Full text data of LHPP
LHPP
[Confidence: low (only semi-automatic identification from reviews)]
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase; hLHPP; 3.1.3.-; 3.6.1.1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase; hLHPP; 3.1.3.-; 3.6.1.1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H008
ID LHPP_HUMAN Reviewed; 270 AA.
AC Q9H008; B3KP20; Q2TBE9; Q5VUV9; Q5VUW0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-OCT-2007, sequence version 2.
DT 22-JAN-2014, entry version 89.
DE RecName: Full=Phospholysine phosphohistidine inorganic pyrophosphate phosphatase;
DE Short=hLHPP;
DE EC=3.1.3.-;
DE EC=3.6.1.1;
GN Name=LHPP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP VARIANT ARG-94.
RC TISSUE=Cervix carcinoma;
RX PubMed=12801912; DOI=10.1093/jb/mvg078;
RA Yokoi F., Hiraishi H., Izuhara K.;
RT "Molecular cloning of a cDNA for the human phospholysine
RT phosphohistidine inorganic pyrophosphate phosphatase.";
RL J. Biochem. 133:607-614(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ARG-94.
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-94.
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16430861; DOI=10.1016/j.bbrc.2006.01.016;
RA Koike E., Toda S., Yokoi F., Izuhara K., Koike N., Itoh K.,
RA Miyazaki K., Sugihara H.;
RT "Expression of new human inorganic pyrophosphatase in thyroid
RT diseases: its intimate association with hyperthyroidism.";
RL Biochem. Biophys. Res. Commun. 341:691-696(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
RP ANALOG AND MAGNESIUM IONS, AND COFACTOR.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human phospholysine phosphohistidine inorganic
RT pyrophosphate phosphatase LHPP.";
RL Submitted (MAR-2010) to the PDB data bank.
CC -!- FUNCTION: Phosphatase that hydrolyzes imidodiphosphate, 3-
CC phosphohistidine and 6-phospholysine. Has broad substrate
CC specificity and can also hydrolyze inorganic diphosphate, but with
CC lower efficiency (By similarity).
CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0 for PNP, and 5.5 for PPi;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H008-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H008-2; Sequence=VSP_041685, VSP_041686;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in brain, and at lower levels in
CC liver and kidney. Detected in thyroid (at protein level).
CC Expressed in liver, kidney and moderately in brain.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AB049629; BAB16411.1; -; mRNA.
DR EMBL; AK055532; BAG51532.1; -; mRNA.
DR EMBL; AL513190; CAH70377.1; -; Genomic_DNA.
DR EMBL; AL445237; CAH70377.1; JOINED; Genomic_DNA.
DR EMBL; AL513190; CAH70378.1; -; Genomic_DNA.
DR EMBL; AL391708; CAH70378.1; JOINED; Genomic_DNA.
DR EMBL; AL445237; CAH70378.1; JOINED; Genomic_DNA.
DR EMBL; AL391708; CAH74011.1; -; Genomic_DNA.
DR EMBL; AL445237; CAH74011.1; JOINED; Genomic_DNA.
DR EMBL; AL513190; CAH74011.1; JOINED; Genomic_DNA.
DR EMBL; AL445237; CAI17295.1; -; Genomic_DNA.
DR EMBL; AL513190; CAI17295.1; JOINED; Genomic_DNA.
DR EMBL; AL445237; CAI17296.1; -; Genomic_DNA.
DR EMBL; AL391708; CAI17296.1; JOINED; Genomic_DNA.
DR EMBL; AL513190; CAI17296.1; JOINED; Genomic_DNA.
DR EMBL; BC110344; AAI10345.1; -; mRNA.
DR EMBL; BC113629; AAI13630.1; -; mRNA.
DR EMBL; BC113631; AAI13632.1; -; mRNA.
DR RefSeq; NP_001161352.1; NM_001167880.1.
DR RefSeq; NP_071409.3; NM_022126.3.
DR UniGene; Hs.527748; -.
DR PDB; 2X4D; X-ray; 1.92 A; A/B=1-270.
DR PDBsum; 2X4D; -.
DR ProteinModelPortal; Q9H008; -.
