ID LIFR_RAT Reviewed; 1093 AA.
AC O70535;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 24-JAN-2024, entry version 137.
DE RecName: Full=Leukemia inhibitory factor receptor;
DE Short=LIF receptor;
DE Short=LIF-R;
DE AltName: CD_antigen=CD118;
DE Flags: Precursor;
GN Name=Lifr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wister-Imamichi; TISSUE=Liver;
RX PubMed=9349722; DOI=10.1016/s0167-4781(97)00079-1;
RA Aikawa J., Ikeda-Naiki S., Ohgane J., Min K.S., Imamura T., Sasai K.,
RA Shiota K., Ogawa T.;
RT "Molecular cloning of rat leukemia inhibitory factor receptor alpha-chain
RT gene and its expression during pregnancy.";
RL Biochim. Biophys. Acta 1353:266-276(1997).
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 (By similarity).
CC {ECO:0000250}.
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: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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; D86345; BAA25907.1; -; mRNA.
DR RefSeq; NP_112310.1; NM_031048.1.
DR AlphaFoldDB; O70535; -.
DR SMR; O70535; -.
DR STRING; 10116.ENSRNOP00000016036; -.
DR GlyCosmos; O70535; 16 sites, No reported glycans.
DR GlyGen; O70535; 16 sites.
DR PhosphoSitePlus; O70535; -.
DR SwissPalm; O70535; -.
DR PaxDb; 10116-ENSRNOP00000016036; -.
DR GeneID; 81680; -.
DR KEGG; rno:81680; -.
DR UCSC; RGD:621431; rat.
DR AGR; RGD:621431; -.
DR CTD; 3977; -.
DR RGD; 621431; Lifr.
DR eggNOG; ENOG502QQF6; Eukaryota.
DR InParanoid; O70535; -.
DR OrthoDB; 5347052at2759; -.
DR PhylomeDB; O70535; -.
DR Reactome; R-RNO-6788467; IL-6-type cytokine receptor ligand interactions.
DR PRO; PR:O70535; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; ISO:RGD.
DR GO; GO:0019955; F:cytokine binding; IMP:RGD.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019838; F:growth factor binding; ISO:RGD.
DR GO; GO:0004923; F:leukemia inhibitory factor receptor activity; IMP:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IMP:RGD.
DR GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0048861; P:leukemia inhibitory factor signaling pathway; ISO:RGD.
DR GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; IDA:RGD.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; ISO:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR048497; LIF-R-like_Ig-like.
DR InterPro; IPR040817; LIFR_D2.
DR InterPro; IPR040901; LIFR_N.
DR PANTHER; PTHR23036; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR23036:SF105; LEUKEMIA INHIBITORY FACTOR RECEPTOR; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF21177; LIF-R_Ig-like; 1.
DR Pfam; PF17971; LIFR_D2; 1.
DR Pfam; PF18207; LIFR_N; 1.
DR SMART; SM00060; FN3; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..1093
FT /note="Leukemia inhibitory factor receptor"
FT /id="PRO_0000228095"
FT TOPO_DOM 44..829
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 830..850
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 851..1093
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..127
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 331..428
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 431..530
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 534..625
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 623..715
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 720..829
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 908..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 515..519
FT /note="WSXWS motif"
FT MOTIF 865..873
FT /note="Box 1 motif"
FT COMPBIAS 925..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42702"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42703"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..64
FT /evidence="ECO:0000250"
FT DISULFID 81..89
FT /evidence="ECO:0000250"
FT DISULFID 209..266
FT /evidence="ECO:0000250"
FT DISULFID 337..347
FT /evidence="ECO:0000250"
FT DISULFID 462..507
FT /evidence="ECO:0000250"
SQ SEQUENCE 1093 AA; 122394 MW; 08D43DEAF8F5E3F6 CRC64;
MGAFSWWRQP SWMADNKRGR MTPSLPWLLS ALTLLHLMMH VNGLKRGVQQ DLKCTTNNMR
VWDCSWPAPL GVSPGTVKDI CIKDRPHSCH RLETTNVKIP ALSPGDHEVT INYQNGFQSK
FTLNEKDVSL VPDTPEILSL SADFSTSTLQ LKWNDKGSAL PYPSNATWEV KVLQNPRTEP
VALVSLNTVL SGKDKGHHWN WTSELPLQCA THSVSIRWHI DYPRFSGYKE WSEWSPLKNI
SWTRNTETNV FPQDKVVLAG SNMTICCIST TKVLSGQIGN TFRPLIHLYG ETVAINILNI
PVSENSGSNV IFSTVDDVYG TVVFAGYPPD VPQKLSCETH DLKEIICSWN PGRITGLVGP
RNTEYTLFES ISGKSAVFHR FEELANETYW LTLKMAPDQE IHNFTLTARN PLGQTESAIV
INATERVALH VPISLKVKDV NSTVVTLSWY LPGNFTKINL VCQIEICKAN SKKEVRNVTM
RGAEDSTYHV AVDKLNPYTI YTFRVRCSSE TFWKWSKWSN EKRYLTTEAT PSKGPDTWRE
WSSDGKNLII YWKPLPINEA NGKILSYNVS CSSSEETQSL SEILDPQHKA EIKVNKNDYI
ISVVARNSAG SSPPSKIASM EIPNDDITVE QAVGIGNRIF LSWQHNPNMT CDYVIKWCNS
SWSEPCLLDW IKVPSNSTGT VIESDQFQPG VRYNFYLYGC TNQGYQLLRS TIGYIEELAP
IVAPNFTVED TSADSILVKW DDIPVEELRG FLRGYLFYFQ KGERDTPKTR SLETSHSDIK
LKNITDISQK TLRIADLQGK TSYHLVLRAY THGGLGPEKS MFVVTKENSV GLIIAILIPV
AVAVIVGVVT SILCYRKREW IKETFYPDIP NPENCKALQF QKSVCEGSNA LKTLEMNPCT
PNHVEVLESR SIPPKIEDTE ITSPVSERPG ESSETDPENQ AAVSYCPPII EEEITNPAAD
EAGGASQVVY IDVQSMYQPQ AKAEDEQDTD PVMVAGYKPQ MRLPINPTAE DTTAEDEADK
TAGYRPQANV NTWNLVSPDS PRSTDSNSEV VSFGSPCSIN SRQFLIPPKD EDSPKSNGGG
WSFTNFFQNK PND
//
