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P16330

- CN37_MOUSE

UniProt

P16330 - CN37_MOUSE

Protein

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

Gene

Cnp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (16 Aug 2004)
      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.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei250 – 2501Proton acceptor1 Publication
    Binding sitei252 – 2521Substrate
    Active sitei329 – 3291Proton donor1 Publication
    Binding sitei331 – 3311Substrate

    GO - Molecular functioni

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

    GO - Biological processi

    1. adult locomotory behavior Source: MGI
    2. aging Source: Ensembl
    3. axonogenesis Source: MGI
    4. cyclic nucleotide catabolic process Source: InterPro
    5. forebrain development Source: Ensembl
    6. microtubule cytoskeleton organization Source: Ensembl
    7. oligodendrocyte differentiation Source: MGI
    8. regulation of mitochondrial membrane permeability Source: Ensembl
    9. response to lipopolysaccharide Source: Ensembl
    10. response to toxic substance Source: MGI

    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
    Synonyms:Cnp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:88437. Cnp.

    Subcellular locationi

    Membrane 1 Publication; Lipid-anchor 1 Publication. Melanosome By similarity
    Note: Firmly bound to membrane structures of brain white matter.

    GO - Cellular componenti

    1. extracellular space Source: Ensembl
    2. melanosome Source: UniProtKB-SubCell
    3. membrane Source: MGI
    4. microtubule Source: Ensembl
    5. microvillus Source: Ensembl
    6. mitochondrial inner membrane Source: Ensembl
    7. mitochondrial outer membrane Source: Ensembl
    8. myelin sheath abaxonal region Source: Ensembl
    9. myelin sheath adaxonal region Source: Ensembl
    10. perinuclear region of cytoplasm Source: Ensembl
    11. plasma membrane Source: Ensembl
    12. pseudopodium Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4174172',3'-cyclic-nucleotide 3'-phosphodiesterasePRO_0000089962Add
    BLAST
    Propeptidei418 – 4203Removed in mature formCuratedPRO_0000422297

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei110 – 1101Phosphotyrosine1 Publication
    Modified residuei417 – 4171Cysteine methyl esterCurated
    Lipidationi417 – 4171S-farnesyl cysteine1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP16330.
    PaxDbiP16330.
    PRIDEiP16330.

    PTM databases

    PhosphoSiteiP16330.

    Expressioni

    Gene expression databases

    ArrayExpressiP16330.
    BgeeiP16330.
    CleanExiMM_CNP.
    GenevestigatoriP16330.

    Interactioni

    Subunit structurei

    Exists as monomers and homodimers.1 Publication

    Protein-protein interaction databases

    BioGridi198792. 4 interactions.
    IntActiP16330. 11 interactions.
    MINTiMINT-1955077.

    Structurei

    Secondary structure

    1
    420
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi187 – 1937
    Helixi195 – 21420
    Helixi216 – 2205
    Helixi222 – 2254
    Helixi237 – 2404
    Beta strandi246 – 2483
    Beta strandi250 – 2556
    Helixi257 – 2593
    Helixi264 – 2685
    Helixi271 – 2766
    Beta strandi280 – 29011
    Beta strandi292 – 3009
    Helixi303 – 3064
    Helixi317 – 3193
    Beta strandi320 – 3223
    Turni324 – 3274
    Beta strandi329 – 3346
    Helixi342 – 35514
    Turni357 – 3593
    Beta strandi364 – 3663
    Beta strandi369 – 3757
    Beta strandi378 – 39619

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XMIX-ray1.74A179-398[»]
    2Y1PX-ray1.82A179-398[»]
    2Y3XX-ray2.10A/B/E179-398[»]
    2YDBX-ray2.15A179-398[»]
    2YDCX-ray2.05A179-398[»]
    2YDDX-ray2.40A179-398[»]
    2YOZX-ray2.10A179-398[»]
    2YP0X-ray2.30A179-398[»]
    2YPCX-ray1.89A179-398[»]
    2YPEX-ray1.90A179-398[»]
    2YPHX-ray2.10A179-398[»]
    2YQ9X-ray1.90A179-398[»]
    3ZBRX-ray2.30A/B179-398[»]
    3ZBSX-ray2.45A179-398[»]
    3ZBZX-ray2.10A179-398[»]
    ProteinModelPortaliP16330.
    SMRiP16330. Positions 53-123, 181-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG314041.
    HOGENOMiHOG000111838.
    HOVERGENiHBG001451.
    InParanoidiP16330.
    KOiK01121.
    OMAiLWPNDVD.
    OrthoDBiEOG78PVBC.
    PhylomeDBiP16330.
    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: P16330-1) [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