DR SMR; Q9H008; 1-269.
DR STRING; 9606.ENSP00000357835; -.
DR PhosphoSite; Q9H008; -.
DR DMDM; 158705883; -.
DR PaxDb; Q9H008; -.
DR PRIDE; Q9H008; -.
DR DNASU; 64077; -.
DR Ensembl; ENST00000368839; ENSP00000357832; ENSG00000107902.
DR Ensembl; ENST00000368842; ENSP00000357835; ENSG00000107902.
DR GeneID; 64077; -.
DR KEGG; hsa:64077; -.
DR UCSC; uc001lhs.2; human.
DR CTD; 64077; -.
DR GeneCards; GC10P126140; -.
DR HGNC; HGNC:30042; LHPP.
DR HPA; HPA009163; -.
DR HPA; HPA009269; -.
DR neXtProt; NX_Q9H008; -.
DR PharmGKB; PA165548763; -.
DR eggNOG; COG0647; -.
DR HOGENOM; HOG000068106; -.
DR HOVERGEN; HBG075146; -.
DR InParanoid; Q9H008; -.
DR KO; K11725; -.
DR OMA; QAMGVEA; -.
DR PhylomeDB; Q9H008; -.
DR GenomeRNAi; 64077; -.
DR NextBio; 65859; -.
DR PRO; PR:Q9H008; -.
DR ArrayExpress; Q9H008; -.
DR Bgee; Q9H008; -.
DR Genevestigator; Q9H008; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008969; F:phosphohistidine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 2.
DR Gene3D; 3.40.50.10410; -; 1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR006355; HAD-SF_hydro_IIA_hyp2.
DR InterPro; IPR023215; NPhePase-like_dom.
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 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Hydrolase; Magnesium; Metal-binding; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 270 Phospholysine phosphohistidine inorganic
FT pyrophosphate phosphatase.
FT /FTId=PRO_0000305074.
FT REGION 17 19 Substrate binding.
FT REGION 54 55 Substrate binding.
FT METAL 17 17 Magnesium.
FT METAL 19 19 Magnesium; via carbonyl oxygen.
FT METAL 214 214 Magnesium.
FT BINDING 189 189 Substrate.
FT VAR_SEQ 210 210 V -> Q (in isoform 2).
FT /FTId=VSP_041685.
FT VAR_SEQ 211 270 Missing (in isoform 2).
FT /FTId=VSP_041686.
FT VARIANT 94 94 Q -> R (in dbSNP:rs6597801).
FT /FTId=VAR_035163.
FT CONFLICT 155 155 K -> R (in Ref. 2; BAG51532).
FT CONFLICT 170 170 G -> C (in Ref. 4; AAI10345).
FT HELIX 4 7
FT TURN 8 10
FT STRAND 13 16
FT TURN 19 21
FT STRAND 22 24
FT TURN 27 29
FT HELIX 36 45
FT STRAND 46 53
FT HELIX 61 70
FT HELIX 77 79
FT HELIX 83 94
FT STRAND 98 101
FT HELIX 104 110
FT STRAND 119 123
FT HELIX 127 129
FT HELIX 132 144
FT STRAND 150 153
FT STRAND 157 161
FT STRAND 164 167
FT HELIX 169 180
FT STRAND 185 188
FT HELIX 192 202
FT HELIX 206 208
FT STRAND 209 214
FT TURN 216 219
FT HELIX 220 225
FT STRAND 229 235
FT HELIX 240 244
FT STRAND 251 256
FT HELIX 257 267
SQ SEQUENCE 270 AA; 29165 MW; 09C301584453E79D CRC64;
MAPWGKRLAG VRGVLLDISG VLYDSGAGGG TAIAGSVEAV ARLKRSRLKV RFCTNESQKS
RAELVGQLQR LGFDISEQEV TAPAPAACQI LKEQGLRPYL LIHDGVRSEF DQIDTSNPNC
VVIADAGESF SYQNMNNAFQ VLMELEKPVL ISLGKGRYYK ETSGLMLDVG PYMKALEYAC
GIKAEVVGKP SPEFFKSALQ AIGVEAHQAV MIGDDIVGDV GGAQRCGMRA LQVRTGKFRP
SDEHHPEVKA DGYVDNLAEA VDLLLQHADK
//
ID LHPP_HUMAN Reviewed; 270 AA.
