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P09543

- CN37_HUMAN

UniProt

P09543 - CN37_HUMAN

Protein

2',3'-cyclic-nucleotide 3'-phosphodiesterase

Gene

CNP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin.By similarity

    Catalytic activityi

    Nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei251 – 2511Proton acceptor
    Binding sitei253 – 2531Substrate
    Active sitei330 – 3301Proton donor
    Binding sitei332 – 3321Substrate

    GO - Molecular functioni

    1. 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity Source: ProtInc
    2. cyclic nucleotide binding Source: Ensembl
    3. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. adult locomotory behavior Source: Ensembl
    2. aging Source: Ensembl
    3. axonogenesis Source: Ensembl
    4. cyclic nucleotide catabolic process Source: InterPro
    5. microtubule cytoskeleton organization Source: Ensembl
    6. regulation of mitochondrial membrane permeability Source: Ensembl
    7. response to lipopolysaccharide Source: Ensembl
    8. response to toxic substance Source: Ensembl
    9. substantia nigra development Source: UniProt
    10. synaptic transmission Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2',3'-cyclic-nucleotide 3'-phosphodiesterase (EC:3.1.4.37)
    Short name:
    CNP
    Short name:
    CNPase
    Gene namesi
    Name:CNP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:2158. CNP.

    Subcellular locationi

    Membrane; Lipid-anchor. Melanosome
    Note: Firmly bound to membrane structures of brain white matter. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. melanosome Source: UniProtKB-SubCell
    5. membrane Source: UniProtKB
    6. microtubule Source: UniProtKB
    7. microvillus Source: Ensembl
    8. mitochondrial inner membrane Source: Ensembl
    9. mitochondrial outer membrane Source: Ensembl
    10. myelin sheath abaxonal region Source: Ensembl
    11. myelin sheath adaxonal region Source: Ensembl
    12. nucleus Source: HPA
    13. perinuclear region of cytoplasm Source: Ensembl
    14. plasma membrane Source: Ensembl
    15. pseudopodium Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26680.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4184182',3'-cyclic-nucleotide 3'-phosphodiesterasePRO_0000089961Add
    BLAST
    Propeptidei419 – 4213Removed in mature formBy similarityPRO_0000422296

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei110 – 1101PhosphotyrosineBy similarity
    Modified residuei418 – 4181Cysteine methyl esterBy similarity
    Lipidationi418 – 4181S-farnesyl cysteineBy similarity

    Keywords - PTMi

    Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP09543.
    PaxDbiP09543.
    PRIDEiP09543.

    2D gel databases

    UCD-2DPAGEP09543.

    PTM databases

    PhosphoSiteiP09543.

    Expressioni

    Gene expression databases

    ArrayExpressiP09543.
    BgeeiP09543.
    CleanExiHS_CNP.
    GenevestigatoriP09543.

    Organism-specific databases

    HPAiCAB002672.
    HPA023266.
    HPA023278.
    HPA023280.
    HPA023338.

    Interactioni

    Subunit structurei

    Exists as monomers and homodimers.By similarity

    Protein-protein interaction databases

    BioGridi107667. 8 interactions.
    IntActiP09543. 7 interactions.
    MINTiMINT-4999529.
    STRINGi9606.ENSP00000377470.

    Structurei

    Secondary structure

    1
    421
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi188 – 1947
    Helixi196 – 21520
    Helixi217 – 2215
    Helixi223 – 2264
    Helixi238 – 2414
    Beta strandi251 – 2566
    Helixi258 – 2603
    Helixi265 – 2706
    Helixi272 – 2776
    Beta strandi281 – 29111
    Beta strandi293 – 3019
    Helixi306 – 3094
    Turni325 – 3284
    Beta strandi330 – 3356
    Helixi343 – 35614
    Beta strandi362 – 3676
    Beta strandi370 – 3767
    Beta strandi379 – 39719

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WOJX-ray1.80A186-399[»]
    ProteinModelPortaliP09543.
    SMRiP09543. Positions 47-124, 186-399.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09543.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG314041.
    HOGENOMiHOG000111838.
    HOVERGENiHBG001451.
    InParanoidiP09543.
    KOiK01121.
    OMAiLWPNDVD.
    PhylomeDBiP09543.
    TreeFamiTF332157.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR008431. CNPase.
    IPR027417. P-loop_NTPase.
    IPR009097. RNA_ligase/cNuc_Pdiesterase.
    [Graphical view]
    PANTHERiPTHR10156. PTHR10156. 1 hit.
    PfamiPF05881. CNPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000970. CNPase. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF55144. SSF55144. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform CNPII (identifier: P09543-1) [UniParc]FASTAAdd to Basket

