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Protein

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

Gene

Cnp

Organism
Rattus norvegicus (Rat)
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.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei250 – 2501Proton acceptor
Binding sitei252 – 2521SubstrateBy similarity
Active sitei329 – 3291Proton donor
Binding sitei331 – 3311SubstrateBy similarity

GO - Molecular functioni

  • 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity Source: RGD
  • cyclic nucleotide binding Source: RGD
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • adult locomotory behavior Source: Ensembl
  • aging Source: RGD
  • axonogenesis Source: Ensembl
  • cyclic nucleotide catabolic process Source: InterPro
  • forebrain development Source: RGD
  • microtubule cytoskeleton organization Source: RGD
  • oligodendrocyte differentiation Source: Ensembl
  • regulation of mitochondrial membrane permeability Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to toxic substance Source: Ensembl
  • 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi2368. Cnp.

Subcellular locationi

GO - Cellular componenti

  • cell projection Source: RGD
  • cytoplasm Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: Ensembl
  • melanosome Source: UniProtKB-SubCell
  • microtubule Source: Ensembl
  • microvillus Source: RGD
  • mitochondrial inner membrane Source: RGD
  • mitochondrial outer membrane Source: RGD
  • myelin sheath Source: UniProtKB
  • myelin sheath abaxonal region Source: RGD
  • myelin sheath adaxonal region Source: RGD
  • nucleoplasm Source: Ensembl
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: RGD
  • pseudopodium Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi250 – 2501H → L: Reduces activity 15000-fold. 1 Publication
Mutagenesisi252 – 2521T → A: Reduces activity 100-fold. 1 Publication
Mutagenesisi329 – 3291H → L: Reduces activity 15000-fold. 1 Publication
Mutagenesisi331 – 3311T → A: Reduces activity 700-fold. 1 Publication
Mutagenesisi344 – 3441G → A: Alters secondary structure and lowers activity. 1 Publication
Mutagenesisi417 – 4171C → S: Abolishes binding to myelin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4174172',3'-cyclic-nucleotide 3'-phosphodiesterasePRO_0000089963Add
BLAST
Propeptidei418 – 4203Removed in mature formCuratedPRO_0000422299

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101PhosphotyrosineBy similarity
Modified residuei169 – 1691PhosphoserineCombined sources
Modified residuei227 – 2271PhosphoserineCombined sources
Modified residuei239 – 2391PhosphoserineCombined sources
Modified residuei262 – 2621PhosphothreonineCombined sources
Modified residuei358 – 3581PhosphoserineCombined sources
Modified residuei417 – 4171Cysteine methyl esterCurated
Lipidationi417 – 4171S-farnesyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiP13233.
PRIDEiP13233.

PTM databases

iPTMnetiP13233.
PhosphoSiteiP13233.

Expressioni

Gene expression databases

GenevisibleiP13233. RN.

Interactioni

Subunit structurei

Exists as monomers and homodimers.By similarity

Protein-protein interaction databases

BioGridi247315. 3 interactions.
IntActiP13233. 1 interaction.
STRINGi10116.ENSRNOP00000023875.

Structurei

Secondary structure

1
420
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi187 – 1937Combined sources
Helixi195 – 21319Combined sources
Helixi216 – 2194Combined sources
Helixi222 – 2254Combined sources
Beta strandi229 – 2313Combined sources
Helixi237 – 2404Combined sources
Beta strandi250 – 2556Combined sources
Turni257 – 2604Combined sources
Beta strandi261 – 2633Combined sources
Helixi264 – 2685Combined sources
Helixi271 – 2766Combined sources
Beta strandi280 – 29011Combined sources
Beta strandi295 – 2995Combined sources
Helixi303 – 3075Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi317 – 3204Combined sources
Beta strandi326 – 3316Combined sources
Helixi340 – 35516Combined sources
Beta strandi361 – 3666Combined sources
Beta strandi369 – 3735Combined sources
Beta strandi379 – 39618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ILXNMR-A184-398[»]
ProteinModelPortaliP13233.
SMRiP13233. Positions 184-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13233.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IT06. Eukaryota.
ENOG4111F3B. LUCA.
GeneTreeiENSGT00510000048410.
HOGENOMiHOG000111838.
HOVERGENiHBG001451.
InParanoidiP13233.
KOiK01121.
OMAiLWPNDVD.
OrthoDBiEOG78PVBC.
PhylomeDBiP13233.
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.

Sequencei

Sequence statusi: Complete.

