APY1_CAEEL
ID APY1_CAEEL Reviewed; 355 AA.
AC Q19202;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Apyrase apy-1 {ECO:0000303|PubMed:18216284};
DE EC=3.6.1.6 {ECO:0000305|PubMed:18216284};
DE AltName: Full=Uridine-diphosphatase {ECO:0000303|PubMed:18216284};
DE Short=UDPase {ECO:0000303|PubMed:18216284};
GN Name=apy-1 {ECO:0000312|WormBase:F08C6.6};
GN ORFNames=F08C6.6 {ECO:0000312|WormBase:F08C6.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION BY ER STRESS,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=18216284; DOI=10.1091/mbc.e07-06-0547;
RA Uccelletti D., Pascoli A., Farina F., Alberti A., Mancini P.,
RA Hirschberg C.B., Palleschi C.;
RT "APY-1, a novel Caenorhabditis elegans apyrase involved in unfolded protein
RT response signalling and stress responses.";
RL Mol. Biol. Cell 19:1337-1345(2008).
CC -!- FUNCTION: Hydrolyzes UDP and to a lesser extent GDP. By preventing the
CC accumulation of NDP, may promote the reglucosylation of incompletely
CC folded glycoproteins in the endoplasmic reticulum following the
CC unfolded protein response. {ECO:0000269|PubMed:18216284}.
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 Evidence={ECO:0000305|PubMed:18216284};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q8WVQ1};
CC -!- INTERACTION:
CC Q19202; Q21746: sgt-1; NbExp=3; IntAct=EBI-319014, EBI-312019;
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000303|PubMed:18216284}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:18216284}.
CC -!- INDUCTION: By ER stress. {ECO:0000269|PubMed:18216284}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a 50% reduction of
CC progeny numbers and a slower growth. RNAi-mediated knockdown at the L4
CC larval stage results in a reduced lifespan and in the lysosomal
CC accumulation of lipofuscin in the intestine with age. Motility is
CC decreased and muscle sarcomeres are often patched or wrinkled. Moderate
CC decrease in pharyngeal pumping associated with an abnormal pharynx
CC morphology characterized by irregular and discontinued cell junction
CC protein ajm-1 localization at the beginning and at the end of the
CC procorpus and in the isthmus and a loss of one of the three loops
CC forming the lumen. In addition, causes the up-regulation of ER stress
CC marker hsp-4 which is prevented in an ire-1 mutant background. UDPase
CC and to a lesser extent GDPase activities are reduced.
CC {ECO:0000269|PubMed:18216284}.
CC -!- SIMILARITY: Belongs to the apyrase family. {ECO:0000305}.
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DR EMBL; BX284606; CCD67349.1; -; Genomic_DNA.
DR PIR; T15973; T15973.
DR RefSeq; NP_509283.1; NM_076882.6.
DR AlphaFoldDB; Q19202; -.
DR SMR; Q19202; -.
DR DIP; DIP-24879N; -.
DR IntAct; Q19202; 2.
DR STRING; 6239.F08C6.6; -.
DR EPD; Q19202; -.
DR PaxDb; Q19202; -.
DR PeptideAtlas; Q19202; -.
DR EnsemblMetazoa; F08C6.6.1; F08C6.6.1; WBGene00017244.
DR GeneID; 181019; -.
DR KEGG; cel:CELE_F08C6.6; -.
DR CTD; 181019; -.
DR WormBase; F08C6.6; CE27925; WBGene00017244; apy-1.
DR eggNOG; KOG4494; Eukaryota.
DR GeneTree; ENSGT00390000012872; -.
DR HOGENOM; CLU_047493_0_1_1; -.
DR InParanoid; Q19202; -.
DR OMA; DEHMGCN; -.
DR OrthoDB; 1126948at2759; -.
DR PhylomeDB; Q19202; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q19202; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00017244; Expressed in larva and 4 other tissues.
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; IMP:WormBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IMP:WormBase.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEP:WormBase.
DR GO; GO:0007369; P:gastrulation; IMP:WormBase.
DR GO; GO:0046712; P:GDP catabolic process; IMP:WormBase.
DR GO; GO:0060465; P:pharynx development; IMP:WormBase.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0040009; P:regulation of growth rate; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0009408; P:response to heat; IEP:WormBase.
DR GO; GO:0006256; P:UDP catabolic process; IMP:WormBase.
DR Gene3D; 2.120.10.100; -; 1.
DR InterPro; IPR009283; Apyrase.
DR InterPro; IPR036258; Apyrase_sf.
DR PANTHER; PTHR13023; PTHR13023; 1.
DR SUPFAM; SSF101887; SSF101887; 1.
PE 1: Evidence at protein level;
KW Calcium; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..355
FT /note="Apyrase apy-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437964"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..355
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ 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
