PHP14_PONAB
ID PHP14_PONAB Reviewed; 125 AA.
AC Q5R8L6; Q5R855;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Heart, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R8L6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R8L6-2; Sequence=VSP_021108;
CC -!- SIMILARITY: Belongs to the janus family. {ECO:0000305}.
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DR EMBL; CR859736; CAH91894.1; -; mRNA.
DR EMBL; CR859899; CAH92055.1; -; mRNA.
DR RefSeq; NP_001127500.1; NM_001134028.1. [Q5R8L6-2]
DR RefSeq; NP_001128837.1; NM_001135365.1. [Q5R8L6-1]
DR AlphaFoldDB; Q5R8L6; -.
DR SMR; Q5R8L6; -.
DR STRING; 9601.ENSPPYP00000022187; -.
DR PRIDE; Q5R8L6; -.
DR GeneID; 100174576; -.
DR GeneID; 100189753; -.
DR KEGG; pon:100174576; -.
DR CTD; 29085; -.
DR eggNOG; ENOG502S4DR; Eukaryota.
DR InParanoid; Q5R8L6; -.
DR Proteomes; UP000001595; 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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cytoplasm; 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_0000253632"
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"
FT VAR_SEQ 94..125
FT /note="TMAYGPAQHAISTEKIKAKYPDYEVTWANDGY -> SMMRPTCVPLGASGPR
FT IHHQGLWSCPTRHFN (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021108"
SQ SEQUENCE 125 AA; 13860 MW; CE3FEB9C2272FC3A CRC64;
MAAADLAHIP DVDIDSDGVF KYVLIRVHSA SRSGAPVAES KEIVRGYKWA EYHADIYDKV
SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYTMAYGPA QHAISTEKIK AKYPDYEVTW
ANDGY