ID NUD14_HUMAN Reviewed; 222 AA. AC O95848; Q86SJ8; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2004, sequence version 2. DT 14-OCT-2015, entry version 119. DE RecName: Full=Uridine diphosphate glucose pyrophosphatase; 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; Synonyms=UGPP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10662552; DOI=10.1006/geno.1999.6045; RA Deng Y., Madan A., Banta A.B., Friedman C., Trask B.J., Hood L., RA Li L.; RT "Characterization, chromosomal localization, and the complete 30-kb RT DNA sequence of the human Jagged2 (JAG2) gene."; RL Genomics 63:133-138(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, RP AND SUBUNIT. RC TISSUE=Thyroid; RX PubMed=12429023; DOI=10.1042/BJ20021140; RA Yagi T., Baroja-Fernandez E., Yamamoto R., Munoz F.J., Akazawa T., RA Hong K.S., Pozueta-Romero J.; RT "Cloning, expression and characterization of a mammalian Nudix RT hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP- RT glucose."; RL Biochem. J. 370:409-415(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., RA Quetier F., Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 28-222. RG Structural genomics consortium (SGC); RT "Crystal structure of human uridine diphosphate glucose RT pyrophosphatase (NUDT14)."; RL Submitted (FEB-2011) to the PDB data bank. CC -!- FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP CC and ADP-ribose to ribose 5-phosphate and AMP. The physiological CC substrate is probably UDP-glucose. Poor activity on other CC substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP- CC mannose. CC -!- CATALYTIC ACTIVITY: UDP-sugar + H(2)O = UMP + alpha-D-aldose 1- CC phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.0-9.5.; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12429023}. CC -!- INTERACTION: CC P10398:ARAF; NbExp=3; IntAct=EBI-536866, EBI-365961; CC Q8TBB1:LNX1; NbExp=5; IntAct=EBI-536866, EBI-739832; CC Q9GZT8:NIF3L1; NbExp=3; IntAct=EBI-536866, EBI-740897; CC Q04864:REL; NbExp=3; IntAct=EBI-536866, EBI-307352; CC Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-536866, EBI-741158; CC Q8TBK6:ZCCHC10; NbExp=3; IntAct=EBI-536866, EBI-597063; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12429023}. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00794}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD15563.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF111170; AAD15563.1; ALT_INIT; Genomic_DNA. DR EMBL; AB087802; BAC65455.1; -; mRNA. DR EMBL; AL512355; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC041584; AAH41584.1; -; mRNA. DR CCDS; CCDS10000.1; -. DR RefSeq; NP_803877.2; NM_177533.4. DR UniGene; Hs.526432; -. DR PDB; 3Q91; X-ray; 2.70 A; A/B/C/D=28-222. DR PDBsum; 3Q91; -. DR ProteinModelPortal; O95848; -. DR SMR; O95848; 39-220. DR BioGrid; 129152; 8. DR IntAct; O95848; 7. DR STRING; 9606.ENSP00000376349; -. DR PhosphoSite; O95848; -. DR BioMuta; NUDT14; -. DR MaxQB; O95848; -. DR PaxDb; O95848; -. DR PRIDE; O95848; -. DR DNASU; 256281; -. DR Ensembl; ENST00000392568; ENSP00000376349; ENSG00000183828. DR GeneID; 256281; -. DR KEGG; hsa:256281; -. DR UCSC; uc010tyn.3; human. DR CTD; 256281; -. DR GeneCards; NUDT14; -. DR HGNC; HGNC:20141; NUDT14. DR HPA; HPA046755; -. DR MIM; 609219; gene. DR neXtProt; NX_O95848; -. DR PharmGKB; PA134971372; -. DR eggNOG; COG0494; -. DR GeneTree; ENSGT00410000025889; -. DR HOGENOM; HOG000102292; -. DR HOVERGEN; HBG052689; -. DR InParanoid; O95848; -. DR KO; K08077; -. DR OMA; YTYELCA; -. DR OrthoDB; EOG7JHM6K; -. DR PhylomeDB; O95848; -. DR TreeFam; TF313661; -. DR BRENDA; 3.6.1.45; 2681. DR EvolutionaryTrace; O95848; -. DR GenomeRNAi; 256281; -. DR NextBio; 92764; -. DR PRO; PR:O95848; -. DR Proteomes; UP000005640; Chromosome 14. DR Bgee; O95848; -. DR CleanEx; HS_NUDT14; -. DR ExpressionAtlas; O95848; baseline and differential. DR Genevisible; O95848; HS. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IEA:UniProtKB-EC. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR004385; NDP_pyrophosphatase. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. 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 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Magnesium; KW Reference proteome. FT CHAIN 1 222 Uridine diphosphate glucose FT pyrophosphatase. FT /FTId=PRO_0000057113. FT DOMAIN 38 206 Nudix hydrolase. {ECO:0000255|PROSITE- FT ProRule:PRU00794}. FT MOTIF 111 129 Nudix box. FT STRAND 42 49 {ECO:0000244|PDB:3Q91}. FT HELIX 50 52 {ECO:0000244|PDB:3Q91}. FT STRAND 54 61 {ECO:0000244|PDB:3Q91}. FT HELIX 63 69 {ECO:0000244|PDB:3Q91}. FT STRAND 99 102 {ECO:0000244|PDB:3Q91}. FT STRAND 104 107 {ECO:0000244|PDB:3Q91}. FT STRAND 110 112 {ECO:0000244|PDB:3Q91}. FT HELIX 115 127 {ECO:0000244|PDB:3Q91}. FT HELIX 133 135 {ECO:0000244|PDB:3Q91}. FT STRAND 137 144 {ECO:0000244|PDB:3Q91}. FT STRAND 151 160 {ECO:0000244|PDB:3Q91}. FT HELIX 162 164 {ECO:0000244|PDB:3Q91}. FT STRAND 179 185 {ECO:0000244|PDB:3Q91}. FT HELIX 186 188 {ECO:0000244|PDB:3Q91}. FT HELIX 189 194 {ECO:0000244|PDB:3Q91}. FT HELIX 202 214 {ECO:0000244|PDB:3Q91}. FT HELIX 216 218 {ECO:0000244|PDB:3Q91}. SQ SEQUENCE 222 AA; 24118 MW; FB1DFA40A67E72B6 CRC64; MERIEGASVG RCAASPYLRP LTLHYRQNGA QKSWDFMKTH DSVTVLLFNS SRRSLVLVKQ FRPAVYAGEV ERRFPGSLAA VDQDGPRELQ PALPGSAGVT VELCAGLVDQ PGLSLEEVAC KEAWEECGYH LAPSDLRRVA TYWSGVGLTG SRQTMFYTEV TDAQRSGPGG GLVEEGELIE VVHLPLEGAQ AFADDPDIPK TLGVIFGVSW FLSQVAPNLD LQ //