ID A0A2I2YBY1_GORGO Unreviewed; 212 AA.
AC A0A2I2YBY1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Phospholysine phosphohistidine inorganic pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00039357};
DE EC=3.6.1.1 {ECO:0000256|ARBA:ARBA00012146};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000032439.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000032439.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000032439.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000032439.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; CABD030076608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030076609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030076610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030076611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030076612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030076613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030076614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030076615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030076616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030076617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018890350.1; XM_019034805.1.
DR AlphaFoldDB; A0A2I2YBY1; -.
DR Ensembl; ENSGGOT00000043385.1; ENSGGOP00000032439.1; ENSGGOG00000009416.3.
DR GeneID; 101142689; -.
DR KEGG; ggo:101142689; -.
DR CTD; 64077; -.
DR GeneTree; ENSGT00940000159002; -.
DR OrthoDB; 2876640at2759; -.
DR Proteomes; UP000001519; Chromosome 10.
DR Bgee; ENSGGOG00000009416; Expressed in prefrontal cortex and 5 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 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 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:UP000001519}.
SQ SEQUENCE 212 AA; 22880 MW; 66C938EA34C73C82 CRC64;
MAPWGKRLAG VRGVLLDISG VLYDSGAGGG TAIAGSVEAV ARLKRSRLKV RFCTNESQKS
RAELVGQLRR LGFDISEGEV TAPAPAACQI LKERGLRPYL LIHDGVRSEF DQIDTSNPNC
VVIADAGESF SYQNMNNAFQ VLMELENPVL ISLGKGRYYK ETSGLMLDVG PYMKALEYAC
GIKAEVVGKP SPEFFKSALQ AIGVEAHQLL SV
//