    Also known as: DNAII

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNRGFSRKSH TFLPKIFFRK MSSSGAKDKP ELQFPFLQDE DTVATLLECK    50
    TLFILRGLPG SGKSTLARVI VDKYRDGTKM VSADAYKITP GARGAFSEEY 100
    KRLDEDLAAY CRRRDIRILV LDDTNHERER LEQLFEMADQ YQYQVVLVEP 150
    KTAWRLDCAQ LKEKNQWQLS ADDLKKLKPG LEKDFLPLYF GWFLTKKSSE 200
    TLRKAGQVFL EELGNHKAFK KELRQFVPGD EPREKMDLVT YFGKRPPGVL 250
    HCTTKFCDYG KAPGAEEYAQ QDVLKKSYSK AFTLTISALF VTPKTTGARV 300
    ELSEQQLQLW PSDVDKLSPT DNLPRGSRAH ITLGCAADVE AVQTGLDLLE 350
    ILRQEKGGSR GEEVGELSRG KLYSLGNGRW MLTLAKNMEV RAIFTGYYGK 400
    GKPVPTQGSR KGGALQSCTI I 421
    Length:421
    Mass (Da):47,579
    Last modified:October 1, 1996 - v2
    Checksum:iCA6D0097DFD87255
    GO
    Isoform CNPI (identifier: P09543-2) [UniParc]FASTAAdd to Basket

    Also known as: DNAI

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: Missing.

    Show »
    Length:401
    Mass (Da):45,099
    Checksum:i81F0E080822D3B0D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti207 – 2071Q → R.
    Corresponds to variant rs34353668 [ dbSNP | Ensembl ].
    VAR_033746

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2020Missing in isoform CNPI. 2 PublicationsVSP_004171Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S46849
    , S46843, S46845, S46846 Genomic DNA. Translation: AAB23928.2.
    M19650 mRNA. Translation: AAA35704.1.
    D13146 Genomic DNA. Translation: BAA39694.1.
    D13146 Genomic DNA. Translation: BAA02435.1.
    S50017
    , S50013, S50014, S50016 Genomic DNA. Translation: AAB24298.2.
    AC125257 Genomic DNA. No translation available.
    BC001362 mRNA. Translation: AAH01362.1.
    BC006392 mRNA. Translation: AAH06392.1.
    BC011046 mRNA. Translation: AAH11046.1.
    BC028040 mRNA. Translation: AAH28040.1.
    CCDSiCCDS11414.2. [P09543-1]
    PIRiJC1517.
    RefSeqiNP_149124.3. NM_033133.4. [P09543-1]
    XP_006721764.1. XM_006721701.1. [P09543-2]
    XP_006721765.1. XM_006721702.1. [P09543-2]
    UniGeneiHs.273621.

    Genome annotation databases

    EnsembliENST00000393888; ENSP00000377466; ENSG00000173786. [P09543-2]
    ENST00000393892; ENSP00000377470; ENSG00000173786. [P09543-1]
    GeneIDi1267.
    KEGGihsa:1267.
    UCSCiuc002hyl.1. human. [P09543-1]

    Polymorphism databases

    DMDMi1705945.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S46849
    , S46843 , S46845 , S46846 Genomic DNA. Translation: AAB23928.2 .
    M19650 mRNA. Translation: AAA35704.1 .
    D13146 Genomic DNA. Translation: BAA39694.1 .
    D13146 Genomic DNA. Translation: BAA02435.1 .
    S50017
    , S50013 , S50014 , S50016 Genomic DNA. Translation: AAB24298.2 .
    AC125257 Genomic DNA. No translation available.
    BC001362 mRNA. Translation: AAH01362.1 .
    BC006392 mRNA. Translation: AAH06392.1 .
    BC011046 mRNA. Translation: AAH11046.1 .
    BC028040 mRNA. Translation: AAH28040.1 .
    CCDSi CCDS11414.2. [P09543-1 ]
    PIRi JC1517.
    RefSeqi NP_149124.3. NM_033133.4. [P09543-1 ]
    XP_006721764.1. XM_006721701.1. [P09543-2 ]
    XP_006721765.1. XM_006721702.1. [P09543-2 ]
    UniGenei Hs.273621.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WOJ X-ray 1.80 A 186-399 [» ]
    ProteinModelPortali P09543.
    SMRi P09543. Positions 47-124, 186-399.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107667. 8 interactions.
    IntActi P09543. 7 interactions.
    MINTi MINT-4999529.
    STRINGi 9606.ENSP00000377470.

