位置:首页 > 蛋白库 > LIFR_RAT
LIFR_RAT
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   03-AUG-2022, entry version 133.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyGen; O70535; 16 sites.
DR   PhosphoSitePlus; O70535; -.
DR   PaxDb; O70535; -.
DR   PRIDE; O70535; -.
DR   GeneID; 81680; -.
DR   KEGG; rno:81680; -.
DR   UCSC; RGD:621431; rat.
DR   CTD; 3977; -.
DR   RGD; 621431; Lifr.
DR   eggNOG; ENOG502QQF6; Eukaryota.
DR   InParanoid; O70535; -.
DR   OrthoDB; 331447at2759; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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   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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024