P16330 (CN37_MOUSE) 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
Synonyms:	Cnp1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Ref.9
Catalytic activity	Nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate.
Subunit structure	Exists as monomers and homodimers. Ref.9
Subcellular location	Membrane; Lipid-anchor. Melanosome By similarity. Note: Firmly bound to membrane structures of brain white matter. Ref.7
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
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 mutant phenotype PubMed 12590258. Source: MGI aging Inferred from electronic annotation. Source: Compara axonogenesis Inferred from mutant phenotype PubMed 12590258. Source: MGI 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 toxin Inferred from direct assay PubMed 20578039. Source: MGI
Cellular_component	extracellular space Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay PubMed 12590258. Source: MGI microtubule Inferred from electronic annotation. Source: Compara 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 Inferred from direct assay PubMed 12590258. Source: MGI 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: P16330-1)

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: P16330-2)

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 – 417

417

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

PRO_0000089962

Propeptide

418 – 420

3

Removed in mature form Probable

PRO_0000422297

Sites

Active site

250

1

Proton acceptor Ref.9

Active site

329

1

Proton donor Ref.9

Binding site

252

1

Substrate

Binding site

331

1

Substrate

Amino acid modifications

Modified residue

110

1

Phosphotyrosine Ref.8

Modified residue

372

1

Phosphotyrosine Ref.8

Modified residue

417

1

Cysteine methyl ester Probable

Lipidation

417

1

S-farnesyl cysteine Probable

Natural variations

Alternative sequence

1 – 20

20

Missing in isoform CNPI.

VSP_004172

Experimental info

Sequence conflict

115

1

I → M in BAA07621. Ref.1

Sequence conflict

115

1

I → M in BAA07622. Ref.1

Sequence conflict

136

1

M → L in BAA07621. Ref.1

Sequence conflict

136

1

M → L in BAA07622. Ref.1

Secondary structure

1

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420

Helix Strand Turn

Details...

Beta strand

187 – 193

7

Helix

195 – 214

20

Helix

216 – 220

5

Helix

222 – 225

4

Helix

237 – 240

4

Beta strand

246 – 248

3

Beta strand

250 – 255

6

Helix

257 – 259

3

Helix

264 – 268

5

Helix

271 – 276

6

Beta strand

280 – 290

11

Beta strand

292 – 300

9

Helix

303 – 306

4

Helix

317 – 319

3

Turn

324 – 327

4

Beta strand

329 – 334

6

Helix

342 – 355

14

Beta strand

364 – 366

3

Beta strand

369 – 375

7

Beta strand

378 – 396

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform CNPII (DNAII) [UniParc]. Last modified August 16, 2004. Version 3. Checksum: 2FAFFDE5F0E99EAB	FASTA	420	47,123
	10 20 30 40 50 60 MNTSFTRKSH TFLPKLFFRK MSSSGAKEKP ELQFPFLQDE DTVATLHECK TLFILRGLPG 70 80 90 100 110 120 SGKSTLARLI LEKYHDGTKM VSADAYKIIP GSRADFSEAY KRLDEDLAGY CRRDIRVLVL 130 140 150 160 170 180 DDTNHERERL DQLFEMADQY QYQVVLVEPK TAWRLDCAQL KEKNQWQLSA DDLKKLKPGL 190 200 210 220 230 240 EKDFLPLYFG WFLTKKSSET LRKAGQVFLE ELGNHKAFKK ELRHFISGDE PKEKLELVSY 250 260 270 280 290 300 FGKRPPGVLH CTTKFCDYGK AAGAEEYAQQ EVVKRSYGKA FKLSISALFV TPKTAGAQVV 310 320 330 340 350 360 LTDQELQLWP SDLDKPSASE GLPPGSRAHV TLGCAADVQP VQTGLDLLDI LQQVKGGSQG 370 380 390 400 410 420 EAVGELPRGK LYSLGKGRWM LSLTKKMEVK AIFTGYYGKG KPVPIHGSRK GGAMQICTII
	Isoform CNPI (DNAI) [UniParc]. Checksum: B974404499DE29BE	FASTA	400	44,654
	10 20 30 40 50 60 MSSSGAKEKP ELQFPFLQDE DTVATLHECK TLFILRGLPG SGKSTLARLI LEKYHDGTKM 70 80 90 100 110 120 VSADAYKIIP GSRADFSEAY KRLDEDLAGY CRRDIRVLVL DDTNHERERL DQLFEMADQY 130 140 150 160 170 180 QYQVVLVEPK TAWRLDCAQL KEKNQWQLSA DDLKKLKPGL EKDFLPLYFG WFLTKKSSET 190 200 210 220 230 240 LRKAGQVFLE ELGNHKAFKK ELRHFISGDE PKEKLELVSY FGKRPPGVLH CTTKFCDYGK 250 260 270 280 290 300 AAGAEEYAQQ EVVKRSYGKA FKLSISALFV TPKTAGAQVV LTDQELQLWP SDLDKPSASE 310 320 330 340 350 360 GLPPGSRAHV TLGCAADVQP VQTGLDLLDI LQQVKGGSQG EAVGELPRGK LYSLGKGRWM 370 380 390 400 LSLTKKMEVK AIFTGYYGKG KPVPIHGSRK GGAMQICTII

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of mouse 2',3'-cyclic-nucleotide 3'-phosphodiesterase gene." Monoh K., Kurihara T., Sakimura K., Takahashi Y. Biochem. Biophys. Res. Commun. 165:1213-1220(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CNPI). Strain: DBA.
[2]	"Alternative splicing of mouse brain 2',3'-cyclic-nucleotide 3'-phosphodiesterase mRNA." Kurihara T., Monoh K., Sakimura K., Takahashi Y. Biochem. Biophys. Res. Commun. 170:1074-1081(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS CNPI AND CNPII). Strain: DBA. Tissue: Brain.
[3]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M. Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CNPI). Strain: ILS and ISS.
[4]	"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] (ISOFORM CNPII). Strain: FVB/N. Tissue: Mammary tumor.
[5]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-418 (ISOFORM CNPII). Strain: C57BL/6J. Tissue: Thymus.
[6]	Lubec G., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 94-101; 103-112; 117-127; 130-150; 164-174; 183-195; 203-216; 235-243; 261-274; 276-293; 356-368; 379-385 AND 391-399. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[7]	"Structures and micelle locations of the nonlipidated and lipidated C-terminal membrane anchor of 2',3'-cyclic nucleotide-3'-phosphodiesterase." Esposito C., Scrima M., Carotenuto A., Tedeschi A., Rovero P., D'Errico G., Malfitano A.M., Bifulco M., D'Ursi A.M. Biochemistry 47:308-319(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ISOPRENYLATION, SUBCELLULAR LOCATION.
[8]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110 AND TYR-372, MASS SPECTROMETRY. Tissue: Brain.
[9]	"Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: active-site ligand binding and molecular conformation." Myllykoski M., Raasakka A., Han H., Kursula P. PLoS ONE 7:E32336-E32336(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 179-398, ACTIVE SITE, SUBSTRATE-BINDING SITES, RNA-BINDING, FUNCTION, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D38642 Genomic DNA. Translation: BAA07621.1.
D38642 Genomic DNA. Translation: BAA07622.1.
M31810 mRNA. Translation: AAA37429.1.
M58045 mRNA. Translation: AAA37430.1.
M58047, M58046 Genomic DNA. Translation: AAA37431.1.
AF332055 mRNA. Translation: AAK56084.1.
AF332056 mRNA. Translation: AAK56085.1.
BC005544 mRNA. Translation: AAH05544.1.
BC021904 mRNA. Translation: AAH21904.1.
AK050628 mRNA. Translation: BAC34351.1.

IPI

IPI00229598.
IPI00319602.

PIR

ESMS32. A35708.

RefSeq

NP_001139790.1. NM_001146318.1.
NP_034053.2. NM_009923.2.

UniGene

Mm.15711.
Mm.453219.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XMI	X-ray	1.74	A	179-398	[»]
2Y1P	X-ray	1.82	A	179-398	[»]
2Y3X	X-ray	2.10	A/B/E	179-398	[»]
2YDB	X-ray	2.15	A	179-398	[»]
2YDC	X-ray	2.05	A	179-398	[»]
2YDD	X-ray	2.40	A	179-398	[»]

ProteinModelPortal

P16330.

SMR

P16330. Positions 48-398.

ModBase

Search...

Protein-protein interaction databases

IntAct

P16330. 8 interactions.

MINT

MINT-1955077.

PTM databases

PhosphoSite

P16330.

Proteomic databases

PaxDb

P16330.

PRIDE

P16330.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000103120; ENSMUSP00000099409; ENSMUSG00000006782.

GeneID

12799.

KEGG

mmu:12799.

Organism-specific databases

CTD

1267.

MGI

MGI:88437. Cnp.

Phylogenomic databases

eggNOG

NOG314041.

HOGENOM

HOG000111838.

HOVERGEN

HBG001451.

InParanoid

P16330.

KO

K01121.

OMA

LWPNDVD.

OrthoDB

EOG4D52ZC.

Gene expression databases

ArrayExpress

P16330.

Bgee

P16330.

CleanEx

MM_CNP.

Genevestigator

P16330.

GermOnline

ENSMUSG00000006782. Mus musculus.

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

ChiTaRS

CNP. mouse.

NextBio

282222.

SOURCE

Search...

Entry information

Entry name

CN37_MOUSE

Accession

Primary (citable) accession number: P16330
Secondary accession number(s): Q61424 , Q8C7C9, Q91V42, Q923F3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program