AC Q9H008; B3KP20; Q2TBE9; Q5VUV9; Q5VUW0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-OCT-2007, sequence version 2.
DT 22-JAN-2014, entry version 89.
DE RecName: Full=Phospholysine phosphohistidine inorganic pyrophosphate phosphatase;
DE Short=hLHPP;
DE EC=3.1.3.-;
DE EC=3.6.1.1;
GN Name=LHPP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP VARIANT ARG-94.
RC TISSUE=Cervix carcinoma;
RX PubMed=12801912; DOI=10.1093/jb/mvg078;
RA Yokoi F., Hiraishi H., Izuhara K.;
RT "Molecular cloning of a cDNA for the human phospholysine
RT phosphohistidine inorganic pyrophosphate phosphatase.";
RL J. Biochem. 133:607-614(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ARG-94.
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-94.
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16430861; DOI=10.1016/j.bbrc.2006.01.016;
RA Koike E., Toda S., Yokoi F., Izuhara K., Koike N., Itoh K.,
RA Miyazaki K., Sugihara H.;
RT "Expression of new human inorganic pyrophosphatase in thyroid
RT diseases: its intimate association with hyperthyroidism.";
RL Biochem. Biophys. Res. Commun. 341:691-696(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
RP ANALOG AND MAGNESIUM IONS, AND COFACTOR.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human phospholysine phosphohistidine inorganic
RT pyrophosphate phosphatase LHPP.";
RL Submitted (MAR-2010) to the PDB data bank.
CC -!- FUNCTION: Phosphatase that hydrolyzes imidodiphosphate, 3-
CC phosphohistidine and 6-phospholysine. Has broad substrate
CC specificity and can also hydrolyze inorganic diphosphate, but with
CC lower efficiency (By similarity).
CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0 for PNP, and 5.5 for PPi;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H008-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H008-2; Sequence=VSP_041685, VSP_041686;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in brain, and at lower levels in
CC liver and kidney. Detected in thyroid (at protein level).
CC Expressed in liver, kidney and moderately in brain.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
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DR EMBL; AB049629; BAB16411.1; -; mRNA.
DR EMBL; AK055532; BAG51532.1; -; mRNA.
DR EMBL; AL513190; CAH70377.1; -; Genomic_DNA.
DR EMBL; AL445237; CAH70377.1; JOINED; Genomic_DNA.
DR EMBL; AL513190; CAH70378.1; -; Genomic_DNA.
DR EMBL; AL391708; CAH70378.1; JOINED; Genomic_DNA.
DR EMBL; AL445237; CAH70378.1; JOINED; Genomic_DNA.
DR EMBL; AL391708; CAH74011.1; -; Genomic_DNA.
DR EMBL; AL445237; CAH74011.1; JOINED; Genomic_DNA.
DR EMBL; AL513190; CAH74011.1; JOINED; Genomic_DNA.
DR EMBL; AL445237; CAI17295.1; -; Genomic_DNA.
DR EMBL; AL513190; CAI17295.1; JOINED; Genomic_DNA.
DR EMBL; AL445237; CAI17296.1; -; Genomic_DNA.
DR EMBL; AL391708; CAI17296.1; JOINED; Genomic_DNA.
DR EMBL; AL513190; CAI17296.1; JOINED; Genomic_DNA.
DR EMBL; BC110344; AAI10345.1; -; mRNA.
DR EMBL; BC113629; AAI13630.1; -; mRNA.
DR EMBL; BC113631; AAI13632.1; -; mRNA.
DR RefSeq; NP_001161352.1; NM_001167880.1.
DR RefSeq; NP_071409.3; NM_022126.3.
DR UniGene; Hs.527748; -.
DR PDB; 2X4D; X-ray; 1.92 A; A/B=1-270.
DR PDBsum; 2X4D; -.
DR ProteinModelPortal; Q9H008; -.
DR SMR; Q9H008; 1-269.
DR STRING; 9606.ENSP00000357835; -.
