NUD14_MOUSE
ID NUD14_MOUSE Reviewed; 222 AA.
AC Q9D142; Q9CSD2;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Uridine diphosphate glucose pyrophosphatase NUDT14;
DE Short=UDPG pyrophosphatase;
DE Short=UGPPase;
DE EC=3.6.1.45;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 14;
DE Short=Nudix motif 14;
GN Name=Nudt14;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and
CC ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate
CC is probably UDP-glucose. Poor activity on other substrates such as ADP-
CC glucose, CDP-glucose, GDP-glucose and GDP-mannose (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.;
CC EC=3.6.1.45;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AK003991; BAB23110.1; -; mRNA.
DR EMBL; AK013174; BAB28691.2; -; mRNA.
DR EMBL; BC025444; AAH25444.1; -; mRNA.
DR CCDS; CCDS26201.1; -.
DR RefSeq; NP_001303653.1; NM_001316724.1.
DR RefSeq; NP_079675.1; NM_025399.4.
DR AlphaFoldDB; Q9D142; -.
DR SMR; Q9D142; -.
DR BioGRID; 211271; 4.
DR STRING; 10090.ENSMUSP00000002881; -.
DR iPTMnet; Q9D142; -.
DR PhosphoSitePlus; Q9D142; -.
DR EPD; Q9D142; -.
DR MaxQB; Q9D142; -.
DR PaxDb; Q9D142; -.
DR PeptideAtlas; Q9D142; -.
DR PRIDE; Q9D142; -.
DR ProteomicsDB; 291923; -.
DR Antibodypedia; 49103; 73 antibodies from 17 providers.
DR DNASU; 66174; -.
DR Ensembl; ENSMUST00000221397; ENSMUSP00000152599; ENSMUSG00000002804.
DR GeneID; 66174; -.
DR KEGG; mmu:66174; -.
DR UCSC; uc007pfm.1; mouse.
DR CTD; 256281; -.
DR MGI; MGI:1913424; Nudt14.
DR VEuPathDB; HostDB:ENSMUSG00000002804; -.
DR eggNOG; KOG4432; Eukaryota.
DR GeneTree; ENSGT00940000154045; -.
DR HOGENOM; CLU_062658_1_0_1; -.
DR InParanoid; Q9D142; -.
DR OMA; YTYELCA; -.
DR OrthoDB; 1164318at2759; -.
DR PhylomeDB; Q9D142; -.
DR TreeFam; TF313661; -.
DR BRENDA; 3.6.1.45; 3474.
DR Reactome; R-MMU-480985; Synthesis of dolichyl-phosphate-glucose.
DR BioGRID-ORCS; 66174; 6 hits in 71 CRISPR screens.
DR PRO; PR:Q9D142; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9D142; protein.
DR Bgee; ENSMUSG00000002804; Expressed in lip and 204 other tissues.
DR ExpressionAtlas; Q9D142; baseline and differential.
DR Genevisible; Q9D142; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IDA:MGI.
DR GO; GO:0006753; P:nucleoside phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0019693; P:ribose phosphate metabolic process; IBA:GO_Central.
DR InterPro; IPR004385; NDP_pyrophosphatase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR TIGRFAMs; TIGR00052; TIGR00052; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..222
FT /note="Uridine diphosphate glucose pyrophosphatase NUDT14"
FT /id="PRO_0000057114"
FT DOMAIN 38..206
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 111..129
FT /note="Nudix box"
FT CONFLICT 192
FT /note="F -> I (in Ref. 1; BAB28691)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 24444 MW; D95555CDABBBC5D9 CRC64;
MERIDGVAVG LCAHSPYLRP FTLHYRQDGV QKSWDFMKTH DSVTILMFNS SRRSLVLVKQ
FRPAVYAGEV ERHFPGSLTA VNQDQPQELQ QALPGSAGVM VELCAGIVDQ PGLSLEEAAC
KEAWEECGYR LVPTDLRRVA TYMSGVGLTS SRQTMFYAEV TDAQRGGPGG GLAEEGELIE
VIHLNLDDAQ AFADNPDIPK TLGVIYAISW FFSQVVPHLS LQ