    MNTSFTRKSH TFLPKLFFRK MSSSGAKEKP ELQFPFLQDE DTVATLHECK    50
    TLFILRGLPG SGKSTLARLI LEKYHDGTKM VSADAYKIIP GSRADFSEAY 100
    KRLDEDLAGY CRRDIRVLVL DDTNHERERL DQLFEMADQY QYQVVLVEPK 150
    TAWRLDCAQL KEKNQWQLSA DDLKKLKPGL EKDFLPLYFG WFLTKKSSET 200
    LRKAGQVFLE ELGNHKAFKK ELRHFISGDE PKEKLELVSY FGKRPPGVLH 250
    CTTKFCDYGK AAGAEEYAQQ EVVKRSYGKA FKLSISALFV TPKTAGAQVV 300
    LTDQELQLWP SDLDKPSASE GLPPGSRAHV TLGCAADVQP VQTGLDLLDI 350
    LQQVKGGSQG EAVGELPRGK LYSLGKGRWM LSLTKKMEVK AIFTGYYGKG 400
    KPVPIHGSRK GGAMQICTII 420
    Length:420
    Mass (Da):47,123
    Last modified:August 16, 2004 - v3
    Checksum:i2FAFFDE5F0E99EAB
    GO
    Isoform CNPI (identifier: P16330-2) [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:400
    Mass (Da):44,654
    Checksum:iB974404499DE29BE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1151I → M in BAA07621. (PubMed:2558653)Curated
    Sequence conflicti115 – 1151I → M in BAA07622. (PubMed:2558653)Curated
    Sequence conflicti136 – 1361M → L in BAA07621. (PubMed:2558653)Curated
    Sequence conflicti136 – 1361M → L in BAA07622. (PubMed:2558653)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2020Missing in isoform CNPI. 2 PublicationsVSP_004172Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38642 Genomic DNA. Translation: BAA07621.1.
    D38642 Genomic DNA. Translation: BAA07622.1.
    M31810 mRNA. Translation: AAA37429.1.
    M58045 mRNA. Translation: AAA37430.1.
    M58047, M58046 Genomic DNA. Translation: AAA37431.1.
    AF332055 mRNA. Translation: AAK56084.1.
    AF332056 mRNA. Translation: AAK56085.1.
    BC005544 mRNA. Translation: AAH05544.1.
    BC021904 mRNA. Translation: AAH21904.1.
    AK050628 mRNA. Translation: BAC34351.1.
    CCDSiCCDS25427.1. [P16330-1]
    PIRiA35708. ESMS32.
    RefSeqiNP_001139790.1. NM_001146318.1. [P16330-2]
    NP_034053.2. NM_009923.2. [P16330-1]
    UniGeneiMm.15711.

    Genome annotation databases

    EnsembliENSMUST00000103120; ENSMUSP00000099409; ENSMUSG00000006782. [P16330-1]
    GeneIDi12799.
    KEGGimmu:12799.
    UCSCiuc007llo.2. mouse. [P16330-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38642 Genomic DNA. Translation: BAA07621.1 .
    D38642 Genomic DNA. Translation: BAA07622.1 .
    M31810 mRNA. Translation: AAA37429.1 .
    M58045 mRNA. Translation: AAA37430.1 .
    M58047 , M58046 Genomic DNA. Translation: AAA37431.1 .
    AF332055 mRNA. Translation: AAK56084.1 .
    AF332056 mRNA. Translation: AAK56085.1 .
    BC005544 mRNA. Translation: AAH05544.1 .
    BC021904 mRNA. Translation: AAH21904.1 .
    AK050628 mRNA. Translation: BAC34351.1 .
    CCDSi CCDS25427.1. [P16330-1 ]
    PIRi A35708. ESMS32.
    RefSeqi NP_001139790.1. NM_001146318.1. [P16330-2 ]
    NP_034053.2. NM_009923.2. [P16330-1 ]
    UniGenei Mm.15711.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XMI X-ray 1.74 A 179-398 [» ]
    2Y1P X-ray 1.82 A 179-398 [» ]
    2Y3X X-ray 2.10 A/B/E 179-398 [» ]
    2YDB X-ray 2.15 A 179-398 [» ]
    2YDC X-ray 2.05 A 179-398 [» ]
    2YDD X-ray 2.40 A 179-398 [» ]
    2YOZ X-ray 2.10 A 179-398 [» ]
    2YP0 X-ray 2.30 A 179-398 [» ]
    2YPC X-ray 1.89 A 179-398 [» ]
    2YPE X-ray 1.90 A 179-398 [» ]
    2YPH X-ray 2.10 A 179-398 [» ]
    2YQ9 X-ray 1.90 A 179-398 [» ]
    3ZBR X-ray 2.30 A/B 179-398 [» ]
    3ZBS X-ray 2.45 A 179-398 [» ]
    3ZBZ X-ray 2.10 A 179-398 [» ]
    ProteinModelPortali P16330.
    SMRi P16330. Positions 53-123, 181-398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198792. 4 interactions.
    IntActi P16330. 11 interactions.
    MINTi MINT-1955077.

