IPYR_CAEEL
ID IPYR_CAEEL Reviewed; 427 AA.
AC Q18680; Q86DB1; Q86DB2; Q86DB3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 5.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Inorganic pyrophosphatase 1 {ECO:0000312|WormBase:C47E12.4c};
DE EC=3.6.1.1 {ECO:0000269|PubMed:17981157};
DE AltName: Full=Pyrophosphate phospho-hydrolase;
DE Short=PPase;
GN Name=pyp-1 {ECO:0000312|WormBase:C47E12.4c};
GN ORFNames=C47E12.4 {ECO:0000312|WormBase:C47E12.4c};
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=17981157; DOI=10.1016/j.febslet.2007.10.047;
RA Ko K.M., Lee W., Yu J.R., Ahnn J.;
RT "PYP-1, inorganic pyrophosphatase, is required for larval development and
RT intestinal function in C. elegans.";
RL FEBS Lett. 581:5445-5453(2007).
CC -!- FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi)
CC forming two phosphate ions. Plays a role in intestinal development and
CC subsequent normal secretory, digestive and absorption functions.
CC Required for larval development. {ECO:0000269|PubMed:17981157}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; EC=3.6.1.1;
CC Evidence={ECO:0000269|PubMed:17981157};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WI55};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17981157}. Note=In
CC intestinal cells, localizes around intestinal granules and vacuoles.
CC {ECO:0000269|PubMed:17981157}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c {ECO:0000312|WormBase:C47E12.4c};
CC IsoId=Q18680-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C47E12.4a};
CC IsoId=Q18680-2; Sequence=VSP_059613;
CC Name=d {ECO:0000312|WormBase:C47E12.4d};
CC IsoId=Q18680-4; Sequence=VSP_059612;
CC -!- TISSUE SPECIFICITY: Expressed in coelomocytes, the intestine and in the
CC nervous system including the nerve cords and sensory neurons.
CC {ECO:0000269|PubMed:17981157}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the embryonic stage of development
CC to adulthood. {ECO:0000269|PubMed:17981157}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR EMBL; BX284604; CAA93107.4; -; Genomic_DNA.
DR EMBL; BX284604; CAD89727.1; -; Genomic_DNA.
DR EMBL; BX284604; CAD89728.1; -; Genomic_DNA.
DR PIR; E88797; E88797.
DR PIR; T20014; T20014.
DR RefSeq; NP_001023073.1; NM_001027902.2. [Q18680-2]
DR RefSeq; NP_001023075.2; NM_001027904.4. [Q18680-1]
DR RefSeq; NP_001023076.1; NM_001027905.5. [Q18680-4]
DR AlphaFoldDB; Q18680; -.
DR SMR; Q18680; -.
DR BioGRID; 42959; 15.
DR STRING; 6239.C47E12.4b; -.
DR EPD; Q18680; -.
DR PaxDb; Q18680; -.
DR PeptideAtlas; Q18680; -.
DR EnsemblMetazoa; C47E12.4a.1; C47E12.4a.1; WBGene00008149. [Q18680-2]
DR EnsemblMetazoa; C47E12.4c.1; C47E12.4c.1; WBGene00008149. [Q18680-1]
DR EnsemblMetazoa; C47E12.4d.1; C47E12.4d.1; WBGene00008149. [Q18680-4]
DR GeneID; 177856; -.
DR KEGG; cel:CELE_C47E12.4; -.
DR UCSC; C47E12.5a.1; c. elegans. [Q18680-1]
DR CTD; 177856; -.
DR WormBase; C47E12.4a; CE33767; WBGene00008149; pyp-1. [Q18680-2]
DR WormBase; C47E12.4c; CE48296; WBGene00008149; pyp-1. [Q18680-1]
DR WormBase; C47E12.4d; CE05448; WBGene00008149; pyp-1. [Q18680-4]
DR eggNOG; KOG1626; Eukaryota.
DR GeneTree; ENSGT00390000017004; -.
DR HOGENOM; CLU_040684_3_0_1; -.
DR InParanoid; Q18680; -.
DR OrthoDB; 1398991at2759; -.
DR BRENDA; 3.6.1.1; 1045.
DR Reactome; R-CEL-379716; Cytosolic tRNA aminoacylation.
DR Reactome; R-CEL-379726; Mitochondrial tRNA aminoacylation.
DR Reactome; R-CEL-71737; Pyrophosphate hydrolysis.
DR PRO; PR:Q18680; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00008149; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0005773; C:vacuole; IDA:WormBase.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; HEP:WormBase.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IBA:GO_Central.
DR CDD; cd00412; pyrophosphatase; 1.
DR Gene3D; 3.90.80.10; -; 1.
DR InterPro; IPR008162; Pyrophosphatase.
DR InterPro; IPR036649; Pyrophosphatase_sf.
DR PANTHER; PTHR10286; PTHR10286; 1.
DR Pfam; PF00719; Pyrophosphatase; 1.
DR SUPFAM; SSF50324; SSF50324; 1.
DR PROSITE; PS00387; PPASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..427
FT /note="Inorganic pyrophosphatase 1"
FT /id="PRO_0000137571"
FT REGION 36..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT VAR_SEQ 1..135
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_059612"
FT VAR_SEQ 1..118
FT /note="MILSCRSVATARGFLLSTRLIMGCAVSQESAIATVSSSSNTATTSTSSSNTS
FT QKWATSRTSRPVTNVTQVSAIHTTSMDSGSSTVQLPSPRGSLTTAVSTSSSGAQRQMSA
FT NSERSLH -> MGLVLIAKRNKPLIAMMAAILFTVAVFLA (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_059613"
SQ SEQUENCE 427 AA; 46330 MW; 0D81AFF506ECC1E6 CRC64;
MILSCRSVAT ARGFLLSTRL IMGCAVSQES AIATVSSSSN TATTSTSSSN TSQKWATSRT
SRPVTNVTQV SAIHTTSMDS GSSTVQLPSP RGSLTTAVST SSSGAQRQMS ANSERSLHTR
PLSETAVILQ SQAVKMSTGA GDSAVYEAVE RGSLYSLDYR VYIKGPQGIV SPWHDIPLFA
NKDKRVYNMI VEIPRWTNAK MEMATKEPFS PIKQDEKKGV ARFVHNIFPH KGYIWNYGAL
PQTWEDPNHV VPDTGAKGDN DPIDVIEVGS KVAGRGAVLQ VKVLGTLALI DEGETDWKLV
AIDVNDENAD KLNDIDDVEK VYPGLLAASV EWFRNYKIPA GKPANEFAFN GEFKNREYAE
KVIDETNEYW KTLIKEANPS LNTVSRVPEA VHQGTDEAAA TAIGATPEHG ANAPLPGDVD
KWHFVQG
