by
CC blocking its binding to receptors on target cells.
CC -!- SUBUNIT: Heterodimer composed of LIFR and IL6ST. The heterodimer formed
CC by LIFR and IL6ST interacts with the complex formed by CNTF and CNTFR
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Membrane;
CC IsoId=P42703-1; Sequence=Displayed;
CC Name=2; Synonyms=Secreted;
CC IsoId=P42703-2; Sequence=VSP_001686, VSP_001687;
CC -!- TISSUE SPECIFICITY: Placenta, liver, kidney, heart, lung, brain, and
CC embryos. The liver may be the primary site of synthesis of the secreted
CC form.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; S73496; AAC60698.1; -; mRNA.
DR EMBL; S73495; AAC60697.1; -; mRNA.
DR EMBL; D26177; BAA05165.1; -; mRNA.
DR EMBL; D17444; BAA04258.1; -; mRNA.
DR EMBL; BC031929; AAH31929.1; -; mRNA.
DR CCDS; CCDS27369.1; -. [P42703-1]
DR CCDS; CCDS49577.1; -. [P42703-2]
DR PIR; JX0312; JX0312.
DR RefSeq; NP_001106857.1; NM_001113386.1. [P42703-2]
DR RefSeq; NP_038612.1; NM_013584.2. [P42703-1]
DR RefSeq; XP_006520030.1; XM_006519967.3.
DR RefSeq; XP_006520032.1; XM_006519969.3. [P42703-1]
DR RefSeq; XP_006520033.1; XM_006519970.3. [P42703-2]
DR RefSeq; XP_006520034.1; XM_006519971.2. [P42703-2]
DR RefSeq; XP_011243628.1; XM_011245326.2. [P42703-1]
DR PDB; 2Q7N; X-ray; 4.00 A; A/C=50-529.
DR PDBsum; 2Q7N; -.
DR AlphaFoldDB; P42703; -.
DR SMR; P42703; -.
DR BioGRID; 201163; 8.
DR DIP; DIP-5772N; -.
DR IntAct; P42703; 1.
DR STRING; 10090.ENSMUSP00000126137; -.
DR GlyConnect; 2478; 4 N-Linked glycans (3 sites).
DR GlyGen; P42703; 16 sites, 4 N-linked glycans (3 sites).
DR iPTMnet; P42703; -.
DR PhosphoSitePlus; P42703; -.
DR CPTAC; non-CPTAC-3515; -.
DR jPOST; P42703; -.
DR MaxQB; P42703; -.
DR PaxDb; P42703; -.
DR PeptideAtlas; P42703; -.
DR PRIDE; P42703; -.
DR ProteomicsDB; 286197; -. [P42703-1]
DR ProteomicsDB; 286198; -. [P42703-2]
DR Antibodypedia; 4137; 472 antibodies from 31 providers.
DR DNASU; 16880; -.
DR Ensembl; ENSMUST00000067190; ENSMUSP00000064551; ENSMUSG00000054263. [P42703-1]
DR Ensembl; ENSMUST00000164529; ENSMUSP00000131434; ENSMUSG00000054263. [P42703-2]
DR Ensembl; ENSMUST00000171588; ENSMUSP00000126137; ENSMUSG00000054263. [P42703-1]
DR Ensembl; ENSMUST00000226471; ENSMUSP00000154750; ENSMUSG00000054263. [P42703-1]
DR Ensembl; ENSMUST00000226934; ENSMUSP00000153968; ENSMUSG00000054263. [P42703-2]
DR Ensembl; ENSMUST00000227727; ENSMUSP00000154181; ENSMUSG00000054263. [P42703-2]
DR GeneID; 16880; -.
DR KEGG; mmu:16880; -.
DR UCSC; uc007vdw.2; mouse. [P42703-2]
DR UCSC; uc007vdx.2; mouse. [P42703-1]
DR CTD; 3977; -.
DR MGI; MGI:96788; Lifr.
DR VEuPathDB; HostDB:ENSMUSG00000054263; -.
DR eggNOG; ENOG502QQF6; Eukaryota.
DR GeneTree; ENSGT00940000155776; -.
DR HOGENOM; CLU_283805_0_0_1; -.
DR InParanoid; P42703; -.
DR OMA; HYVKIRC; -.
DR OrthoDB; 331447at2759; -.
DR PhylomeDB; P42703; -.
DR TreeFam; TF338122; -.
DR Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
DR BioGRID-ORCS; 16880; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Lifr; mouse.
DR EvolutionaryTrace; P42703; -.
DR PRO; PR:P42703; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P42703; protein.
DR Bgee; ENSMUSG00000054263; Expressed in diaphysis of femur and 286 other tissues.
DR ExpressionAtlas; P42703; baseline and differential.
DR Genevisible; P42703; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0004897; F:ciliary neurotrophic factor receptor activity; ISO:MGI.