    PTM databases

    PhosphoSitei P09543.

    Polymorphism databases

    DMDMi 1705945.

    2D gel databases

    UCD-2DPAGE P09543.

    Proteomic databases

    MaxQBi P09543.
    PaxDbi P09543.
    PRIDEi P09543.

    Protocols and materials databases

    DNASUi 1267.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000393888 ; ENSP00000377466 ; ENSG00000173786 . [P09543-2 ]
    ENST00000393892 ; ENSP00000377470 ; ENSG00000173786 . [P09543-1 ]
    GeneIDi 1267.
    KEGGi hsa:1267.
    UCSCi uc002hyl.1. human. [P09543-1 ]

    Organism-specific databases

    CTDi 1267.
    GeneCardsi GC17P040118.
    HGNCi HGNC:2158. CNP.
    HPAi CAB002672.
    HPA023266.
    HPA023278.
    HPA023280.
    HPA023338.
    MIMi 123830. gene.
    neXtProti NX_P09543.
    PharmGKBi PA26680.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314041.
    HOGENOMi HOG000111838.
    HOVERGENi HBG001451.
    InParanoidi P09543.
    KOi K01121.
    OMAi LWPNDVD.
    PhylomeDBi P09543.
    TreeFami TF332157.

    Miscellaneous databases

    ChiTaRSi CNP. human.
    EvolutionaryTracei P09543.
    GeneWikii 2%27,3%27-Cyclic-nucleotide_3%27-phosphodiesterase.
    GenomeRNAii 1267.
    NextBioi 5129.
    PROi P09543.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09543.
    Bgeei P09543.
    CleanExi HS_CNP.
    Genevestigatori P09543.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR008431. CNPase.
    IPR027417. P-loop_NTPase.
    IPR009097. RNA_ligase/cNuc_Pdiesterase.
    [Graphical view ]
    PANTHERi PTHR10156. PTHR10156. 1 hit.
    Pfami PF05881. CNPase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000970. CNPase. 1 hit.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    SSF55144. SSF55144. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "2',3'-cyclic nucleotide-3'-phosphohydrolase and signal transduction in central nervous system myelin."
      Thompson R.J.
      Biochem. Soc. Trans. 20:621-626(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "cDNA cloning and amino acid sequence of human brain 2',3'-cyclic-nucleotide 3'-phosphodiesterase."
      Kurihara T., Takahashi Y., Nishiyama A., Kumanishi T.
      Biochem. Biophys. Res. Commun. 152:837-842(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CNPI).
      Tissue: Brain.
    3. "Structure, expression and chromosomal localization of the gene encoding human 2',3'-cyclic-nucleotide 3'-phosphodiesterase."
      Monoh K., Kurihara T., Takahashi Y., Ichikawa T., Kumanishi T., Hayashi S., Minoshima S., Shimizu N.
      Gene 129:297-301(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Structure and chromosomal localization of the human 2',3'-cyclic nucleotide 3'-phosphodiesterase gene."
      Douglas A.J., Fox M.F., Abbott C.M., Hinks L.J., Sharpe G., Povey S., Thompson R.J.
      Ann. Hum. Genet. 56:243-254(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORMS CNPI AND CNPII).
      Tissue: Brain and Skin.
    7. "The epitope recognized by a monoclonal antibody in the myelin-associated protein CNP."
      Stricker R., Kalbacher H., Reiser G.
      Biochem. Biophys. Res. Commun. 237:266-270(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-58.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Crystal structure of the catalytic fragment of human brain 2',3'-cyclic-nucleotide 3'-phosphodiesterase."
      Sakamoto Y., Tanaka N., Ichimiya T., Kurihara T., Nakamura K.T.
      J. Mol. Biol. 346:789-800(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 186-399 IN COMPLEX WITH PHOSPHATE.

    Entry informationi

    Entry nameiCN37_HUMAN
    AccessioniPrimary (citable) accession number: P09543
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 155 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3