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Apyrase apy-1 (EC 3.6.1.6) (Uridine-diphosphatase) (UDPase)

 APY1_CAEEL              Reviewed;         355 AA.
Q19202;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 2.
25-OCT-2017, entry version 117.
RecName: Full=Apyrase apy-1 {ECO:0000303|PubMed:18216284};
EC=3.6.1.6 {ECO:0000305|PubMed:18216284};
AltName: Full=Uridine-diphosphatase {ECO:0000303|PubMed:18216284};
Short=UDPase {ECO:0000303|PubMed:18216284};
Name=apy-1 {ECO:0000312|WormBase:F08C6.6};
ORFNames=F08C6.6 {ECO:0000312|WormBase:F08C6.6};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION BY ER
STRESS, AND DISRUPTION PHENOTYPE.
PubMed=18216284; DOI=10.1091/mbc.E07-06-0547;
Uccelletti D., Pascoli A., Farina F., Alberti A., Mancini P.,
Hirschberg C.B., Palleschi C.;
"APY-1, a novel Caenorhabditis elegans apyrase involved in unfolded
protein response signalling and stress responses.";
Mol. Biol. Cell 19:1337-1345(2008).
-!- FUNCTION: Hydrolyzes UDP and to a lesser extent GDP. By preventing
the accumulation of NDP, may promote the reglucosylation of
incompletely folded glycoproteins in the endoplasmic reticulum
following the unfolded protein response.
{ECO:0000269|PubMed:18216284}.
-!- CATALYTIC ACTIVITY: A nucleoside diphosphate + H(2)O = a
nucleoside phosphate + phosphate. {ECO:0000305|PubMed:18216284}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:Q8WVQ1};
-!- INTERACTION:
Q21746:sgt-1; NbExp=3; IntAct=EBI-319014, EBI-312019;
-!- SUBCELLULAR LOCATION: Endomembrane system
{ECO:0000303|PubMed:18216284}; Single-pass type II membrane
protein {ECO:0000305|PubMed:18216284}.
-!- INDUCTION: By ER stress. {ECO:0000269|PubMed:18216284}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a 50%
reduction of progeny numbers and a slower growth. RNAi-mediated
knockdown at the L4 larval stage results in a reduced lifespan and
in the lysosomal accumulation of lipofuscin in the intestine with
age. Motility is decreased and muscle sarcomeres are often patched
or wrinkled. Moderate decrease in pharyngeal pumping associated
with an abnormal pharynx morphology characterized by irregular and
discontinued cell junction protein ajm-1 localization at the
beginning and at the end of the procorpus and in the isthmus and a
loss of one of the three loops forming the lumen. In addition,
causes the up-regulation of ER stress marker hsp-4 which is
prevented in a ire-1 mutant background. UDPase and to a lesser
extent GDPase activities are reduced.
{ECO:0000269|PubMed:18216284}.
-!- SIMILARITY: Belongs to the apyrase family. {ECO:0000305}.
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EMBL; BX284606; CCD67349.1; -; Genomic_DNA.
PIR; T15973; T15973.
RefSeq; NP_509283.1; NM_076882.6.
UniGene; Cel.11047; -.
ProteinModelPortal; Q19202; -.
SMR; Q19202; -.
DIP; DIP-24879N; -.
IntAct; Q19202; 2.
MINT; MINT-1041351; -.
STRING; 6239.F08C6.6; -.
EPD; Q19202; -.
PaxDb; Q19202; -.
PeptideAtlas; Q19202; -.
PRIDE; Q19202; -.
EnsemblMetazoa; F08C6.6; F08C6.6; WBGene00017244.
GeneID; 181019; -.
KEGG; cel:CELE_F08C6.6; -.
CTD; 181019; -.
WormBase; F08C6.6; CE27925; WBGene00017244; apy-1.
eggNOG; KOG4494; Eukaryota.
eggNOG; ENOG410XS4T; LUCA.
GeneTree; ENSGT00390000012872; -.
HOGENOM; HOG000008129; -.
InParanoid; Q19202; -.
KO; K12304; -.
OMA; GSMGKEW; -.
OrthoDB; EOG091G0DL5; -.
PhylomeDB; Q19202; -.
Reactome; R-CEL-6798695; Neutrophil degranulation.
PRO; PR:Q19202; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00017244; -.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IMP:WormBase.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004382; F:guanosine-diphosphatase activity; IMP:WormBase.
GO; GO:0045134; F:uridine-diphosphatase activity; IMP:WormBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEP:WormBase.
GO; GO:0007369; P:gastrulation; IMP:WormBase.
GO; GO:0046712; P:GDP catabolic process; IMP:WormBase.
GO; GO:0060465; P:pharynx development; IMP:WormBase.
GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
GO; GO:0040009; P:regulation of growth rate; IMP:WormBase.
GO; GO:0000003; P:reproduction; IMP:WormBase.
GO; GO:0009408; P:response to heat; IEP:WormBase.
GO; GO:0006256; P:UDP catabolic process; IMP:WormBase.
InterPro; IPR009283; Apyrase.
InterPro; IPR036258; Apyrase-like_sf.
PANTHER; PTHR13023; PTHR13023; 1.
Pfam; PF06079; Apyrase; 1.
SUPFAM; SSF101887; SSF101887; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Reference proteome; Signal-anchor; Stress response;
Transmembrane; Transmembrane helix.
CHAIN 1 355 Apyrase apy-1. {ECO:0000305}.
/FTId=PRO_0000437964.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000305}.
TRANSMEM 7 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 355 Lumenal. {ECO:0000305}.
METAL 119 119 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q8WVQ1}.
METAL 166 166 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q8WVQ1}.
METAL 235 235 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q8WVQ1}.
METAL 350 350 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q8WVQ1}.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
SEQUENCE 355 AA; 40310 MW; 4AD6F807FE9812AC CRC64;
MTQESNSNFF NFLLFGFVTA IAFYSGTQFN KSSEQEEHIN HANLYSVKKF DDGAKEYSIM
LITDLDHDSK DGKKWKSLVS RGFLKVSADH KHADIHFDKD SEYYVDTNIA AGGRAMELSD
LAVFNGKLYS IDDRTGLIYQ ISDKKALPWV LLNDGPGNVV KGFKGEWITV KDTELIVGGL
GKEWTTTDGV YVNDHPMWVK HVSAHGAVHH ENWKDVYIRV RRAAGIEYPG YMIHEAVQWS
AIHRKWFFLP RRMSNEKYSE AEDENRGTNV LVIGNEELTD FEVVRVGSEN NKSRGFAAFQ
FVPNTHHQLI VAIKSEEKDG KPVASYASVF DIHGNVILDE YLLHGPYKYE GIAFA


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