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Protein

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

Gene

Cnp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. 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
  11. substantia nigra development Source: Ensembl
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 1 Publication; Lipid-anchor 1 Publication. Melanosome By similarity
Note: Firmly bound to membrane structures of brain white matter.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. extracellular space Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. melanosome Source: UniProtKB-SubCell
  5. membrane Source: MGI
  6. microtubule Source: MGI
  7. microvillus Source: Ensembl
  8. mitochondrial inner membrane Source: Ensembl
  9. mitochondrial outer membrane Source: Ensembl
  10. myelin sheath Source: UniProtKB
  11. myelin sheath abaxonal region Source: Ensembl
  12. myelin sheath adaxonal region Source: Ensembl
  13. nucleoplasm Source: MGI
  14. nucleus Source: MGI
  15. perinuclear region of cytoplasm Source: Ensembl
  16. plasma membrane Source: Ensembl
  17. 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'-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

BgeeiP16330.
CleanExiMM_CNP.
ExpressionAtlasiP16330. baseline and differential.
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 – 1937Combined sources
Helixi195 – 21420Combined sources
Helixi216 – 2205Combined sources
Helixi222 – 2254Combined sources
Helixi237 – 2404Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi250 – 2556Combined sources
Helixi257 – 2593Combined sources
Helixi264 – 2685Combined sources
Helixi271 – 2766Combined sources
Beta strandi280 – 29011Combined sources
Beta strandi292 – 3009Combined sources
Helixi303 – 3064Combined sources
Helixi317 – 3193Combined sources
Beta strandi320 – 3223Combined sources
Turni324 – 3274Combined sources
Beta strandi329 – 3346Combined sources
Helixi342 – 35514Combined sources
Turni357 – 3593Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi369 – 3757Combined sources
Beta strandi378 – 39619Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 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. AlignAdd to basket

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

        10         20         30         40         50
MNTSFTRKSH TFLPKLFFRK MSSSGAKEKP ELQFPFLQDE DTVATLHECK
60 70 80 90 100
TLFILRGLPG SGKSTLARLI LEKYHDGTKM VSADAYKIIP GSRADFSEAY
110 120 130 140 150
KRLDEDLAGY CRRDIRVLVL DDTNHERERL DQLFEMADQY QYQVVLVEPK
160 170 180 190 200
TAWRLDCAQL KEKNQWQLSA DDLKKLKPGL EKDFLPLYFG WFLTKKSSET
210 220 230 240 250
LRKAGQVFLE ELGNHKAFKK ELRHFISGDE PKEKLELVSY FGKRPPGVLH
260 270 280 290 300
CTTKFCDYGK AAGAEEYAQQ EVVKRSYGKA FKLSISALFV TPKTAGAQVV
310 320 330 340 350
LTDQELQLWP SDLDKPSASE GLPPGSRAHV TLGCAADVQP VQTGLDLLDI
360 370 380 390 400
LQQVKGGSQG EAVGELPRGK LYSLGKGRWM LSLTKKMEVK AIFTGYYGKG
410 420
KPVPIHGSRK GGAMQICTII
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 181-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP16330.

Proteomic databases

MaxQBiP16330.
PaxDbiP16330.
PRIDEiP16330.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1267.
MGIiMGI:88437. Cnp.

Phylogenomic databases

eggNOGiNOG314041.
HOGENOMiHOG000111838.
HOVERGENiHBG001451.
InParanoidiP16330.
KOiK01121.
OMAiLWPNDVD.
OrthoDBiEOG78PVBC.
PhylomeDBiP16330.
TreeFamiTF332157.

Miscellaneous databases

ChiTaRSiCnp. mouse.
NextBioi282222.
PROiP16330.
SOURCEiSearch...

Gene expression databases

BgeeiP16330.
CleanExiMM_CNP.
ExpressionAtlasiP16330. baseline and differential.
GenevestigatoriP16330.

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.
ProtoNetiSearch...

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: March 4, 2015
This is version 142 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.