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

P13233-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTSFARKSH TFLPKIFFRK MSSSGAKDKP ELQFPFLQDE DTVATLHECK
60 70 80 90 100
TLFILRGLPG SGKSTLARLI VEKYHNGTKM VSADAYKIIP GSRADFSEEY
110 120 130 140 150
KRLDEDLAGY CRRDIRVLVL DDTNHERERL DQLFEMADQY QYQVVLVEPK
160 170 180 190 200
TAWRLDCAQL KEKNQWQLSL DDLKKLKPGL EKDFLPLYFG WFLTKKSSET
210 220 230 240 250
LRKAGQVFLE ELGNHKAFKK ELRHFISGDE PKEKLDLVSY FGKRPPGVLH
260 270 280 290 300
CTTKFCDYGK ATGAEEYAQQ DVVRRSYGKA FKLSISALFV TPKTAGAQVV
310 320 330 340 350
LNEQELQLWP SDLDKPSSSE SLPPGSRAHV TLGCAADVQP VQTGLDLLEI
360 370 380 390 400
LQQVKGGSQG EEVGELPRGK LYSLGKGRWM LSLAKKMEVK AIFTGYYGKG
410 420
KPVPVHGSRK GGAMQICTII
Length:420
Mass (Da):47,268
Last modified:August 16, 2004 - v2
Checksum:i83001BBA2C057826
GO

Sequence cautioni

The sequence AAA40939.1 differs from that shown.Sequencing errors.Curated
The sequence AAA40939.1 differs from that shown. Reason: Frameshift at several positions. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18630 mRNA. Translation: AAA40939.1. Sequence problems.
L16532 mRNA. Translation: AAA64429.1.
BC098066 mRNA. Translation: AAH98066.1.
PIRiA45670.
I56577.
RefSeqiNP_036941.1. NM_012809.2.
UniGeneiRn.31762.

Genome annotation databases

EnsembliENSRNOT00000023872; ENSRNOP00000023875; ENSRNOG00000017496.
GeneIDi25275.
KEGGirno:25275.
UCSCiRGD:2368. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18630 mRNA. Translation: AAA40939.1. Sequence problems.
L16532 mRNA. Translation: AAA64429.1.
BC098066 mRNA. Translation: AAH98066.1.
PIRiA45670.
I56577.
RefSeqiNP_036941.1. NM_012809.2.
UniGeneiRn.31762.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ILXNMR-A184-398[»]
ProteinModelPortaliP13233.
SMRiP13233. Positions 184-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247315. 3 interactions.
IntActiP13233. 1 interaction.
STRINGi10116.ENSRNOP00000023875.

PTM databases

iPTMnetiP13233.
PhosphoSiteiP13233.

Proteomic databases

PaxDbiP13233.
PRIDEiP13233.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023872; ENSRNOP00000023875; ENSRNOG00000017496.
GeneIDi25275.
KEGGirno:25275.
UCSCiRGD:2368. rat.

Organism-specific databases

CTDi1267.
RGDi2368. Cnp.

Phylogenomic databases

eggNOGiENOG410IT06. Eukaryota.
ENOG4111F3B. LUCA.
GeneTreeiENSGT00510000048410.
HOGENOMiHOG000111838.
HOVERGENiHBG001451.
InParanoidiP13233.
KOiK01121.
OMAiLWPNDVD.
OrthoDBiEOG78PVBC.
PhylomeDBiP13233.
TreeFamiTF332157.

Miscellaneous databases

EvolutionaryTraceiP13233.
NextBioi605973.
PROiP13233.

Gene expression databases

GenevisibleiP13233. RN.

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. "Molecular cloning of a 2',3'-cyclic nucleotide 3'-phosphodiesterase: mRNAs with different 5' ends encode the same set of proteins in nervous and lymphoid tissues."
    Bernier L., Alvarez F., Norgard E.M., Raible D.W., Mentaberry A., Schembri J.G., Sabatini D.D., Colman D.R.
    J. Neurosci. 7:2703-2710(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning and characterization of rat brain 2',3'-cyclic nucleotide 3'-phosphodiesterase isoform 2."
    Gravel M., DeAngelis D., Braun P.E.
    J. Neurosci. Res. 38:243-247(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "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].
    Tissue: Placenta.
  4. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-15; 20-63; 80-87; 94-112; 117-150; 155-202; 204-216; 224-274; 283-368 AND 379-410, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  5. "Isoprenylation of brain 2',3'-cyclic nucleotide 3'-phosphodiesterase modulates cell morphology."
    De Angelis D.A., Braun P.E.
    J. Neurosci. Res. 39:386-397(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-417, MUTAGENESIS OF CYS-417.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-227; SER-239; THR-262 AND SER-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Structural evidence that brain cyclic nucleotide phosphodiesterase is a member of the 2H phosphodiesterase superfamily."
    Kozlov G., Lee J., Elias D., Gravel M., Gutierrez P., Ekiel I., Braun P.E., Gehring K.
    J. Biol. Chem. 278:46021-46028(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 184-398 IN COMPLEX WITH PHOSPHATE, MUTAGENESIS OF HIS-250; THR-252; HIS-329; THR-331 AND GLY-344.

Entry informationi

Entry nameiCN37_RAT
AccessioniPrimary (citable) accession number: P13233
Secondary accession number(s): Q4V796, Q64575
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: August 16, 2004
Last modified: January 20, 2016
This is version 128 of the entry and version 2 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.