UDA1_CAEEL
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 03-AUG-2022, entry version 126.
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 Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC 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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300, AND IDENTIFICATION BY 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 to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP 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 IDENTIFICATION BY 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 involved
CC in glycoproteins folding and quality control in the endoplasmic
CC reticulum. {ECO:0000269|PubMed:15102851}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15102851};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15102851};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15102851};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=180 uM for UDP {ECO:0000269|PubMed:15102851};
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 {ECO:0000269|PubMed:15102851};
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000305|PubMed:15102851}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:15102851}.
CC -!- INDUCTION: By stress such as high temperature or ethanol.
CC {ECO:0000269|PubMed:15102851}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; Z83113; CAB05544.1; -; Genomic_DNA.
DR PIR; T23508; T23508.
DR RefSeq; NP_505573.1; NM_073172.3.
DR AlphaFoldDB; Q9XU84; -.
DR SMR; Q9XU84; -.
DR BioGRID; 44428; 3.
DR STRING; 6239.K08H10.4; -.
DR iPTMnet; Q9XU84; -.
DR EPD; Q9XU84; -.
DR PaxDb; Q9XU84; -.
DR PeptideAtlas; Q9XU84; -.
DR EnsemblMetazoa; K08H10.4.1; K08H10.4.1; WBGene00010697.
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; KOG1385; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_0_2_1; -.
DR InParanoid; Q9XU84; -.
DR OMA; DKPIVQY; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q9XU84; -.
DR Reactome; R-CEL-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR PRO; PR:Q9XU84; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010697; Expressed in adult organism and 4 other tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:WormBase.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IDA:WormBase.
DR GO; GO:0046710; P:GDP metabolic process; IDA:WormBase.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
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.
PE 1: Evidence at protein level;
KW Calcium; Glycoprotein; Hydrolase; Magnesium; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..479
FT /note="Nucleoside-diphosphatase uda-1"
FT /id="PRO_0000248568"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..479
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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
