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P26992 (CNTFR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ciliary neurotrophic factor receptor subunit alpha

Short name=CNTF receptor subunit alpha
Short name=CNTFR-alpha
Gene names
Name:CNTFR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to CNTF. The alpha subunit provides the receptor specificity.

Subunit structure

Heterotrimer of the alpha subunit, LIFR and IL6ST.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Tissue specificity

Nervous system and skeletal muscle.

Domain

The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.

Sequence similarities

Belongs to the type I cytokine receptor family. Type 3 subfamily.

Contains 2 fibronectin type-III domains.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainImmunoglobulin domain
Repeat
Signal
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrainstem development

Inferred from electronic annotation. Source: Ensembl

ciliary neurotrophic factor-mediated signaling pathway

Inferred from direct assay PubMed 12643274. Source: BHF-UCL

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

nervous system development

Traceable author statement PubMed 7585948. Source: ProtInc

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

sex differentiation

Inferred from electronic annotation. Source: Ensembl

signal transduction

Non-traceable author statement Ref.1. Source: ProtInc

skeletal muscle organ development

Inferred from electronic annotation. Source: Ensembl

suckling behavior

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentCNTFR-CLCF1 complex

Inferred from direct assay PubMed 11285233. Source: BHF-UCL

anchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

extrinsic component of membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionciliary neurotrophic factor receptor activity

Traceable author statement PubMed 7585948. Source: ProtInc

cytokine binding

Inferred from physical interaction PubMed 15272019. Source: HGNC

receptor binding

Inferred from physical interaction Ref.7. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 342320Ciliary neurotrophic factor receptor subunit alpha
PRO_0000010991
Propeptide343 – 37230Removed in mature form Potential
PRO_0000010992

Regions

Domain27 – 10478Ig-like C2-type
Domain108 – 20598Fibronectin type-III 1
Domain206 – 306101Fibronectin type-III 2
Motif290 – 2945WSXWS motif

Amino acid modifications

Lipidation3421GPI-anchor amidated serine Potential
Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Disulfide bond46 ↔ 89 Potential

Secondary structure

..................... 372
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26992 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: B2F3F73DE8F8750E

FASTA37240,633
        10         20         30         40         50         60 
MAAPVPWACC AVLAAAAAVV YAQRHSPQEA PHVQYERLGS DVTLPCGTAN WDAAVTWRVN 

        70         80         90        100        110        120 
GTDLAPDLLN GSQLVLHGLE LGHSGLYACF HRDSWHLRHQ VLLHVGLPPR EPVLSCRSNT 

       130        140        150        160        170        180 
YPKGFYCSWH LPTPTYIPNT FNVTVLHGSK IMVCEKDPAL KNRCHIRYMH LFSTIKYKVS 

       190        200        210        220        230        240 
ISVSNALGHN ATAITFDEFT IVKPDPPENV VARPVPSNPR RLEVTWQTPS TWPDPESFPL 

       250        260        270        280        290        300 
KFFLRYRPLI LDQWQHVELS DGTAHTITDA YAGKEYIIQV AAKDNEIGTW SDWSVAAHAT 

       310        320        330        340        350        360 
PWTEEPRHLT TEAQAAETTT STTSSLAPPP TTKICDPGEL GSGGGPSAPF LVSVPITLAL 

       370 
AAAAATASSL LI 

« Hide

References

« Hide 'large scale' references
[1]"The receptor for ciliary neurotrophic factor."
Davis S., Aldrich T.H., Valenzuela D.M., Wong V., Furth M.E., Squinto S.P., Yancopoulos G.D.
Science 253:59-63(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genomic organization and chromosomal localization of the human and mouse genes encoding the alpha receptor component for ciliary neurotrophic factor."
Valenzuela D.M., Rojas E., le Beau M.M., Espinosa R., Brannan C.I., McClain J., Masiakowski P., Ip N.Y., Copeland N.G., Jenkins N.A., Yancopoulos G.D.
Genomics 25:157-163(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"Solution structure of the C-terminal domain of the ciliary neurotrophic factor (CNTF) receptor and ligand free associations among components of the CNTF receptor complex."
Man D., He W., Sze K.H., Gong K., Smith D.K., Zhu G., Ip N.Y.
J. Biol. Chem. 278:23285-23294(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 202-305.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73238 mRNA. Translation: AAA35707.1.
L38025 expand/collapse EMBL AC list , L38022, L38023, L38024 Genomic DNA. Translation: AAA91337.1.
BT019824 mRNA. Translation: AAV38627.1.
AL160270 Genomic DNA. Translation: CAI13159.1.
CH471071 Genomic DNA. Translation: EAW58445.1.
CH471071 Genomic DNA. Translation: EAW58446.1.
CH471071 Genomic DNA. Translation: EAW58447.1.
CH471071 Genomic DNA. Translation: EAW58448.1.
BC001492 mRNA. Translation: AAH01492.1.
PIRUHHUCN. A40854.
RefSeqNP_001193940.1. NM_001207011.1.
NP_001833.1. NM_001842.4.
NP_671693.1. NM_147164.2.
XP_005251419.1. XM_005251362.2.
XP_005251420.1. XM_005251363.2.
UniGeneHs.129966.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UC6NMR-A202-305[»]
ProteinModelPortalP26992.
SMRP26992. Positions 24-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107671. 8 interactions.
DIPDIP-5777N.
IntActP26992. 9 interactions.
STRING9606.ENSP00000242338.

Polymorphism databases

DMDM1352099.

Proteomic databases

PaxDbP26992.
PRIDEP26992.

Protocols and materials databases

DNASU1271.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351266; ENSP00000242338; ENSG00000122756.
ENST00000378980; ENSP00000368265; ENSG00000122756.
GeneID1271.
KEGGhsa:1271.
UCSCuc003zup.2. human.

Organism-specific databases

CTD1271.
GeneCardsGC09M034541.
HGNCHGNC:2170. CNTFR.
HPACAB025310.
MIM118946. gene.
neXtProtNX_P26992.
PharmGKBPA26684.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42607.
HOGENOMHOG000171060.
HOVERGENHBG051048.
InParanoidP26992.
KOK05059.
OMASPQETPH.
OrthoDBEOG72NRQF.
PhylomeDBP26992.
TreeFamTF331210.

Enzyme and pathway databases

SignaLinkP26992.

Gene expression databases

ArrayExpressP26992.
BgeeP26992.
CleanExHS_CNTFR.
GenevestigatorP26992.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR003961. Fibronectin_type3.
IPR003530. Hematopoietin_rcpt_L_F3_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
[Graphical view]
PfamPF00041. fn3. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 2 hits.
PS01354. HEMATOPO_REC_L_F3. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26992.
GenomeRNAi1271.
NextBio5147.
PROP26992.
SOURCESearch...

Entry information

Entry nameCNTFR_HUMAN
AccessionPrimary (citable) accession number: P26992
Secondary accession number(s): Q5U050
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM