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P09543 (CN37_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2',3'-cyclic-nucleotide 3'-phosphodiesterase

Short name=CNP
Short name=CNPase
EC=3.1.4.37
Gene names
Name:CNP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Note: Firmly bound to membrane structures of brain white matter. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.8 Ref.9

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandRNA-binding
   Molecular functionHydrolase
   PTMLipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

axonogenesis

Inferred from electronic annotation. Source: Ensembl

cyclic nucleotide catabolic process

Inferred from electronic annotation. Source: InterPro

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

regulation of mitochondrial membrane permeability

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

synaptic transmission

Traceable author statement PubMed 1322358. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 12379507. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 12379507. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

microvillus

Inferred from electronic annotation. Source: Ensembl

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: Ensembl

myelin sheath abaxonal region

Inferred from electronic annotation. Source: Ensembl

myelin sheath adaxonal region

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

pseudopodium

Inferred from electronic annotation. Source: Ensembl

   Molecular_function2',3'-cyclic-nucleotide 3'-phosphodiesterase activity

Traceable author statement Ref.3. Source: ProtInc

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclic nucleotide binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform CNPII (identifier: P09543-1)

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.
Isoform CNPI (identifier: P09543-2)

Also known as: DNAI;

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4184182',3'-cyclic-nucleotide 3'-phosphodiesterase
PRO_0000089961
Propeptide419 – 4213Removed in mature form By similarity
PRO_0000422296

Sites

Active site2511Proton acceptor
Active site3301Proton donor
Binding site2531Substrate
Binding site3321Substrate

Amino acid modifications

Modified residue1101Phosphotyrosine By similarity
Modified residue4181Cysteine methyl ester By similarity
Lipidation4181S-farnesyl cysteine By similarity

Natural variations

Alternative sequence1 – 2020Missing in isoform CNPI.
VSP_004171
Natural variant2071Q → R.
Corresponds to variant rs34353668 [ dbSNP | Ensembl ].
VAR_033746

Secondary structure

..................................... 421
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform CNPII (DNAII) [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: CA6D0097DFD87255

FASTA42147,579
        10         20         30         40         50         60 
MNRGFSRKSH TFLPKIFFRK MSSSGAKDKP ELQFPFLQDE DTVATLLECK TLFILRGLPG 

        70         80         90        100        110        120 
SGKSTLARVI VDKYRDGTKM VSADAYKITP GARGAFSEEY KRLDEDLAAY CRRRDIRILV 

       130        140        150        160        170        180 
LDDTNHERER LEQLFEMADQ YQYQVVLVEP KTAWRLDCAQ LKEKNQWQLS ADDLKKLKPG 

       190        200        210        220        230        240 
LEKDFLPLYF GWFLTKKSSE TLRKAGQVFL EELGNHKAFK KELRQFVPGD EPREKMDLVT 

       250        260        270        280        290        300 
YFGKRPPGVL HCTTKFCDYG KAPGAEEYAQ QDVLKKSYSK AFTLTISALF VTPKTTGARV 

       310        320        330        340        350        360 
ELSEQQLQLW PSDVDKLSPT DNLPRGSRAH ITLGCAADVE AVQTGLDLLE ILRQEKGGSR 

       370        380        390        400        410        420 
GEEVGELSRG KLYSLGNGRW MLTLAKNMEV RAIFTGYYGK GKPVPTQGSR KGGALQSCTI 


I 

« Hide

Isoform CNPI (DNAI) [UniParc].

Checksum: 81F0E080822D3B0D
Show »

