ID   IPYR_BOVIN              Reviewed;         289 AA.
AC   P37980; Q1RMH6;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Inorganic pyrophosphatase;
DE            EC=3.6.1.1;
DE   AltName: Full=Pyrophosphate phospho-hydrolase;
DE            Short=PPase;
GN   Name=PPA1; Synonyms=PP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Retina;
RX   PubMed=1339444; DOI=10.1016/s0021-9258(18)35812-5;
RA   Yang Z., Wensel T.G.;
RT   "Molecular cloning and functional expression of cDNA encoding a mammalian
RT   inorganic pyrophosphatase.";
RL   J. Biol. Chem. 267:24641-24647(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Highest levels are found in retinal rod outer
CC       segments.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR   EMBL; M95283; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC114891; AAI14892.1; -; mRNA.
DR   PIR; A45153; A45153.
DR   RefSeq; NP_001068586.1; NM_001075118.1.
DR   AlphaFoldDB; P37980; -.
DR   SMR; P37980; -.
DR   STRING; 9913.ENSBTAP00000010311; -.
DR   PaxDb; P37980; -.
DR   PeptideAtlas; P37980; -.
DR   PRIDE; P37980; -.
DR   Ensembl; ENSBTAT00000010311; ENSBTAP00000010311; ENSBTAG00000007836.
DR   GeneID; 280701; -.
DR   KEGG; bta:280701; -.
DR   CTD; 5464; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007836; -.
DR   VGNC; VGNC:55992; PPA1.
DR   eggNOG; KOG1626; Eukaryota.
DR   GeneTree; ENSGT00390000017004; -.
DR   HOGENOM; CLU_040684_0_2_1; -.
DR   InParanoid; P37980; -.
DR   OMA; DWKILCI; -.
DR   OrthoDB; 1398991at2759; -.
DR   TreeFam; TF300887; -.
DR   BRENDA; 3.6.1.1; 908.
DR   Reactome; R-BTA-379716; Cytosolic tRNA aminoacylation.
DR   Reactome; R-BTA-71737; Pyrophosphate hydrolysis.
DR   Proteomes; UP000009136; Chromosome 28.
DR   Bgee; ENSBTAG00000007836; Expressed in oocyte and 104 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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: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   Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium;
KW   Metal-binding; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q15181"
FT   CHAIN           2..289
FT                   /note="Inorganic pyrophosphatase"
FT                   /id="PRO_0000137566"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15181"
FT   MOD_RES         57
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15181"
FT   MOD_RES         250
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15181"
FT   CONFLICT        3
FT                   /note="G -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   289 AA;  32814 MW;  66E65A21F8C7892A CRC64;
     MSGFSSEERA APFTLEYRVF LKNEKGQYIS PFHDIPIYAD KEVFHMVVEV PRWSNAKMEI
     ATKDPLNPIK QDVKKGKLRY VANLFPYKGY IWNYGAIPQT WEDPGHNDKH TGCCGDNDPI
     DVCEIGSKVC ARGEIIRVKV LGILAMIDEG ETDWKVIAIN VEDPDAANYN DINDVKRLKP
     GYLEATVDWF RRYKVPDGKP ENEFAFNAEF KDKNFAIDII ESTHDYWRAL VTKKTDGKGI
     SCMNTTVSES PFQCDPDAAK AIVDALPPPC ESACTIPTDV DKWFHHQKN