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Protein

Ciliary neurotrophic factor receptor subunit alpha

Gene

CNTFR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. ciliary neurotrophic factor receptor activity Source: ProtInc
  2. cytokine binding Source: HGNC
  3. receptor binding Source: BHF-UCL

GO - Biological processi

  1. brainstem development Source: Ensembl
  2. ciliary neurotrophic factor-mediated signaling pathway Source: BHF-UCL
  3. negative regulation of neuron apoptotic process Source: Ensembl
  4. nervous system development Source: ProtInc
  5. positive regulation of cell proliferation Source: Ensembl
  6. sex differentiation Source: Ensembl
  7. signal transduction Source: ProtInc
  8. skeletal muscle organ development Source: Ensembl
  9. suckling behavior Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

SignaLinkiP26992.

Names & Taxonomyi

Protein namesi
Recommended name:
Ciliary neurotrophic factor receptor subunit alpha
Short name:
CNTF receptor subunit alpha
Short name:
CNTFR-alpha
Gene namesi
Name:CNTFR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:2170. CNTFR.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. ciliary neurotrophic factor receptor complex Source: BHF-UCL
  3. CNTFR-CLCF1 complex Source: BHF-UCL
  4. extrinsic component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26684.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 342320Ciliary neurotrophic factor receptor subunit alphaPRO_0000010991Add
BLAST
Propeptidei343 – 37230Removed in mature formSequence AnalysisPRO_0000010992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 89PROSITE-ProRule annotation
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
Lipidationi342 – 3421GPI-anchor amidated serineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP26992.
PRIDEiP26992.

Expressioni

Tissue specificityi

Nervous system and skeletal muscle.

Gene expression databases

BgeeiP26992.
CleanExiHS_CNTFR.
ExpressionAtlasiP26992. baseline and differential.
GenevestigatoriP26992.

Organism-specific databases

HPAiCAB025310.

Interactioni

Subunit structurei

Heterotrimer of the alpha subunit, LIFR and IL6ST.

Protein-protein interaction databases

BioGridi107671. 8 interactions.
DIPiDIP-5777N.
IntActiP26992. 9 interactions.
STRINGi9606.ENSP00000242338.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi208 – 2147Combined sources
Beta strandi222 – 2276Combined sources
Turni235 – 2395Combined sources
Beta strandi242 – 25110Combined sources
Beta strandi257 – 2615Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi276 – 2816Combined sources
Beta strandi284 – 2874Combined sources
Beta strandi295 – 2995Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UC6NMR-A202-305[»]
ProteinModelPortaliP26992.
SMRiP26992. Positions 27-305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26992.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 10478Ig-like C2-typeAdd
BLAST
Domaini108 – 20598Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini206 – 306101Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi290 – 2945WSXWS motif

Domaini

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

Sequence similaritiesi

Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG42607.
GeneTreeiENSGT00530000063103.
HOGENOMiHOG000171060.
HOVERGENiHBG051048.
InParanoidiP26992.
KOiK05059.
OMAiQETPHVQ.
OrthoDBiEOG72NRQF.
PhylomeDBiP26992.
TreeFamiTF331210.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR003961. FN3_dom.
IPR003530. Hematopoietin_rcpt_L_F3_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
PS01354. HEMATOPO_REC_L_F3. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26992-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPVPWACC AVLAAAAAVV YAQRHSPQEA PHVQYERLGS DVTLPCGTAN
60 70 80 90 100
WDAAVTWRVN GTDLAPDLLN GSQLVLHGLE LGHSGLYACF HRDSWHLRHQ
110 120 130 140 150
VLLHVGLPPR EPVLSCRSNT YPKGFYCSWH LPTPTYIPNT FNVTVLHGSK
160 170 180 190 200
IMVCEKDPAL KNRCHIRYMH LFSTIKYKVS ISVSNALGHN ATAITFDEFT
210 220 230 240 250
IVKPDPPENV VARPVPSNPR RLEVTWQTPS TWPDPESFPL KFFLRYRPLI
260 270 280 290 300
LDQWQHVELS DGTAHTITDA YAGKEYIIQV AAKDNEIGTW SDWSVAAHAT
310 320 330 340 350
PWTEEPRHLT TEAQAAETTT STTSSLAPPP TTKICDPGEL GSGGGPSAPF
360 370
LVSVPITLAL AAAAATASSL LI
Length:372
Mass (Da):40,633
Last modified:February 1, 1996 - v2
Checksum:iB2F3F73DE8F8750E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73238 mRNA. Translation: AAA35707.1.
L38025
, 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.
CCDSiCCDS6558.1.
PIRiA40854. UHHUCN.
RefSeqiNP_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.
UniGeneiHs.129966.

Genome annotation databases

EnsembliENST00000351266; ENSP00000242338; ENSG00000122756.
ENST00000378980; ENSP00000368265; ENSG00000122756.
ENST00000610543; ENSP00000480451; ENSG00000122756.
GeneIDi1271.
KEGGihsa:1271.
UCSCiuc003zup.2. human.

Polymorphism databases

DMDMi1352099.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73238 mRNA. Translation: AAA35707.1.
L38025
, 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.
CCDSiCCDS6558.1.
PIRiA40854. UHHUCN.
RefSeqiNP_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.
UniGeneiHs.129966.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UC6NMR-A202-305[»]
ProteinModelPortaliP26992.
SMRiP26992. Positions 27-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107671. 8 interactions.
DIPiDIP-5777N.
IntActiP26992. 9 interactions.
STRINGi9606.ENSP00000242338.

Polymorphism databases

DMDMi1352099.

Proteomic databases

PaxDbiP26992.
PRIDEiP26992.

Protocols and materials databases

DNASUi1271.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000351266; ENSP00000242338; ENSG00000122756.
ENST00000378980; ENSP00000368265; ENSG00000122756.
ENST00000610543; ENSP00000480451; ENSG00000122756.
GeneIDi1271.
KEGGihsa:1271.
UCSCiuc003zup.2. human.

Organism-specific databases

CTDi1271.
GeneCardsiGC09M034541.
HGNCiHGNC:2170. CNTFR.
HPAiCAB025310.
MIMi118946. gene.
neXtProtiNX_P26992.
PharmGKBiPA26684.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42607.
GeneTreeiENSGT00530000063103.
HOGENOMiHOG000171060.
HOVERGENiHBG051048.
InParanoidiP26992.
KOiK05059.
OMAiQETPHVQ.
OrthoDBiEOG72NRQF.
PhylomeDBiP26992.
TreeFamiTF331210.

Enzyme and pathway databases

SignaLinkiP26992.

Miscellaneous databases

ChiTaRSiCNTFR. human.
EvolutionaryTraceiP26992.
GenomeRNAii1271.
NextBioi5147.
PROiP26992.
SOURCEiSearch...

Gene expression databases

BgeeiP26992.
CleanExiHS_CNTFR.
ExpressionAtlasiP26992. baseline and differential.
GenevestigatoriP26992.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR003961. FN3_dom.
IPR003530. Hematopoietin_rcpt_L_F3_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
PS01354. HEMATOPO_REC_L_F3. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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(1994) [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 (SEP-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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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(2003) [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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 202-305.

Entry informationi

Entry nameiCNTFR_HUMAN
AccessioniPrimary (citable) accession number: P26992
Secondary accession number(s): Q5U050
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1996
Last modified: April 1, 2015
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.