FASTA40145,099

References

« Hide 'large scale' references
[1]"2',3'-cyclic nucleotide-3'-phosphohydrolase and signal transduction in central nervous system myelin."
Thompson R.J.
Biochem. Soc. Trans. 20:621-626(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"cDNA cloning and amino acid sequence of human brain 2',3'-cyclic-nucleotide 3'-phosphodiesterase."
Kurihara T., Takahashi Y., Nishiyama A., Kumanishi T.
Biochem. Biophys. Res. Commun. 152:837-842(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CNPI).
Tissue: Brain.
[3]"Structure, expression and chromosomal localization of the gene encoding human 2',3'-cyclic-nucleotide 3'-phosphodiesterase."
Monoh K., Kurihara T., Takahashi Y., Ichikawa T., Kumanishi T., Hayashi S., Minoshima S., Shimizu N.
Gene 129:297-301(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structure and chromosomal localization of the human 2',3'-cyclic nucleotide 3'-phosphodiesterase gene."
Douglas A.J., Fox M.F., Abbott C.M., Hinks L.J., Sharpe G., Povey S., Thompson R.J.
Ann. Hum. Genet. 56:243-254(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS CNPI AND CNPII).
Tissue: Brain and Skin.
[7]"The epitope recognized by a monoclonal antibody in the myelin-associated protein CNP."
Stricker R., Kalbacher H., Reiser G.
Biochem. Biophys. Res. Commun. 237:266-270(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-58.
[8]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[9]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Crystal structure of the catalytic fragment of human brain 2',3'-cyclic-nucleotide 3'-phosphodiesterase."
Sakamoto Y., Tanaka N., Ichimiya T., Kurihara T., Nakamura K.T.
J. Mol. Biol. 346:789-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 186-399 IN COMPLEX WITH PHOSPHATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S46849 expand/collapse EMBL AC list , S46843, S46845, S46846 Genomic DNA. Translation: AAB23928.2.
M19650 mRNA. Translation: AAA35704.1.
D13146 Genomic DNA. Translation: BAA39694.1.
D13146 Genomic DNA. Translation: BAA02435.1.
S50017 expand/collapse EMBL AC list , S50013, S50014, S50016 Genomic DNA. Translation: AAB24298.2.
AC125257 Genomic DNA. No translation available.
BC001362 mRNA. Translation: AAH01362.1.
BC006392 mRNA. Translation: AAH06392.1.
BC011046 mRNA. Translation: AAH11046.1.
BC028040 mRNA. Translation: AAH28040.1.
PIRJC1517.
RefSeqNP_149124.3. NM_033133.4.
UniGeneHs.273621.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WOJX-ray1.80A186-399[»]
ProteinModelPortalP09543.
SMRP09543. Positions 36-161, 186-399.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107667. 9 interactions.
IntActP09543. 5 interactions.
MINTMINT-4999529.
STRING9606.ENSP00000377470.

PTM databases

PhosphoSiteP09543.

Polymorphism databases

DMDM1705945.

2D gel databases

UCD-2DPAGEP09543.

Proteomic databases

PaxDbP09543.
PRIDEP09543.

Protocols and materials databases

DNASU1267.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393888; ENSP00000377466; ENSG00000173786. [P09543-2]
ENST00000393892; ENSP00000377470; ENSG00000173786. [P09543-1]
ENST00000562963; ENSP00000457200; ENSG00000260283. [P09543-1]
ENST00000563912; ENSP00000454542; ENSG00000260283. [P09543-2]
GeneID1267.
KEGGhsa:1267.
UCSCuc002hyl.1. human. [P09543-1]

Organism-specific databases

CTD1267.
GeneCardsGC17P040118.
HGNCHGNC:2158. CNP.
HPACAB002672.
HPA023266.
HPA023278.
HPA023280.
HPA023338.
MIM123830. gene.
neXtProtNX_P09543.
PharmGKBPA26680.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314041.
HOGENOMHOG000111838.
HOVERGENHBG001451.
InParanoidP09543.
KOK01121.
OMALWPNDVD.
PhylomeDBP09543.
TreeFamTF332157.

Gene expression databases

ArrayExpressP09543.
BgeeP09543.
CleanExHS_CNP.
GenevestigatorP09543.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR008431. CNPase.
IPR027417. P-loop_NTPase.
IPR009097. RNA_ligase/cNuc_Pdiesterase.
[Graphical view]
PANTHERPTHR10156. PTHR10156. 1 hit.
PfamPF05881. CNPase. 1 hit.
[Graphical view]
PIRSFPIRSF000970. CNPase. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
SSF55144. SSF55144. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCNP. human.
EvolutionaryTraceP09543.
GeneWiki2%27,3%27-Cyclic-nucleotide_3%27-phosphodiesterase.
GenomeRNAi1267.
NextBio5129.
PROP09543.
SOURCESearch...

Entry information

Entry nameCN37_HUMAN
AccessionPrimary (citable) accession number: P09543
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM