LIFR_CANLF
ID LIFR_CANLF Reviewed; 1097 AA.
AC Q5XNR9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hanson J.M., Mol J.A., Meij B.P.;
RT "Expression of LIFR in the normal canine pituitary and in corticotroph
RT adenomas.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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; AY745241; AAU43788.1; -; mRNA.
DR RefSeq; NP_001005760.1; NM_001005760.1.
DR AlphaFoldDB; Q5XNR9; -.
DR SMR; Q5XNR9; -.
DR STRING; 9612.ENSCAFP00000027533; -.
DR PaxDb; Q5XNR9; -.
DR PRIDE; Q5XNR9; -.
DR Ensembl; ENSCAFT00000029624; ENSCAFP00000027533; ENSCAFG00000018661.
DR GeneID; 449478; -.
DR KEGG; cfa:449478; -.
DR CTD; 3977; -.
DR VGNC; VGNC:42672; LIFR.
DR eggNOG; ENOG502QQF6; Eukaryota.
DR HOGENOM; CLU_283805_0_0_1; -.
DR InParanoid; Q5XNR9; -.
DR OMA; HYVKIRC; -.
DR OrthoDB; 331447at2759; -.
DR TreeFam; TF338122; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; IBA:GO_Central.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0004923; F:leukemia inhibitory factor receptor activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IEA:GOC.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
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; 4.
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..44
FT /evidence="ECO:0000255"
FT CHAIN 45..1097
FT /note="Leukemia inhibitory factor receptor"
FT /id="PRO_0000228094"
FT TOPO_DOM 45..833
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 834..854
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 855..1097
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..131
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 332..434
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 435..534
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 538..629
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 627..719
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 724..833
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 982..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 519..523
FT /note="WSXWS motif"
FT MOTIF 869..877
FT /note="Box 1 motif"
FT COMPBIAS 1031..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42702"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42703"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..65
FT /evidence="ECO:0000250"
FT DISULFID 82..90
FT /evidence="ECO:0000250"
FT DISULFID 213..270
FT /evidence="ECO:0000250"
FT DISULFID 341..351
FT /evidence="ECO:0000250"
FT DISULFID 466..511
FT /evidence="ECO:0000250"
SQ SEQUENCE 1097 AA; 123688 MW; 2B48F1F6C0AE731D CRC64;
MMNISLRLRR PPWMVDSNGR RMTSHFQWLL LTFILLYLMN QVTSEKRGAP RDLKCITNNL
RVWDCSWKAP SAAGHGTVYE ICIENRSHSC YQSEKTNTKI PALLPGDHEI TINRLYDFGN
PISKFTLNEK NVSLIPDTPE ILNLSADFST STIHLKWNDR GSVFPHQLTV IWEIKILRKE
NMEIVKLITH NTTVNGKDTV HHWSWTSDMP LECAIHSVGI RCYVDDPHFS GRKEWSDWSP
LKNISWSPDS QTKVFPQDKV ILVGSDITFC CVTQEKVLSA QIGQTNCPLI HLDGENVAIK
IHNISVSANS GTNVVFTTED NIFGTVIFVG YPPDIPQKVN CETYDLKEIV CTWNPGRPTA
LVGPRNTSYT LFESFSGKYV RFKRVEAPTN ESYQLFFQMR PNQEIYNFTL NARNPLGRSE
STILINITEK VYPRIPTSIK VKDINSTAVM LSWHLPGNFA KIKLLCQIEI NKTNSVQELR
NVTIKGVENS SYLVAVDKLN PYTIYTFRIR CSTETFWKWS KWSNEKKYLT TEAIPSKGPD
TWREWSSDGK NLIIYWKPLP INEANGKILS YNVSCSLDEE TQSLSEIPDP QHKAELQLDK
NDYIISVVAK NSVGSSPPSK IASMEIPNDD LKVEQAVGMG NGILLTWNYD PNMTCDYVIK
WCNSSRSEPC LMDWKKVPSN STEAVIESDQ FRPGVRYSFF LYGCRNEGYQ LLRSIIGYIE
ELAPIVAPNF TVEDTSADSI LVKWEDIPVE ELRGFLRGYL FYFEKGERDT SKIRGLESGR
SDIKVKNITD LSQKTLRIAD LQGKTSYHLV LRAYTDGGMG PEKSMFVVTK ENSVGLIIAI
LIPVAVAVIV GVVTSILCYR KREWIKETFY PDIPNPENCK ALQFQKSVCE GNSALKTLEM
NPCTPNNVEV LETRSAVPKI EDTEIISPIA ERPEESSDAE AENHVVVSYC PPVIEEETPN
PGADEAGGAS QVVYIDIQSM YQPQAKPEEE QENDPVGGAG YKPQMHLPVT STVEDLAAED
DLDKAAGYRP QANVNTWNLV SPDSPRSTDS NSEIVSFGSP CSINSRQFLI PPKDEDSPKS
SGGGWSFTNF FQNKPND
