ID   PHP14_BOVIN             Reviewed;         125 AA.
AC   Q32PA4;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=14 kDa phosphohistidine phosphatase;
DE            EC=3.9.1.3 {ECO:0000250|UniProtKB:Q9NRX4};
DE   AltName: Full=Phosphohistidine phosphatase 1;
DE            Short=PHPT1;
DE   AltName: Full=Protein histidine phosphatase;
DE            Short=PHP;
GN   Name=PHPT1; Synonyms=PHP14;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Exhibits phosphohistidine phosphatase activity.
CC       {ECO:0000250|UniProtKB:Q9NRX4}.
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:0000250|UniProtKB:Q9NRX4};
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:0000250|UniProtKB:Q9NRX4};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NRX4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the janus family. {ECO:0000305}.
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DR   EMBL; BC108196; AAI08197.1; -; mRNA.
DR   RefSeq; NP_001069984.1; NM_001076516.2.
DR   AlphaFoldDB; Q32PA4; -.
DR   SMR; Q32PA4; -.
DR   STRING; 9913.ENSBTAP00000028712; -.
DR   PaxDb; Q32PA4; -.
DR   PeptideAtlas; Q32PA4; -.
DR   PRIDE; Q32PA4; -.
DR   Ensembl; ENSBTAT00000085105; ENSBTAP00000068756; ENSBTAG00000050722.
DR   GeneID; 618691; -.
DR   KEGG; bta:618691; -.
DR   CTD; 29085; -.
DR   VEuPathDB; HostDB:ENSBTAG00000050722; -.
DR   VGNC; VGNC:32846; PHPT1.
DR   eggNOG; ENOG502S4DR; Eukaryota.
DR   GeneTree; ENSGT00390000002738; -.
DR   HOGENOM; CLU_120717_0_0_1; -.
DR   InParanoid; Q32PA4; -.
DR   OMA; MCTQTRA; -.
DR   OrthoDB; 1529401at2759; -.
DR   TreeFam; TF315158; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000050722; Expressed in tongue muscle and 106 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; IEA:Ensembl.
DR   GO; GO:0101006; F:protein histidine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR   GO; GO:2000984; P:negative regulation of ATP citrate synthase activity; IEA:Ensembl.
DR   GO; GO:0051350; P:negative regulation of lyase activity; IEA:Ensembl.
DR   GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0035971; P:peptidyl-histidine dephosphorylation; IEA:Ensembl.
DR   GO; GO:2000147; P:positive regulation of cell motility; IEA:Ensembl.
DR   GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRX4"
FT   CHAIN           2..125
FT                   /note="14 kDa phosphohistidine phosphatase"
FT                   /id="PRO_0000253631"
FT   ACT_SITE        53
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRX4"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRX4"
FT   BINDING         94..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRX4"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRX4"
SQ   SEQUENCE   125 AA;  13931 MW;  06102DE495483FAB CRC64;
     MAAAGLAQIP DVDIDSDGVF KYVLIRVYAA PPSGDPAVET KEIVRGYKWA EYHADIYDKV
     SGEIQKKGYD CECLGGGRIS HQSQDRKIHV YGYSMGYGRA QHSVSTEKIK AKYPDYEVTW
     ADDGY