DR GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; ISO:MGI.
DR GO; GO:0019955; F:cytokine binding; ISO:MGI.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0004923; F:leukemia inhibitory factor receptor activity; ISO:MGI.
DR GO; GO:0004924; F:oncostatin-M receptor activity; ISO:MGI.
DR GO; GO:0031100; P:animal organ regeneration; ISO:MGI.
DR GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0048861; P:leukemia inhibitory factor signaling pathway; ISO:MGI.
DR GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 8.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040817; LIFR_D2.
DR InterPro; IPR040901; LIFR_N.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF17971; LIFR_D2; 1.
DR Pfam; PF18207; LIFR_N; 1.
DR SMART; SM00060; FN3; 5.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..1092
FT /note="Leukemia inhibitory factor receptor"
FT /id="PRO_0000010903"
FT TOPO_DOM 44..828
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..1092
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..126
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 330..429
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 430..529
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 533..624
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 622..714
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 719..828
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1009..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 514..518
FT /note="WSXWS motif"
FT MOTIF 864..872
FT /note="Box 1 motif"
FT COMPBIAS 1024..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 922
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42702"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17652170"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17652170"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17652170"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17652170"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941, ECO:0000269|PubMed:17652170,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17652170"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17652170"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17652170"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17652170"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..63
FT /evidence="ECO:0000269|PubMed:17652170"
FT DISULFID 80..88
FT /evidence="ECO:0000269|PubMed:17652170"
FT DISULFID 208..265
FT /evidence="ECO:0000269|PubMed:17652170"
FT DISULFID 336..346
FT /evidence="ECO:0000269|PubMed:17652170"
FT DISULFID 461..506
FT /evidence="ECO:0000269|PubMed:17652170"
FT VAR_SEQ 718..719
FT /note="AP -> EA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1915266, ECO:0000303|PubMed:7901054,
FT ECO:0000303|PubMed:8056772"
FT /id="VSP_001686"
FT VAR_SEQ 720..1092
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1915266, ECO:0000303|PubMed:7901054,
FT ECO:0000303|PubMed:8056772"
FT /id="VSP_001687"
SQ SEQUENCE 1092 AA; 122574 MW; 6F02BBC8E154DE70 CRC64;
MAAYSWWRQP SWMVDNKRSR MTPNLPWLLS ALTLLHLTMH ANGLKRGVQD LKCTTNNMRV
WDCTWPAPLG VSPGTVKDIC IKDRFHSCHP LETTNVKIPA LSPGDHEVTI NYLNGFQSKF
TLNEKDVSLI PETPEILDLS ADFFTSSLLL KWNDRGSALP HPSNATWEIK VLQNPRTEPV
ALVLLNTMLS GKDTVQHWNW TSDLPLQCAT HSVSIRWHID SPHFSGYKEW SDWSPLKNIS
WIRNTETNVF PQDKVVLAGS NMTICCMSPT KVLSGQIGNT LRPLIHLYGQ TVAIHILNIP
VSENSGTNII FITDDDVYGT VVFAGYPPDV PQKLSCETHD LKEIICSWNP GRITGLVGPR
NTEYTLFESI SGKSAVFHRI EGLTNETYRL GVQMHPGQEI HNFTLTGRNP LGQAQSAVVI
NVTERVAPHD PTSLKVKDIN STVVTFSWYL PGNFTKINLL CQIEICKANS KKEVRNATIR
GAEDSTYHVA VDKLNPYTAY TFRVRCSSKT FWKWSRWSDE KRHLTTEATP SKGPDTWREW
SSDGKNLIVY WKPLPINEAN GKILSYNVSC SLNEETQSVL EIFDPQHRAE IQLSKNDYII
SVVARNSAGS SPPSKIASME IPNDDITVEQ AVGLGNRIFL TWRHDPNMTC DYVIKWCNSS
RSEPCLLDWR KVPSNSTETV IESDQFQPGV RYNFYLYGCT NQGYQLLRSI IGYVEELAPI
VAPNFTVEDT SADSILVKWD DIPVEELRGF LRGYLFYFQK GERDTPKTRS LEPHHSDIKL
KNITDISQKT LRIADLQGKT SYHLVLRAYT HGGLGPEKSM FVVTKENSVG LIIAILIPVA
VAVIVGVVTS ILCYRKREWI KETFYPDIPN PENCKALQFQ KSVCEGSNAL KTLEMNPCTP
NNVEVLESRS IVPKIEDTEI ISPVAERPGE RSEVDPENHV VVSYCPPIIE EEITNPAADE
VGGASQVVYI DVQSMYQPQA KAEEEQDVDP VVVAGYKPQM RLPISPAVED TAAEDEEGKT
AGYRPQANVN TWNLVSPDSP RSTDSNNEVV SFGSPCSINS RQFLIPPKDE DSPKSNGGGW
SFTNFFQNKP ND
