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P16330 (CN37_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2',3'-cyclic-nucleotide 3'-phosphodiesterase

Short name=CNP
Short name=CNPase
EC=3.1.4.37
Gene names
Name:Cnp
Synonyms:Cnp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin. Ref.9

Catalytic activity

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

Subunit structure

Exists as monomers and homodimers. Ref.9

Subcellular location

Membrane; Lipid-anchor. Melanosome By similarity. Note: Firmly bound to membrane structures of brain white matter. Ref.7

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   Molecular functionHydrolase
   PTMLipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from mutant phenotype PubMed 12590258. Source: MGI

aging

Inferred from electronic annotation. Source: Ensembl

axonogenesis

Inferred from mutant phenotype PubMed 12590258. Source: MGI

cyclic nucleotide catabolic process

Inferred from electronic annotation. Source: InterPro

forebrain development

Inferred from electronic annotation. Source: Ensembl

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

regulation of mitochondrial membrane permeability

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from direct assay PubMed 20578039. Source: MGI

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 12590258. Source: MGI

microtubule

Inferred from electronic annotation. Source: Ensembl

microvillus

Inferred from electronic annotation. Source: Ensembl

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: Ensembl

myelin sheath abaxonal region

Inferred from electronic annotation. Source: Ensembl

myelin sheath adaxonal region

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

pseudopodium

Inferred from electronic annotation. Source: Ensembl

   Molecular_function2',3'-cyclic-nucleotide 3'-phosphodiesterase activity

Inferred from direct assay PubMed 12590258. Source: MGI

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclic nucleotide binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform CNPII (identifier: P16330-1)

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.
Isoform CNPI (identifier: P16330-2)

Also known as: DNAI;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4174172',3'-cyclic-nucleotide 3'-phosphodiesterase
PRO_0000089962
Propeptide418 – 4203Removed in mature form Probable
PRO_0000422297

Sites

Active site2501Proton acceptor Ref.9
Active site3291Proton donor Ref.9
Binding site2521Substrate
Binding site3311Substrate

Amino acid modifications

Modified residue1101Phosphotyrosine Ref.8
Modified residue4171Cysteine methyl ester Probable
Lipidation4171S-farnesyl cysteine Probable

Natural variations

Alternative sequence1 – 2020Missing in isoform CNPI.
VSP_004172

Experimental info

Sequence conflict1151I → M in BAA07621. Ref.1
Sequence conflict1151I → M in BAA07622. Ref.1
Sequence conflict1361M → L in BAA07621. Ref.1
Sequence conflict1361M → L in BAA07622. Ref.1

Secondary structure

............................................ 420
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform CNPII (DNAII) [UniParc].

Last modified August 16, 2004. Version 3.
Checksum: 2FAFFDE5F0E99EAB

FASTA42047,123
        10         20         30         40         50         60 
MNTSFTRKSH TFLPKLFFRK MSSSGAKEKP ELQFPFLQDE DTVATLHECK TLFILRGLPG 

        70         80         90        100        110        120 
SGKSTLARLI LEKYHDGTKM VSADAYKIIP GSRADFSEAY KRLDEDLAGY CRRDIRVLVL 

       130        140        150        160        170        180 
DDTNHERERL DQLFEMADQY QYQVVLVEPK TAWRLDCAQL KEKNQWQLSA DDLKKLKPGL 

       190        200        210        220        230        240 
EKDFLPLYFG WFLTKKSSET LRKAGQVFLE ELGNHKAFKK ELRHFISGDE PKEKLELVSY 

       250        260        270        280        290        300 
FGKRPPGVLH CTTKFCDYGK AAGAEEYAQQ EVVKRSYGKA FKLSISALFV TPKTAGAQVV 

       310        320        330        340        350        360 
LTDQELQLWP SDLDKPSASE GLPPGSRAHV TLGCAADVQP VQTGLDLLDI LQQVKGGSQG 

       370        380        390        400        410        420 
EAVGELPRGK LYSLGKGRWM LSLTKKMEVK AIFTGYYGKG KPVPIHGSRK GGAMQICTII 

« Hide

Isoform CNPI (DNAI) [UniParc].

Checksum: B974404499DE29BE
Show »

FASTA40044,654

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS25427.1. [P16330-1]
PIRESMS32. A35708.
RefSeqNP_001139790.1. NM_001146318.1. [P16330-2]
NP_034053.2. NM_009923.2. [P16330-1]
UniGeneMm.15711.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP16330.
SMRP16330. Positions 53-123, 181-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198792. 4 interactions.
IntActP16330. 11 interactions.
MINTMINT-1955077.

PTM databases

PhosphoSiteP16330.

Proteomic databases

MaxQBP16330.
PaxDbP16330.
PRIDEP16330.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103120; ENSMUSP00000099409; ENSMUSG00000006782. [P16330-1]
GeneID12799.
KEGGmmu:12799.
UCSCuc007llo.2. mouse. [P16330-1]

Organism-specific databases

CTD1267.
MGIMGI:88437. Cnp.

Phylogenomic databases

eggNOGNOG314041.
HOGENOMHOG000111838.
HOVERGENHBG001451.
InParanoidP16330.
KOK01121.
OMALWPNDVD.
OrthoDBEOG78PVBC.
PhylomeDBP16330.
TreeFamTF332157.

Gene expression databases

ArrayExpressP16330.
BgeeP16330.
CleanExMM_CNP.
GenevestigatorP16330.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR008431. CNPase.
IPR027417. P-loop_NTPase.
IPR009097. RNA_ligase/cNuc_Pdiesterase.
[Graphical view]
PANTHERPTHR10156. PTHR10156. 1 hit.
PfamPF05881. CNPase. 1 hit.
[Graphical view]
PIRSFPIRSF000970. CNPase. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
SSF55144. SSF55144. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCNP. mouse.
NextBio282222.
PROP16330.
SOURCESearch...

Entry information

Entry nameCN37_MOUSE
AccessionPrimary (citable) accession number: P16330
Secondary accession number(s): Q61424 expand/collapse secondary AC list , Q8C7C9, Q91V42, Q923F3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot