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Q9CYC6 (DCP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
m7GpppN-mRNA hydrolase
EC=3.6.1.62
Alternative name(s):
mRNA-decapping enzyme 2
Gene names
Name:Dcp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking a RNA moiety. Ref.3

Catalytic activity

M7G5'ppp5'-mRNA + H2O = m7GDP + 5'-phospho-mRNA.

Cofactor

Manganese. Required for highest activity. Can also utilize magnesium ions By similarity.

Subunit structure

Found in a mRNA decay complex with LSM1, LSM3, LSM4, EXOSC2, EXOSC4, EXOSC10, PARN, XRN1, CNOT6, UPF1, UPF2 and UPF3B. Forms a complex with DCP1A, EDC3, DDX6 and EDC4/HEDLS, within this complex directly interacts with EDC4/HEDLS. Interacts with DPC1B, UPF1, UPF2 and UPF3B. Associates with polysomes. Interacts (via N-terminus and C-terminus) with TRIM21 (via N-terminus and C-terminus) By similarity. Interacts with LIMD1, WTIP and AJUBA By similarity. Interacts with DDX17 in an RNA-dependent manner By similarity. Interacts with ZC3HAV1 By similarity. Interacts with APOBEC3G in an RNA-dependent manner By similarity.

Subcellular location

Cytoplasm › P-body By similarity. Nucleus By similarity. Note: Predominantly cytoplasmic, in processing bodies (PB). A minor amount is nuclear By similarity.

Tissue specificity

Strongly expressed in brain and testis. Weakly expressed in lung. Not detected in heart, liver, kidney and muscle (at protein level). Ref.3

Developmental stage

Strongly expressed in brain, heart, liver at 14.5 and 16.5 dpc. Strongly expressed in brain at 20 dpc. Weakly expressed in heart and liver at 20 dpc (at protein level). Ref.3

Sequence similarities

Belongs to the Nudix hydrolase family. DCP2 subfamily.

Contains 1 nudix hydrolase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422m7GpppN-mRNA hydrolase
PRO_0000057052

Regions

Domain95 – 226132Nudix hydrolase
Motif129 – 15022Nudix box

Sites

Metal binding1441Manganese By similarity
Metal binding1481Manganese By similarity

Amino acid modifications

Modified residue2461Phosphoserine Ref.2
Modified residue2471Phosphoserine Ref.2
Modified residue2491Phosphoserine Ref.2
Modified residue2761Phosphoserine By similarity
Modified residue2841Phosphoserine By similarity

Experimental info

Sequence conflict2261F → Y in BAB30946. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CYC6 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 80FE791B05E4C8FD

FASTA42248,380
        10         20         30         40         50         60 
MEPKRLEIPG SVLDDLCSRF ILHIPSEERD NAIRVCFQIE LAHWFYLDFY MQNTPGLPQC 

        70         80         90        100        110        120 
GIRDFAKAVF SHCPFLLPQG EDVEKILDEW KEYKMGVPTY GAIILDETLE NVLLVQGYLA 

       130        140        150        160        170        180 
KSGWGFPKGK VNKEEAPHDC AAREVFEETG FDIKDYICKD DYIELRINDQ LARLYIIPGV 

       190        200        210        220        230        240 
PKDTKFNPKT RREIRNIEWF SIEKLPCHRN DMTPKSKLGL APNKFFMAIP FIRPLRDWLS 

       250        260        270        280        290        300 
RRFGDSSDSD NGFSSAGSTP ARPTVEKLSR TKFRHSQQLF PEGSPSDQWV KHRQPLQQKS 

       310        320        330        340        350        360 
HSNHGEVSDL LKAKNQNMRG NGRKQYQDSP NQKKRANGVH GQPAKQQNPL VKCEKKLHPR 

       370        380        390        400        410        420 
KLQDNFETDA TCDLPCSGEE PSVEHAEGHS VACNGHCKFP FSSRAFLSFK FDQNAIMKIL 


DL

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Embryo.
[2]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-247 AND SER-249, MASS SPECTROMETRY.
Tissue: Liver.
[3]"Multiple mRNA decapping enzymes in mammalian cells."
Song M.G., Li Y., Kiledjian M.
Mol. Cell 40:423-432(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A DECAPPING ENZYME, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK017809 mRNA. Translation: BAB30946.1.
AK166560 mRNA. Translation: BAE38853.1.
IPIIPI00111352.
RefSeqNP_081766.1. NM_027490.1.
UniGeneMm.87629.

3D structure databases

ProteinModelPortalQ9CYC6.
SMRQ9CYC6. Positions 12-242.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000025350.

PTM databases

PhosphoSiteQ9CYC6.

Proteomic databases

PaxDbQ9CYC6.
PRIDEQ9CYC6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025350; ENSMUSP00000025350; ENSMUSG00000024472.
GeneID70640.
KEGGmmu:70640.

Organism-specific databases

CTD167227.
MGIMGI:1917890. Dcp2.

Phylogenomic databases

eggNOGCOG0494.
GeneTreeENSGT00390000018878.
HOGENOMHOG000005974.
HOVERGENHBG051321.
InParanoidQ3TLD9.
KOK12613.
OMAPGVPKDT.
OrthoDBEOG43JC4S.

Gene expression databases

BgeeQ9CYC6.
CleanExMM_DCP2.
GenevestigatorQ9CYC6.
GermOnlineENSMUSG00000024472. Mus musculus.

Family and domain databases

Gene3D3.90.79.10. 1 hit.
InterProIPR007722. mRNA_decapping_BoxA.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamPF05026. DCP2. 1 hit.
PF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMSSF55811. NUDIX_hydrolase. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio332021.
SOURCESearch...

Entry information

Entry nameDCP2_MOUSE
AccessionPrimary (citable) accession number: Q9CYC6
Secondary accession number(s): Q3TLD9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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