P09543 (CN37_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	421 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. 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 component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
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 electronic annotation. Source: Compara axonogenesis Inferred from electronic annotation. Source: Compara cyclic nucleotide catabolic process Inferred from electronic annotation. Source: InterPro forebrain development Inferred from electronic annotation. Source: Compara microtubule cytoskeleton organization Inferred from electronic annotation. Source: Compara regulation of mitochondrial membrane permeability Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to toxic substance Inferred from electronic annotation. Source: Compara synaptic transmission Traceable author statement PubMed 1322358. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay PubMed 12379507. Source: BHF-UCL extracellular space Inferred from direct assay PubMed 12379507. Source: BHF-UCL melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from direct assay PubMed 21525035. Source: UniProtKB microvillus Inferred from electronic annotation. Source: Compara mitochondrial inner membrane Inferred from electronic annotation. Source: Compara mitochondrial outer membrane Inferred from electronic annotation. Source: Compara myelin sheath abaxonal region Inferred from electronic annotation. Source: Compara myelin sheath adaxonal region Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara pseudopodium Inferred from electronic annotation. Source: Compara
Molecular_function	2',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: Compara
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 418

418

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

PRO_0000089961

Propeptide

419 – 421

3

Removed in mature form By similarity

PRO_0000422296

Sites

Active site

251

1

Proton acceptor

Active site

330

1

Proton donor

Binding site

253

1

Substrate

Binding site

332

1

Substrate

Amino acid modifications

Modified residue

110

1

Phosphotyrosine By similarity

Modified residue

373

1

Phosphotyrosine By similarity

Modified residue

418

1

Cysteine methyl ester By similarity

Lipidation

418

1

S-farnesyl cysteine By similarity

Natural variations

Alternative sequence

1 – 20

20

Missing in isoform CNPI.

VSP_004171

Natural variant

207

1

Q → R.
Corresponds to variant rs34353668 [ dbSNP | Ensembl ].

VAR_033746

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

421

Helix Strand Turn

Details...

Beta strand

188 – 194

7

Helix

196 – 215

20

Helix

217 – 221

5

Helix

223 – 226

4

Helix

238 – 241

4

Beta strand

251 – 256

6

Helix

258 – 260

3

Helix

265 – 270

6

Helix

272 – 277

6

Beta strand

281 – 291

11

Beta strand

293 – 301

9

Helix

306 – 309

4

Turn

325 – 328

4

Beta strand

330 – 335

6

Helix

343 – 356

14

Beta strand

362 – 367

6

Beta strand

370 – 376

7

Beta strand

379 – 397

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform CNPII (DNAII) [UniParc]. Last modified October 1, 1996. Version 2. Checksum: CA6D0097DFD87255	FASTA	421	47,579
	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
	Isoform CNPI (DNAI) [UniParc]. Checksum: 81F0E080822D3B0D	FASTA	401	45,099
	10 20 30 40 50 60 MSSSGAKDKP ELQFPFLQDE DTVATLLECK TLFILRGLPG SGKSTLARVI VDKYRDGTKM 70 80 90 100 110 120 VSADAYKITP GARGAFSEEY KRLDEDLAAY CRRRDIRILV LDDTNHERER LEQLFEMADQ 130 140 150 160 170 180 YQYQVVLVEP KTAWRLDCAQ LKEKNQWQLS ADDLKKLKPG LEKDFLPLYF GWFLTKKSSE 190 200 210 220 230 240 TLRKAGQVFL EELGNHKAFK KELRQFVPGD EPREKMDLVT YFGKRPPGVL HCTTKFCDYG 250 260 270 280 290 300 KAPGAEEYAQ QDVLKKSYSK AFTLTISALF VTPKTTGARV ELSEQQLQLW PSDVDKLSPT 310 320 330 340 350 360 DNLPRGSRAH ITLGCAADVE AVQTGLDLLE ILRQEKGGSR GEEVGELSRG KLYSLGNGRW 370 380 390 400 MLTLAKNMEV RAIFTGYYGK GKPVPTQGSR KGGALQSCTI I

References

	« Hide 'large scale' referencesShow '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. , 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], MASS SPECTROMETRY. 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], MASS SPECTROMETRY. Tissue: Melanoma.
[10]	"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].
[11]	"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 , 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 , 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.

IPI

IPI00220993.
IPI00306667.

PIR

JC1517.

RefSeq

NP_149124.3. NM_033133.4.

UniGene

Hs.273621.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WOJ	X-ray	1.80	A	186-399	[»]

ProteinModelPortal

P09543.

ModBase

Search...

Protein-protein interaction databases

IntAct

P09543. 4 interactions.

MINT

MINT-4999529.

STRING

9606.ENSP00000377470.

PTM databases

PhosphoSite

P09543.

Polymorphism databases

DMDM

1705945.

2D gel databases

UCD-2DPAGE

P09543.

Proteomic databases

PaxDb

P09543.

PRIDE

P09543.

Protocols and materials databases

DNASU

1267.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000393888; ENSP00000377466; ENSG00000173786.
ENST00000393892; ENSP00000377470; ENSG00000173786.
ENST00000562963; ENSP00000457200; ENSG00000260283.
ENST00000563912; ENSP00000454542; ENSG00000260283.

GeneID

1267.

KEGG

hsa:1267.

UCSC

uc002hyl.1. human.

Organism-specific databases

CTD

1267.

GeneCards

GC17P040118.

HGNC

HGNC:2158. CNP.

HPA

CAB002672.
HPA023266.
HPA023278.
HPA023280.
HPA023338.

MIM

123830. gene.

neXtProt

NX_P09543.

PharmGKB

PA26680.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG314041.

HOGENOM

HOG000111838.

HOVERGEN

HBG001451.

InParanoid

P09543.

KO

K01121.

OMA

LWPNDVD.

OrthoDB

EOG4D52ZC.

Gene expression databases

ArrayExpress

P09543.

Bgee

P09543.

CleanEx

HS_CNP.

Genevestigator

P09543.

GermOnline

ENSG00000173786. Homo sapiens.

Family and domain databases

InterPro

IPR008431. CNPase.
IPR027417. P-loop_NTPase.
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.
SSF52540. SSF52540. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

CNP. human.

EvolutionaryTrace

P09543.

GenomeRNAi

1267.

NextBio

5129.

SOURCE

Search...

Entry information

Entry name

CN37_HUMAN

Accession

Primary (citable) accession number: P09543

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.