LHPP_MOUSE
ID LHPP_MOUSE Reviewed; 270 AA.
AC Q9D7I5; Q3USP1; Q6P070;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phospholysine phosphohistidine inorganic pyrophosphate phosphatase;
DE EC=3.1.3.-;
DE EC=3.6.1.1;
GN Name=Lhpp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D7I5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D7I5-2; Sequence=VSP_028214, VSP_028215;
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; AK009207; BAB26140.1; -; mRNA.
DR EMBL; AK140229; BAE24290.1; -; mRNA.
DR EMBL; BC065789; AAH65789.1; -; mRNA.
DR CCDS; CCDS21925.1; -. [Q9D7I5-1]
DR RefSeq; NP_083885.1; NM_029609.1. [Q9D7I5-1]
DR AlphaFoldDB; Q9D7I5; -.
DR SMR; Q9D7I5; -.
DR STRING; 10090.ENSMUSP00000033241; -.
DR iPTMnet; Q9D7I5; -.
DR PhosphoSitePlus; Q9D7I5; -.
DR EPD; Q9D7I5; -.
DR jPOST; Q9D7I5; -.
DR MaxQB; Q9D7I5; -.
DR PaxDb; Q9D7I5; -.
DR PeptideAtlas; Q9D7I5; -.
DR PRIDE; Q9D7I5; -.
DR ProteomicsDB; 286193; -. [Q9D7I5-1]
DR ProteomicsDB; 286194; -. [Q9D7I5-2]
DR Antibodypedia; 1952; 131 antibodies from 23 providers.
DR DNASU; 76429; -.
DR Ensembl; ENSMUST00000033241; ENSMUSP00000033241; ENSMUSG00000030946. [Q9D7I5-1]
DR Ensembl; ENSMUST00000106170; ENSMUSP00000147970; ENSMUSG00000030946. [Q9D7I5-2]
DR GeneID; 76429; -.
DR KEGG; mmu:76429; -.
DR UCSC; uc009kce.1; mouse. [Q9D7I5-1]
DR CTD; 64077; -.
DR MGI; MGI:1923679; Lhpp.
DR VEuPathDB; HostDB:ENSMUSG00000030946; -.
DR eggNOG; KOG3040; Eukaryota.
DR GeneTree; ENSGT00940000159002; -.
DR HOGENOM; CLU_043473_4_1_1; -.
DR InParanoid; Q9D7I5; -.
DR OMA; GPCIDVG; -.
DR OrthoDB; 982374at2759; -.
DR PhylomeDB; Q9D7I5; -.
DR TreeFam; TF314344; -.
DR BRENDA; 3.9.1.3; 3474.
DR Reactome; R-MMU-71737; Pyrophosphate hydrolysis.
DR BioGRID-ORCS; 76429; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Lhpp; mouse.
DR PRO; PR:Q9D7I5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D7I5; protein.
DR Bgee; ENSMUSG00000030946; Expressed in lip and 220 other tissues.
DR ExpressionAtlas; Q9D7I5; baseline and differential.
DR Genevisible; Q9D7I5; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
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:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..270
FT /note="Phospholysine phosphohistidine inorganic
FT pyrophosphate phosphatase"
FT /id="PRO_0000305075"
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"
FT VAR_SEQ 241..242
FT /note="GD -> RC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028214"
FT VAR_SEQ 243..270
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028215"
SQ SEQUENCE 270 AA; 29144 MW; 19A258715AA668B5 CRC64;
MAAWAERLTG VRGVLLDISG VLCDSSASGA TAIAGSVEAV ARLKQSPLKV RFCTNESQKS
LRELVGVLQQ LGFDISEEEV TAPAPATCQI LKERGLRPHL LIHEGVRSEF DDIDMSNPNC
VVIADAGEAF SYQNMNRAFQ VLMELENPVL ISLGKGRYYK ETSGLMLDVG GYMKALEYAC
GIKAEVVGKP SPEFFKSALQ AIGVEAHQAI MIGDDIVGDV GGAQQCGMRA LQVRTGKFRP
GDEHHPEVQA DGYVDNLAEA VDLLLKYTDK
