ID UDA1_CAEEL Reviewed; 479 AA.
AC Q9XU84;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 01-MAY-2013, entry version 77.
DE RecName: Full=Nucleoside-diphosphatase uda-1;
DE EC=3.6.1.6;
DE AltName: Full=Uridine-diphosphatase;
GN Name=uda-1; ORFNames=K08H10.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for
RT investigating biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300, AND MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry
RT to identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION BY STRESS.
RX PubMed=15102851; DOI=10.1074/jbc.M402624200;
RA Uccelletti D., O'Callaghan C., Berninsone P., Zemtseva I., Abeijon C.,
RA Hirschberg C.B.;
RT "ire-1-dependent transcriptional up-regulation of a lumenal uridine
RT diphosphatase from Caenorhabditis elegans.";
RL J. Biol. Chem. 279:27390-27398(2004).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300, AND MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Hydrolyzes UDP and GDP but not any other nucleoside di-,
CC mono- or triphosphates. May promote reglycosylation reactions
CC involved in glycoproteins folding and quality control in the
CC endoplasmic reticulum.
CC -!- CATALYTIC ACTIVITY: A nucleoside diphosphate + H(2)O = a
CC nucleoside phosphate + phosphate.
CC -!- COFACTOR: Calcium.
CC -!- COFACTOR: Magnesium.
CC -!- COFACTOR: Manganese.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=180 uM for UDP;
CC Note=In the presence of 10 mM calcium;
CC pH dependence:
CC Optimum pH is 8.0 for UDP and 7.5 for GDP;
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Single-pass type II
CC membrane protein (Probable).
CC -!- INDUCTION: By stress such as high temperature or ethanol.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
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DR EMBL; Z83113; CAB05544.1; -; Genomic_DNA.
DR PIR; T23508; T23508.
DR RefSeq; NP_505573.1; NM_073172.3.
DR ProteinModelPortal; Q9XU84; -.
DR SMR; Q9XU84; 43-434.
DR STRING; 6239.K08H10.4.1; -.
DR PaxDb; Q9XU84; -.
DR EnsemblMetazoa; K08H10.4; K08H10.4; K08H10.4.
DR GeneID; 179395; -.
DR KEGG; cel:CELE_K08H10.4; -.
DR UCSC; K08H10.4.1; c. elegans.
DR CTD; 179395; -.
DR WormBase; K08H10.4; CE18877; WBGene00010697; uda-1.
DR eggNOG; COG5371; -.
DR GeneTree; ENSGT00510000046675; -.
DR HOGENOM; HOG000154769; -.
DR InParanoid; Q9XU84; -.
DR KO; K01511; -.
DR OMA; INGSSSH; -.
DR NextBio; 905214; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:WormBase.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IDA:WormBase.
DR GO; GO:0046710; P:GDP metabolic process; IDA:WormBase.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR GO; GO:0046048; P:UDP metabolic process; IDA:WormBase.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; FALSE_NEG.
PE 1: Evidence at protein level;
KW Calcium; Complete proteome; Glycoprotein; Hydrolase; Magnesium;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1 479 Nucleoside-diphosphatase uda-1.
FT /FTId=PRO_0000248568.
FT TOPO_DOM 1 7 Cytoplasmic (Potential).
FT TRANSMEM 8 24 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 25 479 Lumenal (Potential).
FT ACT_SITE 171 171 Proton acceptor (By similarity).
FT CARBOHYD 300 300 N-linked (GlcNAc...).
FT CARBOHYD 452 452 N-linked (GlcNAc...) (Potential).
SQ SEQUENCE 479 AA; 53844 MW; 7EDC02A9D54A48ED CRC64;
MLFPAFSILL ISFFSLLSVV TTKTQYWCHG DGVLNNQHTC RFFTIVIDAG STGTRLHLYK
FIHDPAIASH GMPFKVEKEI FQEVKPGLSS FAKSPSSAAD SLEPLLQRAR KEVPHFMWEK
TPITLKATAG LRLLPGDMAD DILESVEERI FNSGFFAAFP DAVNVMPGSD EGVYSWFTLN
ILLETLFTDE PTVGHKPAAH RSVAAFDLGG GSTQLTYWPN NEAVFSEHVG YERDIDFFGH
HIRLFTHSFL GNGLIAARLN ILQLETDNEI ESTHQLITSC MPEGYQLTEW EYALKFWNIN
GSSSHSFESC YGTTKNFVES SEIMHLRELK GSPVYLFSYF FDRALNSGLV KGNEGGKIEL
RQFKEAAEIA CRREKTEIDD GSHWMPWQCL DLTYIYSLLR DGYQFEDNQP LVLAKKIKGM
EVSWGQGLAF ATANEFQLTE GAIKTALSSE PNSTVVDQIF DLVYSGTNQV LSYFNIISV
//
