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Q9D142 (NUD14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

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

Names and origin

Protein namesRecommended name:
Uridine diphosphate glucose pyrophosphatase

Short name=UDPG pyrophosphatase
Short name=UGPPase
EC=3.6.1.45
Alternative name(s):
Nucleoside diphosphate-linked moiety X motif 14
Short name=Nudix motif 14
Gene names
Name:Nudt14
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate is probably UDP-glucose. Poor activity on other substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP-mannose By similarity.

Catalytic activity

UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.

Cofactor

Magnesium By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the Nudix hydrolase family.

Contains 1 nudix hydrolase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmetabolic process

Inferred from direct assay PubMed 19896456. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionADP-ribose diphosphatase activity

Inferred from direct assay PubMed 19896456. Source: MGI

UDP-sugar diphosphatase activity

Inferred from direct assay PubMed 19896456. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 222222Uridine diphosphate glucose pyrophosphatase
PRO_0000057114

Regions

Domain38 – 206169Nudix hydrolase
Motif111 – 12919Nudix box

Experimental info

Sequence conflict1921F → I in BAB28691. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D142 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D95555CDABBBC5D9

FASTA22224,444
        10         20         30         40         50         60 
MERIDGVAVG LCAHSPYLRP FTLHYRQDGV QKSWDFMKTH DSVTILMFNS SRRSLVLVKQ 

        70         80         90        100        110        120 
FRPAVYAGEV ERHFPGSLTA VNQDQPQELQ QALPGSAGVM VELCAGIVDQ PGLSLEEAAC 

       130        140        150        160        170        180 
KEAWEECGYR LVPTDLRRVA TYMSGVGLTS SRQTMFYAEV TDAQRGGPGG GLAEEGELIE 

       190        200        210        220 
VIHLNLDDAQ AFADNPDIPK TLGVIYAISW FFSQVVPHLS LQ 

« Hide

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]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003991 mRNA. Translation: BAB23110.1.
AK013174 mRNA. Translation: BAB28691.2.
BC025444 mRNA. Translation: AAH25444.1.
CCDSCCDS26201.1.
RefSeqNP_079675.1. NM_025399.3.
UniGeneMm.7070.

3D structure databases

ProteinModelPortalQ9D142.
SMRQ9D142. Positions 39-219.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9D142.

Proteomic databases

PaxDbQ9D142.
PRIDEQ9D142.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002881; ENSMUSP00000002881; ENSMUSG00000002804.
GeneID66174.
KEGGmmu:66174.
UCSCuc007pfm.1. mouse.

Organism-specific databases

CTD256281.
MGIMGI:1913424. Nudt14.

Phylogenomic databases

eggNOGCOG0494.
GeneTreeENSGT00410000025889.
HOGENOMHOG000102292.
HOVERGENHBG052689.
InParanoidQ9D142.
KOK08077.
OMAIYARHFH.
OrthoDBEOG7JHM6K.
PhylomeDBQ9D142.
TreeFamTF313661.

Gene expression databases

BgeeQ9D142.
GenevestigatorQ9D142.

Family and domain databases

Gene3D3.90.79.10. 1 hit.
InterProIPR004385. NDP_pyrophosphatase.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMSSF55811. SSF55811. 1 hit.
TIGRFAMsTIGR00052. TIGR00052. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio320858.
PROQ9D142.
SOURCESearch...

Entry information

Entry nameNUD14_MOUSE
AccessionPrimary (citable) accession number: Q9D142
Secondary accession number(s): Q9CSD2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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