ID A0A3P8YFC9_ESOLU Unreviewed; 312 AA.
AC A0A3P8YFC9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phospholysine phosphohistidine inorganic pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00039357};
DE EC=3.6.1.1 {ECO:0000256|ARBA:ARBA00012146};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000015283.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000015283.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000015283.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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
CC efficiency. {ECO:0000256|ARBA:ARBA00037258}.
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:0000256|ARBA:ARBA00000926};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00007958}.
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DR AlphaFoldDB; A0A3P8YFC9; -.
DR STRING; 8010.ENSELUP00000015283; -.
DR Ensembl; ENSELUT00000024325.2; ENSELUP00000015283.2; ENSELUG00000015266.2.
DR GeneTree; ENSGT00940000159002; -.
DR InParanoid; A0A3P8YFC9; -.
DR OMA; GPCIDVG; -.
DR OrthoDB; 2876640at2759; -.
DR Proteomes; UP000265140; LG06.
DR Bgee; ENSELUG00000015266; Expressed in muscle tissue and 15 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd07509; HAD_PPase; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01458; HAD-SF-IIA-hyp3; 1.
DR PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR19288:SF44; PHOSPHOLYSINE PHOSPHOHISTIDINE INORGANIC PYROPHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF13344; Hydrolase_6; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140}.
SQ SEQUENCE 312 AA; 34346 MW; D0A34C8F3D52075C CRC64;
MFSIEKTTLT ASPPFWCRFK TTYPSEIFYA HALSVCYTSA MAATSWEDSV KSLKGVILDM
CGVLYDAGED GGTPIPGSVE AVKRLRASDL KLRFCTNETQ ATREKFVAKL QRMGFEISVS
EVFSPAPAAV AILKERGLRP HLLVHDDVVP EFDHVEKTNP NCVVIGDAAE KFSYQNLNTA
FRVLIGLEDP VLFSLGRGKY YKEDDGLNLD VGVYMKALEY ACDVEAEVIG KPAPMFFQKV
LDDMGIPSHE SLMIGDDLVN DVGGAQECGM KGVQVRTGKY RPIDEKHPTV TADGYVNNLA
EAVETILKLR GQ
//
