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P26992

- CNTFR_HUMAN

UniProt

P26992 - CNTFR_HUMAN

Protein

Ciliary neurotrophic factor receptor subunit alpha

Gene

CNTFR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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

    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: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:2170. CNTFR.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. CNTFR-CLCF1 complex Source: BHF-UCL
    3. extrinsic component of membrane Source: ProtInc
    4. plasma membrane Source: UniProtKB-SubCell

    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

    ArrayExpressiP26992.
    BgeeiP26992.
    CleanExiHS_CNTFR.
    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 – 2147
    Beta strandi222 – 2276
    Turni235 – 2395
    Beta strandi242 – 25110
    Beta strandi257 – 2615
    Beta strandi263 – 2675
    Beta strandi272 – 2743
    Beta strandi276 – 2816
    Beta strandi284 – 2874
    Beta strandi295 – 2995

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UC6NMR-A202-305[»]
    ProteinModelPortaliP26992.
    SMRiP26992. Positions 39-305.
    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.
    HOGENOMiHOG000171060.
    HOVERGENiHBG051048.
    InParanoidiP26992.
    KOiK05059.
    OMAiSPQETPH.
    OrthoDBiEOG72NRQF.
    PhylomeDBiP26992.
    TreeFamiTF331210.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR003961. Fibronectin_type3.
    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

    MAAPVPWACC AVLAAAAAVV YAQRHSPQEA PHVQYERLGS DVTLPCGTAN    50
    WDAAVTWRVN GTDLAPDLLN GSQLVLHGLE LGHSGLYACF HRDSWHLRHQ 100
    VLLHVGLPPR EPVLSCRSNT YPKGFYCSWH LPTPTYIPNT FNVTVLHGSK 150
    IMVCEKDPAL KNRCHIRYMH LFSTIKYKVS ISVSNALGHN ATAITFDEFT 200
    IVKPDPPENV VARPVPSNPR RLEVTWQTPS TWPDPESFPL KFFLRYRPLI 250
    LDQWQHVELS DGTAHTITDA YAGKEYIIQV AAKDNEIGTW SDWSVAAHAT 300
    PWTEEPRHLT TEAQAAETTT STTSSLAPPP TTKICDPGEL GSGGGPSAPF 350
    LVSVPITLAL AAAAATASSL LI 372
    Length:372
    Mass (Da):40,633
    Last modified:February 1, 1996 - v2
    Checksum:iB2F3F73DE8F8750E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    GeneIDi1271.
    KEGGihsa:1271.
    UCSCiuc003zup.2. human.

    Polymorphism databases

    DMDMi1352099.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6558.1.
    PIRi A40854. UHHUCN.
    RefSeqi NP_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.
    UniGenei Hs.129966.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UC6 NMR - A 202-305 [» ]
    ProteinModelPortali P26992.
    SMRi P26992. Positions 39-305.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107671. 8 interactions.
    DIPi DIP-5777N.
    IntActi P26992. 9 interactions.
    STRINGi 9606.ENSP00000242338.

    Polymorphism databases

    DMDMi 1352099.

    Proteomic databases

    PaxDbi P26992.
    PRIDEi P26992.

    Protocols and materials databases

    DNASUi 1271.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351266 ; ENSP00000242338 ; ENSG00000122756 .
    ENST00000378980 ; ENSP00000368265 ; ENSG00000122756 .
    GeneIDi 1271.
    KEGGi hsa:1271.
    UCSCi uc003zup.2. human.

    Organism-specific databases

    CTDi 1271.
    GeneCardsi GC09M034541.
    HGNCi HGNC:2170. CNTFR.
    HPAi CAB025310.
    MIMi 118946. gene.
    neXtProti NX_P26992.
    PharmGKBi PA26684.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42607.
    HOGENOMi HOG000171060.
    HOVERGENi HBG051048.
    InParanoidi P26992.
    KOi K05059.
    OMAi SPQETPH.
    OrthoDBi EOG72NRQF.
    PhylomeDBi P26992.
    TreeFami TF331210.

    Enzyme and pathway databases

    SignaLinki P26992.

    Miscellaneous databases

    EvolutionaryTracei P26992.
    GenomeRNAii 1271.
    NextBioi 5147.
    PROi P26992.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26992.
    Bgeei P26992.
    CleanExi HS_CNTFR.
    Genevestigatori P26992.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR003530. Hematopoietin_rcpt_L_F3_CS.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003598. Ig_sub2.
    [Graphical view ]
    Pfami PF00041. fn3. 1 hit.
    [Graphical view ]
    SMARTi SM00060. FN3. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    PROSITEi PS50853. FN3. 2 hits.
    PS01354. HEMATOPO_REC_L_F3. 1 hit.
    PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(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.
      , 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. 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.

    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: October 1, 2014
    This is version 142 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