PHP14_PIG
ID PHP14_PIG Reviewed; 126 AA.
AC P59083; F1RWN4;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=14 kDa phosphohistidine phosphatase {ECO:0000303|PubMed:12383260};
DE EC=3.9.1.3 {ECO:0000269|PubMed:12383260};
DE AltName: Full=Phosphohistidine phosphatase 1;
DE Short=PHPT1;
DE AltName: Full=Protein histidine phosphatase;
DE Short=PHP;
GN Name=PHPT1; Synonyms=PHP14;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc;
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-22; 49-59; 68-79 AND 118-126, FUNCTION, SUBUNIT, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Embryonic kidney;
RX PubMed=12383260; DOI=10.1046/j.1432-1033.2002.03206.x;
RA Ek P., Pettersson G., Ek B., Gong F., Li J.-P., Zetterqvist O.;
RT "Identification and characterization of a mammalian 14-kDa phosphohistidine
RT phosphatase.";
RL Eur. J. Biochem. 269:5016-5023(2002).
CC -!- FUNCTION: Exhibits phosphohistidine phosphatase activity.
CC {ECO:0000269|PubMed:12383260}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(pros)-phospho-L-histidyl-[protein] = L-histidyl-
CC [protein] + phosphate; Xref=Rhea:RHEA:47964, Rhea:RHEA-COMP:9745,
CC Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15377, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:64837; EC=3.9.1.3;
CC Evidence={ECO:0000269|PubMed:12383260};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(tele)-phospho-L-histidyl-[protein] = L-histidyl-
CC [protein] + phosphate; Xref=Rhea:RHEA:47960, Rhea:RHEA-COMP:9745,
CC Rhea:RHEA-COMP:10719, ChEBI:CHEBI:15377, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83586; EC=3.9.1.3;
CC Evidence={ECO:0000269|PubMed:12383260};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12383260}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the janus family. {ECO:0000305}.
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DR EMBL; FP236151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005652779.1; XM_005652722.1.
DR AlphaFoldDB; P59083; -.
DR SMR; P59083; -.
DR STRING; 9823.ENSSSCP00000006234; -.
DR PeptideAtlas; P59083; -.
DR PRIDE; P59083; -.
DR Ensembl; ENSSSCT00070000111; ENSSSCP00070000097; ENSSSCG00070000065.
DR eggNOG; ENOG502S4DR; Eukaryota.
DR InParanoid; P59083; -.
DR OMA; MCTQTRA; -.
DR TreeFam; TF315158; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 1.
DR Genevisible; F1RWN4; SS.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0101006; F:protein histidine phosphatase activity; IDA:BHF-UCL.
DR GO; GO:0035971; P:peptidyl-histidine dephosphorylation; IDA:BHF-UCL.
DR Gene3D; 3.50.20.20; -; 1.
DR InterPro; IPR007702; Janus.
DR InterPro; IPR038596; Janus_sf.
DR InterPro; IPR028441; PHPT1.
DR PANTHER; PTHR12258; PTHR12258; 1.
DR PANTHER; PTHR12258:SF10; PTHR12258:SF10; 1.
DR Pfam; PF05005; Ocnus; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Protein phosphatase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12383260"
FT CHAIN 2..126
FT /note="14 kDa phosphohistidine phosphatase"
FT /id="PRO_0000206154"
FT ACT_SITE 54
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX4"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX4"
FT BINDING 95..97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX4"
SQ SEQUENCE 126 AA; 13932 MW; C1B93EF39B873B69 CRC64;
MAAAADLAQI PDVDIDSDGV FKYVLIRVHA VSPPGTPAGE SKEIVRGYKW AEYHADIYDK
VSGEMQKKGI DCECLGGGRI SHQSQDKKIH VYGYSMGYGR AQHSISTEKI KARYPDYSVT
WADDGY
