PHP14_RABIT
ID PHP14_RABIT Reviewed; 125 AA.
AC P83468;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=14 kDa phosphohistidine phosphatase;
DE EC=3.9.1.3 {ECO:0000269|PubMed:12468887};
DE AltName: Full=Phosphohistidine phosphatase 1;
DE Short=PHPT1;
DE AltName: Full=Protein histidine phosphatase {ECO:0000303|PubMed:12468887};
DE Short=PHP;
GN Name=PHPT1; Synonyms=PHP14;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000305};
RN [1]
RP NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 2-45; 49-66; 79-99 AND 113-125,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=12468887; DOI=10.1097/01.wcb.0000045041.03034.99;
RA Klumpp S., Hermesmeier J., Selke D., Bechmann G., van den Brulle J.,
RA Weidner G., Scharm B., Guessow D., Baumeister R., Kellner R.,
RA Krieglstein J.;
RT "Protein histidine phosphatase: a novel enzyme with potency for neuronal
RT signaling.";
RL J. Cereb. Blood Flow Metab. 22:1420-1424(2002).
RN [2]
RP ERRATUM OF PUBMED:12468887.
RA Klumpp S., Hermesmeier J., Selke D., Bechmann G., van den Brulle J.,
RA Weidner G., Scharm B., Guessow D., Baumeister R., Kellner R.,
RA Krieglstein J.;
RL J. Cereb. Blood Flow Metab. 23:261-261(2003).
CC -!- FUNCTION: Exhibits phosphohistidine phosphatase activity.
CC {ECO:0000269|PubMed:12468887}.
CC -!- FUNCTION: May have a significant involvement in neuronal signaling.
CC {ECO:0000303|PubMed:12468887}.
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:12468887};
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:12468887};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12468887}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=13700; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12468887};
CC -!- SIMILARITY: Belongs to the janus family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P83468; -.
DR SMR; P83468; -.
DR InParanoid; P83468; -.
DR BRENDA; 3.9.1.3; 1749.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0101006; F:protein histidine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035971; P:peptidyl-histidine dephosphorylation; IEA:InterPro.
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 Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW 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_0000206155"
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; 13850 MW; 67A8291E1507F604 CRC64;
MAAAGLAQIP DVDIDSDGVF KYVLIRVHAA PPSEAPGGES KDIVRGYKWA EYHADIYDKV
SGELQKKGHD CECLGGGRIS HQSQDRKIHV YGYSMGYGRA QHSVSTEKIR AKYPDYEVTW
ADDGY
