ID   LHPP_RAT                Reviewed;         270 AA.
AC   Q5I0D5;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Phospholysine phosphohistidine inorganic pyrophosphate phosphatase;
DE            EC=3.1.3.-;
DE            EC=3.6.1.1;
GN   Name=Lhpp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Phosphatase that hydrolyzes imidodiphosphate, 3-
CC       phosphohistidine and 6-phospholysine. Has broad substrate specificity
CC       and can also hydrolyze inorganic diphosphate, but with lower efficiency
CC       (By similarity). {ECO:0000250}.
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       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC088448; AAH88448.1; -; mRNA.
DR   RefSeq; NP_001009706.1; NM_001009706.1.
DR   AlphaFoldDB; Q5I0D5; -.
DR   SMR; Q5I0D5; -.
DR   STRING; 10116.ENSRNOP00000022971; -.
DR   PhosphoSitePlus; Q5I0D5; -.
DR   PaxDb; Q5I0D5; -.
DR   PRIDE; Q5I0D5; -.
DR   GeneID; 361663; -.
DR   KEGG; rno:361663; -.
DR   UCSC; RGD:1359187; rat.
DR   CTD; 64077; -.
DR   RGD; 1359187; Lhpp.
DR   VEuPathDB; HostDB:ENSRNOG00000017097; -.
DR   eggNOG; KOG3040; Eukaryota.
DR   HOGENOM; CLU_043473_4_1_1; -.
DR   InParanoid; Q5I0D5; -.
DR   OMA; GPCIDVG; -.
DR   OrthoDB; 982374at2759; -.
DR   PhylomeDB; Q5I0D5; -.
DR   TreeFam; TF314344; -.
DR   Reactome; R-RNO-71737; Pyrophosphate hydrolysis.
DR   PRO; PR:Q5I0D5; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000017097; Expressed in kidney and 20 other tissues.
DR   Genevisible; Q5I0D5; RN.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; ISS:UniProtKB.
DR   CDD; cd07509; HAD_PPase; 1.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006355; LHPP/HDHD2.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR   TIGRFAMs; TIGR01458; HAD-SF-IIA-hyp3; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..270
FT                   /note="Phospholysine phosphohistidine inorganic
FT                   pyrophosphate phosphatase"
FT                   /id="PRO_0000305076"
FT   BINDING         17..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         54..55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  29190 MW;  FDBBCD6C5E3DCDBD CRC64;
     MAAWAERLSG VRGVLLDISG VLYDSGTGGG AAIAGSVEAV ARLKRSPLKV RFCTNESQKS
     RRELVGVLQR LGFDISEGEV TAPAPATCQI LKERGLRPHL LIHEGVRSEF DDIDMSNPNC
     VVIADAGEGF SYQNMNRAFQ VLMELENPVL ISLGKGRYYK ETSGLMLDVG GYMKALEYAC
     GIEAEVVGKP SPEFFRSALQ AIGVEAHQAI MIGDDIVGDV GGAQQCGMRA LQVRTGKFRP
     GDEHHPEVRA DGYVDNLAEA VDLLLQHMDK