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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)DescriptionActionsGraphical viewLength
Active sitei250Proton acceptor1
Binding sitei252SubstrateBy similarity1
Active sitei329Proton donor1
Binding sitei331SubstrateBy similarity1

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: RGD
  • aging Source: RGD
  • axonogenesis Source: RGD
  • cyclic nucleotide catabolic process Source: InterPro
  • forebrain development Source: RGD
  • microtubule cytoskeleton organization Source: RGD
  • oligodendrocyte differentiation Source: RGD
  • regulation of mitochondrial membrane permeability Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to toxic substance Source: RGD
  • substantia nigra development Source: RGD

Keywordsi

Molecular functionHydrolase, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi2368. Cnp.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi250H → L: Reduces activity 15000-fold. 1 Publication1
Mutagenesisi252T → A: Reduces activity 100-fold. 1 Publication1
Mutagenesisi329H → L: Reduces activity 15000-fold. 1 Publication1
Mutagenesisi331T → A: Reduces activity 700-fold. 1 Publication1
Mutagenesisi344G → A: Alters secondary structure and lowers activity. 1 Publication1
Mutagenesisi417C → S: Abolishes binding to myelin. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000899631 – 4172',3'-cyclic-nucleotide 3'-phosphodiesteraseAdd BLAST417
PropeptideiPRO_0000422299418 – 420Removed in mature formCurated3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9PhosphoserineBy similarity1
Modified residuei110PhosphotyrosineBy similarity1
Modified residuei169PhosphoserineCombined sources1
Modified residuei227PhosphoserineCombined sources1
Modified residuei239PhosphoserineCombined sources1
Modified residuei262PhosphothreonineCombined sources1
Modified residuei358PhosphoserineCombined sources1
Modified residuei417Cysteine methyl esterCurated1
Lipidationi417S-farnesyl cysteine1 Publication1

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiP13233.
PRIDEiP13233.

PTM databases

iPTMnetiP13233.
PhosphoSitePlusiP13233.

Expressioni

Gene expression databases

BgeeiENSRNOG00000017496.
GenevisibleiP13233. RN.

Interactioni

Subunit structurei

Exists as monomers and homodimers.By similarity

Protein-protein interaction databases

BioGridi247315. 3 interactors.
IntActiP13233. 1 interactor.
STRINGi10116.ENSRNOP00000023875.

Structurei

Secondary structure

1420
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi187 – 193Combined sources7
Helixi195 – 213Combined sources19
Helixi216 – 219Combined sources4
Helixi222 – 225Combined sources4
Beta strandi229 – 231Combined sources3
Helixi237 – 240Combined sources4
Beta strandi250 – 255Combined sources6
Turni257 – 260Combined sources4
Beta strandi261 – 263Combined sources3
Helixi264 – 268Combined sources5
Helixi271 – 276Combined sources6
Beta strandi280 – 290Combined sources11
Beta strandi295 – 299Combined sources5
Helixi303 – 307Combined sources5
Beta strandi313 – 315Combined sources3
Beta strandi317 – 320Combined sources4
Beta strandi326 – 331Combined sources6
Helixi340 – 355Combined sources16
Beta strandi361 – 366Combined sources6
Beta strandi369 – 373Combined sources5
Beta strandi379 – 396Combined sources18

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP13233.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IT06. Eukaryota.
ENOG4111F3B. LUCA.
GeneTreeiENSGT00510000048410.
HOGENOMiHOG000111838.
HOVERGENiHBG001451.
InParanoidiP13233.
KOiK01121.
OMAiLWPNDVD.
OrthoDBiEOG091G0I8Z.
PhylomeDBiP13233.
TreeFamiTF332157.

Family and domain databases

InterProiView protein in InterPro
IPR008431. CNPase.
IPR009097. cNuc_Pdiesterase.
IPR027417. P-loop_NTPase.
PANTHERiPTHR10156. PTHR10156. 1 hit.
PfamiView protein in Pfam
PF05881. CNPase. 1 hit.
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 differs from that shown. Sequencing errors.Curated
The sequence AAA40939 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.

Similar proteinsi

Entry informationi

Entry nameiCN37_RAT
AccessioniPrimary (citable) accession number: P13233
Secondary accession number(s): Q4V796, Q64575
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: August 16, 2004
Last modified: November 22, 2017
This is version 139 of the entry and version 2 of the sequence. See 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