NUD22_MOUSE
ID NUD22_MOUSE Reviewed; 308 AA.
AC Q9DD16; Q8VCI4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Uridine diphosphate glucose pyrophosphatase NUDT22;
DE Short=UDPG pyrophosphatase;
DE Short=UGPPase;
DE EC=3.6.1.45;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 22;
DE Short=Nudix motif 22;
GN Name=Nudt22;
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=Kidney;
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].
RC STRAIN=FVB/N; TISSUE=Liver;
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).
CC -!- FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and
CC UDP-galactose to galactose 1-phosphate and UMP. Preferred substrate is
CC UDP-glucose. {ECO:0000250|UniProtKB:Q9BRQ3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.;
CC EC=3.6.1.45; Evidence={ECO:0000250|UniProtKB:Q9BRQ3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9BRQ3};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AK002252; BAB21966.1; -; mRNA.
DR EMBL; BC019768; AAH19768.1; -; mRNA.
DR CCDS; CCDS29517.1; -.
DR RefSeq; NP_080951.1; NM_026675.2.
DR AlphaFoldDB; Q9DD16; -.
DR SMR; Q9DD16; -.
DR STRING; 10090.ENSMUSP00000041419; -.
DR iPTMnet; Q9DD16; -.
DR PhosphoSitePlus; Q9DD16; -.
DR EPD; Q9DD16; -.
DR MaxQB; Q9DD16; -.
DR PaxDb; Q9DD16; -.
DR PRIDE; Q9DD16; -.
DR ProteomicsDB; 293780; -.
DR Antibodypedia; 51889; 91 antibodies from 18 providers.
DR DNASU; 68323; -.
DR Ensembl; ENSMUST00000041686; ENSMUSP00000041419; ENSMUSG00000037349.
DR Ensembl; ENSMUST00000180765; ENSMUSP00000137738; ENSMUSG00000037349.
DR GeneID; 68323; -.
DR KEGG; mmu:68323; -.
DR UCSC; uc008gjz.1; mouse.
DR CTD; 84304; -.
DR MGI; MGI:1915573; Nudt22.
DR VEuPathDB; HostDB:ENSMUSG00000037349; -.
DR eggNOG; ENOG502QRSW; Eukaryota.
DR GeneTree; ENSGT00390000017869; -.
DR HOGENOM; CLU_061819_1_0_1; -.
DR InParanoid; Q9DD16; -.
DR OMA; PEPQAVC; -.
DR OrthoDB; 1587403at2759; -.
DR PhylomeDB; Q9DD16; -.
DR TreeFam; TF106357; -.
DR BioGRID-ORCS; 68323; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9DD16; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9DD16; protein.
DR Bgee; ENSMUSG00000037349; Expressed in lacrimal gland and 202 other tissues.
DR Genevisible; Q9DD16; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0052751; F:GDP-mannose hydrolase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; ISS:UniProtKB.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PROSITE; PS51462; NUDIX; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..308
FT /note="Uridine diphosphate glucose pyrophosphatase NUDT22"
FT /id="PRO_0000263732"
FT DOMAIN 117..284
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 174..195
FT /note="Nudix box"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ3"
FT CONFLICT 175
FT /note="L -> E (in Ref. 2; AAH19768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 33376 MW; 58BB1DB6FE4EADDA CRC64;
MDPEVSLLLL CPLGGLSQEQ VAVELSPAHD RRPLPGGDKA ITAIWETRQQ AQPWIFDAPK
FRLHSATLVS SSPEPQLLLH LGLTSYRDFL GTNWSSSASW LRQQGAADWG DKQAYLADPL
GVGAALVTAD DFLVFLRRSQ QVAEAPGLVD VPGGHPEPQA LCSGGIPRHK DLPGLLVVRE
LFSSVLQEIC DEVNLPLHTL SQPLLLGIAC NETSAGRASA EFYVQCSLTS EEVRSYYLSG
GPEAHESTGI IFVETQRVQR LQETEMWAQL CPSAKGAILL YNRHPPLQSG VGKSHLSHPS
APALSLQL