DR PhosphoSite; Q9H008; -.
DR DMDM; 158705883; -.
DR PaxDb; Q9H008; -.
DR PRIDE; Q9H008; -.
DR DNASU; 64077; -.
DR Ensembl; ENST00000368839; ENSP00000357832; ENSG00000107902.
DR Ensembl; ENST00000368842; ENSP00000357835; ENSG00000107902.
DR GeneID; 64077; -.
DR KEGG; hsa:64077; -.
DR UCSC; uc001lhs.2; human.
DR CTD; 64077; -.
DR GeneCards; GC10P126140; -.
DR HGNC; HGNC:30042; LHPP.
DR HPA; HPA009163; -.
DR HPA; HPA009269; -.
DR neXtProt; NX_Q9H008; -.
DR PharmGKB; PA165548763; -.
DR eggNOG; COG0647; -.
DR HOGENOM; HOG000068106; -.
DR HOVERGEN; HBG075146; -.
DR InParanoid; Q9H008; -.
DR KO; K11725; -.
DR OMA; QAMGVEA; -.
DR PhylomeDB; Q9H008; -.
DR GenomeRNAi; 64077; -.
DR NextBio; 65859; -.
DR PRO; PR:Q9H008; -.
DR ArrayExpress; Q9H008; -.
DR Bgee; Q9H008; -.
DR Genevestigator; Q9H008; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008969; F:phosphohistidine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 2.
DR Gene3D; 3.40.50.10410; -; 1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR006355; HAD-SF_hydro_IIA_hyp2.
DR InterPro; IPR023215; NPhePase-like_dom.
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 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Hydrolase; Magnesium; Metal-binding; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 270 Phospholysine phosphohistidine inorganic
FT pyrophosphate phosphatase.
FT /FTId=PRO_0000305074.
FT REGION 17 19 Substrate binding.
FT REGION 54 55 Substrate binding.
FT METAL 17 17 Magnesium.
FT METAL 19 19 Magnesium; via carbonyl oxygen.
FT METAL 214 214 Magnesium.
FT BINDING 189 189 Substrate.
FT VAR_SEQ 210 210 V -> Q (in isoform 2).
FT /FTId=VSP_041685.
FT VAR_SEQ 211 270 Missing (in isoform 2).
FT /FTId=VSP_041686.
FT VARIANT 94 94 Q -> R (in dbSNP:rs6597801).
FT /FTId=VAR_035163.
FT CONFLICT 155 155 K -> R (in Ref. 2; BAG51532).
FT CONFLICT 170 170 G -> C (in Ref. 4; AAI10345).
FT HELIX 4 7
FT TURN 8 10
FT STRAND 13 16
FT TURN 19 21
FT STRAND 22 24
FT TURN 27 29
FT HELIX 36 45
FT STRAND 46 53
FT HELIX 61 70
FT HELIX 77 79
FT HELIX 83 94
FT STRAND 98 101
FT HELIX 104 110
FT STRAND 119 123
FT HELIX 127 129
FT HELIX 132 144
FT STRAND 150 153
FT STRAND 157 161
FT STRAND 164 167
FT HELIX 169 180
FT STRAND 185 188
FT HELIX 192 202
FT HELIX 206 208
FT STRAND 209 214
FT TURN 216 219
FT HELIX 220 225
FT STRAND 229 235
FT HELIX 240 244
FT STRAND 251 256
FT HELIX 257 267
SQ SEQUENCE 270 AA; 29165 MW; 09C301584453E79D CRC64;
MAPWGKRLAG VRGVLLDISG VLYDSGAGGG TAIAGSVEAV ARLKRSRLKV RFCTNESQKS
RAELVGQLQR LGFDISEQEV TAPAPAACQI LKEQGLRPYL LIHDGVRSEF DQIDTSNPNC
VVIADAGESF SYQNMNNAFQ VLMELEKPVL ISLGKGRYYK ETSGLMLDVG PYMKALEYAC
GIKAEVVGKP SPEFFKSALQ AIGVEAHQAV MIGDDIVGDV GGAQRCGMRA LQVRTGKFRP
SDEHHPEVKA DGYVDNLAEA VDLLLQHADK
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