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   07-JUL-2009, entry version 59.
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   MEDLINE=20130121; 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   MEDLINE=22478821; 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   MEDLINE=22459283; 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).
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: Magnesium.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0-9.5;
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       P10398:ARAF; NbExp=3; IntAct=EBI-536866, EBI-365961;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family.
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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   IPI; IPI00412878; -.
DR   RefSeq; NP_803877.2; -.
DR   UniGene; Hs.526432; -.
DR   IntAct; O95848; 2.
DR   PRIDE; O95848; -.
DR   Ensembl; ENSG00000183828; Homo sapiens.
DR   GeneID; 256281; -.
DR   KEGG; hsa:256281; -.
DR   NMPDR; fig|9606.3.peg.10277; -.
DR   UCSC; uc001yqj.1; human.
DR   GeneCards; GC14M104710; -.
DR   H-InvDB; HIX0026628; -.
DR   HGNC; HGNC:20141; NUDT14.
DR   MIM; 609219; gene.
DR   PharmGKB; PA134971372; -.
DR   HOGENOM; O95848; -.
DR   HOVERGEN; O95848; -.
DR   OMA; O95848; YTYELCA.
DR   BRENDA; 3.6.1.45; 247.
DR   NextBio; 92764; -.
DR   ArrayExpress; O95848; -.
DR   Bgee; O95848; -.
DR   CleanEx; HS_NUDT14; -.
DR   GermOnline; ENSG00000183828; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008768; F:UDP-sugar diphosphatase activity; IEA:EC.
DR   InterPro; IPR004385; NDP_pyrophos.
DR   InterPro; IPR000086; NUDIX_hydrolase_core.
DR   Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   TIGRFAMs; TIGR00052; NDP_pyrophos; 1.
DR   PROSITE; PS00893; NUDIX; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Hydrolase; Magnesium.
FT   CHAIN         1    222       Uridine diphosphate glucose
FT                                pyrophosphatase.
FT                                /FTId=PRO_0000057113.
FT   MOTIF       111    129       Nudix box.
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
//