    PTM databases

    PhosphoSitei P16330.

    Proteomic databases

    MaxQBi P16330.
    PaxDbi P16330.
    PRIDEi P16330.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000103120 ; ENSMUSP00000099409 ; ENSMUSG00000006782 . [P16330-1 ]
    GeneIDi 12799.
    KEGGi mmu:12799.
    UCSCi uc007llo.2. mouse. [P16330-1 ]

    Organism-specific databases

    CTDi 1267.
    MGIi MGI:88437. Cnp.

    Phylogenomic databases

    eggNOGi NOG314041.
    HOGENOMi HOG000111838.
    HOVERGENi HBG001451.
    InParanoidi P16330.
    KOi K01121.
    OMAi LWPNDVD.
    OrthoDBi EOG78PVBC.
    PhylomeDBi P16330.
    TreeFami TF332157.

    Miscellaneous databases

    ChiTaRSi CNP. mouse.
    NextBioi 282222.
    PROi P16330.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16330.
    Bgeei P16330.
    CleanExi MM_CNP.
    Genevestigatori P16330.

    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. "Structure of mouse 2',3'-cyclic-nucleotide 3'-phosphodiesterase gene."
      Monoh K., Kurihara T., Sakimura K., Takahashi Y.
      Biochem. Biophys. Res. Commun. 165:1213-1220(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CNPI).
      Strain: DBA.
    2. "Alternative splicing of mouse brain 2',3'-cyclic-nucleotide 3'-phosphodiesterase mRNA."
      Kurihara T., Monoh K., Sakimura K., Takahashi Y.
      Biochem. Biophys. Res. Commun. 170:1074-1081(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS CNPI AND CNPII).
      Strain: DBA.
      Tissue: Brain.
    3. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
      Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
      Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CNPI).
      Strain: ILS and ISS.
    4. "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] (ISOFORM CNPII).
      Strain: FVB/N.
      Tissue: Mammary tumor.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-418 (ISOFORM CNPII).
      Strain: C57BL/6J.
      Tissue: Thymus.
    6. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 94-101; 103-112; 117-127; 130-150; 164-174; 183-195; 203-216; 235-243; 261-274; 276-293; 356-368; 379-385 AND 391-399.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    7. "Structures and micelle locations of the nonlipidated and lipidated C-terminal membrane anchor of 2',3'-cyclic nucleotide-3'-phosphodiesterase."
      Esposito C., Scrima M., Carotenuto A., Tedeschi A., Rovero P., D'Errico G., Malfitano A.M., Bifulco M., D'Ursi A.M.
      Biochemistry 47:308-319(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION, SUBCELLULAR LOCATION.
    8. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    9. "Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: active-site ligand binding and molecular conformation."
      Myllykoski M., Raasakka A., Han H., Kursula P.
      PLoS ONE 7:E32336-E32336(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 179-398, ACTIVE SITE, SUBSTRATE-BINDING SITES, RNA-BINDING, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiCN37_MOUSE
    AccessioniPrimary (citable) accession number: P16330
    Secondary accession number(s): Q61424
    , Q8C7C9, Q91V42, Q923F3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3