CNTFR_RAT
ID CNTFR_RAT Reviewed; 372 AA.
AC Q08406;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ciliary neurotrophic factor receptor subunit alpha;
DE Short=CNTF receptor subunit alpha;
DE Short=CNTFR-alpha;
DE Flags: Precursor;
GN Name=Cntfr;
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 TISSUE=Brain;
RX PubMed=8381290; DOI=10.1016/0896-6273(93)90245-m;
RA Ip N.Y., McClain J., Barrezueta N.X., Aldrich T.H., Pan L., Li Y.,
RA Wiegand S.J., Friedman B., Davis S., Yancopoulos G.D.;
RT "The alpha component of the CNTF receptor is required for signaling and
RT defines potential CNTF targets in the adult and during development.";
RL Neuron 10:89-102(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 185-277.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8460125; DOI=10.1073/pnas.90.6.2222;
RA Clatterbuck R.E., Price D.L., Koliatsos V.E.;
RT "Ciliary neurotrophic factor prevents retrograde neuronal death in the
RT adult central nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2222-2226(1993).
CC -!- FUNCTION: Binds to CNTF. The alpha subunit provides the receptor
CC specificity.
CC -!- SUBUNIT: Forms a heterotrimer with LIFR and IL6ST. Interacts with
CC heterodimeric neurotropic cytokine composed of CLCF1/CLC and CRLF1/CLF-
CC 1. Either alone or in complex with the heterodimer CLCF1-CRLF1
CC interacts with SORL1; this interaction may promote internalization and
CC lysosomal degradation. {ECO:0000250|UniProtKB:P26992}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Nervous system.
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 -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
CC subfamily. {ECO:0000305}.
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DR EMBL; S54212; AAB25290.1; -; mRNA.
DR EMBL; S57711; AAB25918.1; -; mRNA.
DR PIR; I58141; I58141.
DR RefSeq; NP_001003929.1; NM_001003929.1.
DR AlphaFoldDB; Q08406; -.
DR BMRB; Q08406; -.
DR SMR; Q08406; -.
DR BioGRID; 260344; 2.
DR IntAct; Q08406; 2.
DR STRING; 10116.ENSRNOP00000066185; -.
DR GlyGen; Q08406; 5 sites.
DR SwissPalm; Q08406; -.
DR PaxDb; Q08406; -.
DR PRIDE; Q08406; -.
DR GeneID; 313173; -.
DR KEGG; rno:313173; -.
DR CTD; 1271; -.
DR RGD; 1303100; Cntfr.
DR eggNOG; ENOG502QUDK; Eukaryota.
DR InParanoid; Q08406; -.
DR PhylomeDB; Q08406; -.
DR Reactome; R-RNO-6788467; IL-6-type cytokine receptor ligand interactions.
DR PRO; PR:Q08406; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; ISO:RGD.
DR GO; GO:0097059; C:CNTFR-CLCF1 complex; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0004897; F:ciliary neurotrophic factor receptor activity; IMP:RGD.
DR GO; GO:0019955; F:cytokine binding; IPI:RGD.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0003360; P:brainstem development; ISO:RGD.
DR GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0007548; P:sex differentiation; ISO:RGD.
DR GO; GO:0060538; P:skeletal muscle organ development; ISO:RGD.
DR GO; GO:0001967; P:suckling behavior; ISO:RGD.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003530; Hematopoietin_rcpt_L_F3_CS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS01354; HEMATOPO_REC_L_F3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Receptor; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..342
FT /note="Ciliary neurotrophic factor receptor subunit alpha"
FT /id="PRO_0000010995"
FT PROPEP 343..372
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010996"
FT DOMAIN 27..104
FT /note="Ig-like C2-type"
FT DOMAIN 108..205
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 206..306
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 301..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 290..294
FT /note="WSXWS motif"
FT COMPBIAS 312..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 342
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 261
FT /note="N -> D (in Ref. 2; AAB25918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 40822 MW; 3B87EE63923FB149 CRC64;
MAASVPWACC AVLAAAAAAV YTQKHSPQEA PHVQYERLGT DVTLPCGTAS WDAAVTWRVN
GTDLAPDLLN GSQLILRSLE LGHSGLYACF HRDSWHLRHQ VLLHVGLPPR EPVLSCRSNT
YPKGFYCSWH LSAPTYIPNT FNVTVLHGSK MMVCEKDPAL KNRCHIRYMH LFSTIKYKVS
ISVSNALGHN TTAITFDEFT IVKPDPPENV VARPVPSNPR RLEVTWQTPS TWPDPESFPL
KFFLRYRPLI LDQWQHVELS NGTAHTITDA YAGKEYIIQV AAKDNEIGTW SDWSVAAHAT
PWTEEPRHLT TEAQAPETTT STTSSLAPPP TTKICDPGEL SSGGGPSIPF LTSVPVTLVL
AAAAATANNL LI
