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

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P13233 (CN37_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
2',3'-cyclic-nucleotide 3'-phosphodiesterase
Short name=CNP
Short name=CNPase
EC=3.1.4.37

Gene names

Name:	Cnp
Synonyms:	Cnp1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity.
Catalytic activity	Nucleoside 2',3'-cyclic phosphate + H₂O = nucleoside 2'-phosphate.
Subunit structure	Exists as monomers and homodimers By similarity.
Subcellular location	Membrane; Lipid-anchor. Melanosome By similarity. Note: Firmly bound to membrane structures of brain white matter.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family.
Sequence caution	The sequence AAA40939.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAA40939.1 differs from that shown. Reason: Sequencing errors.

Ontologies

Keywords
Cellular component	Membrane
Ligand	RNA-binding
Molecular function	Hydrolase
PTM	Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA metabolic process Inferred from electronic annotation. Source: InterPro adult locomotory behavior Inferred from electronic annotation. Source: Compara aging Inferred from expression pattern PubMed 21284091. Source: RGD axonogenesis Inferred from electronic annotation. Source: Compara cyclic nucleotide catabolic process Inferred from electronic annotation. Source: InterPro forebrain development Inferred from expression pattern PubMed 16876328. Source: RGD microtubule cytoskeleton organization Inferred from mutant phenotype PubMed 11842207. Source: RGD regulation of mitochondrial membrane permeability Inferred from mutant phenotype PubMed 19357238. Source: RGD response to lipopolysaccharide Inferred from expression pattern PubMed 17000237. Source: RGD response to toxin Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: Compara microvillus Inferred from direct assay PubMed 16876328. Source: RGD mitochondrial inner membrane Inferred from direct assay PubMed 19357238. Source: RGD mitochondrial outer membrane Inferred from direct assay PubMed 19357238. Source: RGD myelin sheath abaxonal region Inferred from direct assay PubMed 16051705. Source: RGD myelin sheath adaxonal region Inferred from direct assay PubMed 16051705. Source: RGD perinuclear region of cytoplasm Inferred from direct assay PubMed 11842207. Source: RGD plasma membrane Inferred from direct assay PubMed 11842207. Source: RGD pseudopodium Inferred from direct assay PubMed 16876328. Source: RGD
Molecular_function	2',3'-cyclic-nucleotide 3'-phosphodiesterase activity Inferred from direct assay PubMed 19357238. Source: RGD RNA binding Inferred from electronic annotation. Source: UniProtKB-KW cyclic nucleotide binding Inferred from direct assay PubMed 19357238. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 417

417

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

PRO_0000089963

Propeptide

418 – 420

Removed in mature form Probable

PRO_0000422299

Sites

Active site

250

Proton acceptor

Active site

329

Proton donor

Binding site

252

Substrate By similarity

Binding site

331

Substrate By similarity

Amino acid modifications

Modified residue

110

Phosphotyrosine By similarity

Modified residue

372

Phosphotyrosine By similarity

Modified residue

417

Cysteine methyl ester Probable

Lipidation

417

S-farnesyl cysteine Probable

Experimental info

Mutagenesis

250

H → L: Reduces activity 15000-fold. Ref.6

Mutagenesis

252

T → A: Reduces activity 100-fold. Ref.6

Mutagenesis

329

H → L: Reduces activity 15000-fold. Ref.6

Mutagenesis

331

T → A: Reduces activity 700-fold. Ref.6

Mutagenesis

344

G → A: Alters secondary structure and lowers activity. Ref.6

Mutagenesis

417

C → S: Abolishes binding to myelin. Ref.5

Secondary structure

420

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P13233 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 83001BBA2C057826
Show »

FASTA

420

47,268

        10         20         30         40         50         60 
MSTSFARKSH TFLPKIFFRK MSSSGAKDKP ELQFPFLQDE DTVATLHECK TLFILRGLPG 

        70         80         90        100        110        120 
SGKSTLARLI VEKYHNGTKM VSADAYKIIP GSRADFSEEY KRLDEDLAGY CRRDIRVLVL 

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

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

       250        260        270        280        290        300 
FGKRPPGVLH CTTKFCDYGK ATGAEEYAQQ DVVRRSYGKA FKLSISALFV TPKTAGAQVV 

       310        320        330        340        350        360 
LNEQELQLWP SDLDKPSSSE SLPPGSRAHV TLGCAADVQP VQTGLDLLEI LQQVKGGSQG 

       370        380        390        400        410        420 
EEVGELPRGK LYSLGKGRWM LSLAKKMEVK AIFTGYYGKG KPVPVHGSRK GGAMQICTII

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M18630 mRNA. Translation: AAA40939.1. Sequence problems.
L16532 mRNA. Translation: AAA64429.1.
BC098066 mRNA. Translation: AAH98066.1.

IPI

IPI00199394.

PIR

A45670.
I56577.

RefSeq

NP_036941.1. NM_012809.2.

UniGene

Rn.31762.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ILX	NMR	-	A	184-398	[»]

ProteinModelPortal

P13233.

SMR

P13233. Positions 184-398.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13233. 1 interaction.

PTM databases

PhosphoSite

P13233.

Proteomic databases

PaxDb

P13233.

PRIDE

P13233.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000023872; ENSRNOP00000023875; ENSRNOG00000017496.

GeneID

25275.

KEGG

rno:25275.

UCSC

RGD:2368. rat.

Organism-specific databases

CTD

1267.

RGD

2368. Cnp.

Phylogenomic databases

eggNOG

NOG314041.

GeneTree

ENSGT00510000048410.

HOGENOM

HOG000111838.

HOVERGEN

HBG001451.

InParanoid

P13233.

K01121.

OrthoDB

EOG4D52ZC.

Gene expression databases

Genevestigator

P13233.

GermOnline

ENSRNOG00000017496. Rattus norvegicus.

Family and domain databases

InterPro

IPR008431. CNPase.
IPR009097. RNA_ligase/cNuc_Pdiesterase.
[Graphical view]

PANTHER

PTHR10156. PTHR10156. 1 hit.

Pfam

PF05881. CNPase. 1 hit.
[Graphical view]

PIRSF

PIRSF000970. CNPase. 1 hit.

SUPFAM

SSF55144. Cyc_nuc_Pdiester. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P13233.

NextBio

605973.

Entry information

Entry name

CN37_RAT

Accession

Primary (citable) accession number: P13233
Secondary accession number(s): Q4V796, Q64575

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents