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Protein

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

Gene

CNP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 sitei230 – 2301Proton acceptorBy similarity
Binding sitei232 – 2321SubstrateBy similarity
Active sitei309 – 3091Proton donorBy similarity
Binding sitei311 – 3111SubstrateBy similarity

GO - Molecular functioni

  1. 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity Source: GO_Central
  2. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. adult locomotory behavior Source: Ensembl
  2. axonogenesis Source: Ensembl
  3. cyclic nucleotide catabolic process Source: InterPro
  4. oligodendrocyte differentiation Source: Ensembl
  5. response to toxic substance Source: Ensembl
  6. 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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 19

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. melanosome Source: UniProtKB-SubCell
  5. membrane Source: UniProtKB-SubCell
  6. microtubule Source: Ensembl
  7. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3973972',3'-cyclic-nucleotide 3'-phosphodiesterasePRO_0000089960Add
BLAST
Propeptidei398 – 4003Removed in mature formBy similarityPRO_0000422295

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei397 – 3971Cysteine methyl esterBy similarity
Lipidationi397 – 3971S-farnesyl cysteineBy similarity

Post-translational modificationi

Met-1 may be removed after translation.

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PRIDEiP06623.

Interactioni

Subunit structurei

Exists as monomers and homodimers.By similarity

Protein-protein interaction databases

IntActiP06623. 1 interaction.
STRINGi9913.ENSBTAP00000036278.

Structurei

3D structure databases

ProteinModelPortaliP06623.
SMRiP06623. Positions 165-378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG314041.
GeneTreeiENSGT00510000048410.
HOGENOMiHOG000111838.
HOVERGENiHBG001451.
InParanoidiP06623.
KOiK01121.
OMAiLWPNDVD.
OrthoDBiEOG78PVBC.
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.

P06623-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSSGAKDKP ELQFPFLQDE ETVATLQECK TLFILRGLPG SGKSTLARFI
60 70 80 90 100
VDKYRDGTKM VSADSYKITP GARGSFSEEY KQLDEDLAAC CRRDFRVLVL
110 120 130 140 150
DDTNHERERL EQLFELADQY QYQVVLVEPK TAWRLDCAQL KEKNQWQLSA
160 170 180 190 200
DDLKKLKPGL EKDFLPLYFG WFLTKKSSAA LWKTGQTFLE ELGNHKAFKK
210 220 230 240 250
ELRHFVSGDE PREKIELVTY FGKRPPGVLH CTTKFCDYGK AAGAEEYAQQ
260 270 280 290 300
DVVKKSYCKA FTLTISALFV TPKTTGARVE LSEQQLALWP NDVDKLSPSD
310 320 330 340 350
NLPRGSRAHI TLGCAGDVEA VQTGIDLLEI VRQEKGGSRG EEVGELSRGK
360 370 380 390 400
LYSLGSGRWM LSLAKKMEVR AIFTGYYGKG KAVPIRSGRK GGSFQSCTII
Length:400
Mass (Da):44,875
Last modified:July 1, 1993 - v2
Checksum:i3448FC367D647CF8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02659 mRNA. Translation: AAA30456.1. Sequence problems.
Y00405 mRNA. Translation: CAA68466.1.
M27606 mRNA. Translation: AAA30457.1.
BC102820 mRNA. Translation: AAI02821.2.
PIRiA26861. ESBOP3.
RefSeqiNP_851336.1. NM_180993.2.
XP_005220719.1. XM_005220662.1.
UniGeneiBt.5517.

Genome annotation databases

EnsembliENSBTAT00000036420; ENSBTAP00000036278; ENSBTAG00000025762.
GeneIDi280752.
KEGGibta:280752.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02659 mRNA. Translation: AAA30456.1. Sequence problems.
Y00405 mRNA. Translation: CAA68466.1.
M27606 mRNA. Translation: AAA30457.1.
BC102820 mRNA. Translation: AAI02821.2.
PIRiA26861. ESBOP3.
RefSeqiNP_851336.1. NM_180993.2.
XP_005220719.1. XM_005220662.1.
UniGeneiBt.5517.

3D structure databases

ProteinModelPortaliP06623.
SMRiP06623. Positions 165-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP06623. 1 interaction.
STRINGi9913.ENSBTAP00000036278.

Proteomic databases

PRIDEiP06623.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000036420; ENSBTAP00000036278; ENSBTAG00000025762.
GeneIDi280752.
KEGGibta:280752.

Organism-specific databases

CTDi1267.

Phylogenomic databases

eggNOGiNOG314041.
GeneTreeiENSGT00510000048410.
HOGENOMiHOG000111838.
HOVERGENiHBG001451.
InParanoidiP06623.
KOiK01121.
OMAiLWPNDVD.
OrthoDBiEOG78PVBC.
TreeFamiTF332157.

Miscellaneous databases

NextBioi20804919.

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. "cDNA cloning and amino acid sequence of bovine brain 2',3'-cyclic-nucleotide 3'-phosphodiesterase."
    Kurihara T., Fowler A.V., Takahashi Y.
    J. Biol. Chem. 262:3256-3261(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Erratum
    Kurihara T., Fowler A.V., Takahashi Y.
    J. Biol. Chem. 262:16754-16754(1987)
    Cited for: SEQUENCE REVISION TO 318.
  3. "Nucleotide sequence of bovine retina 2',3'-cyclic nucleotide 3'-phosphohydrolase."
    Vogel U.S., Thompson R.J.
    Nucleic Acids Res. 15:7204-7204(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  4. "Molecular cloning of the myelin specific enzyme 2',3'-cyclic-nucleotide 3'-phosphohydrolase."
    Vogel U.S., Thompson R.J.
    FEBS Lett. 218:261-265(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.

Entry informationi

Entry nameiCN37_BOVIN
AccessioniPrimary (citable) accession number: P06623
Secondary accession number(s): Q3SZJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 1, 1993
Last modified: February 4, 2015
This is version 111 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

Complete proteome, Reference proteome

Documents

  1. 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.