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P16330

- CN37_MOUSE

UniProt

P16330 - CN37_MOUSE

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Protein
2',3'-cyclic-nucleotide 3'-phosphodiesterase
Gene
Cnp, Cnp1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. RNA binding Source: UniProtKB-KW
  3. cyclic nucleotide binding Source: Ensembl

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
Complete GO annotation...

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

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
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4174172',3'-cyclic-nucleotide 3'-phosphodiesterase
PRO_0000089962Add
BLAST
Propeptidei418 – 4203Removed in mature form Inferred
PRO_0000422297

Amino acid modifications

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

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

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.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020Missing in isoform CNPI.
VSP_004172Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151I → M in BAA07621. 1 Publication
Sequence conflicti115 – 1151I → M in BAA07622. 1 Publication
Sequence conflicti136 – 1361M → L in BAA07621. 1 Publication
Sequence conflicti136 – 1361M → L in BAA07622. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 136 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

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