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Database: UniProt
Entry: F6XPF7_HORSE
LinkDB: F6XPF7_HORSE
Original site: F6XPF7_HORSE 
ID   F6XPF7_HORSE            Unreviewed;       296 AA.
AC   F6XPF7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=Pyridoxal phosphatase {ECO:0000313|Ensembl:ENSECAP00000002171.2};
GN   Name=PDXP {ECO:0000313|Ensembl:ENSECAP00000002171.2,
GN   ECO:0000313|VGNC:VGNC:56380};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000002171.2, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000002171.2, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000002171.2,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000002171.2}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000002171.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000915-3};
CC       Note=Divalent metal ions. Mg(2+) is the most effective.
CC       {ECO:0000256|PIRSR:PIRSR000915-3};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000256|PIRNR:PIRNR000915}.
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DR   AlphaFoldDB; F6XPF7; -.
DR   SMR; F6XPF7; -.
DR   STRING; 9796.ENSECAP00000002171; -.
DR   PaxDb; 9796-ENSECAP00000002171; -.
DR   Ensembl; ENSECAT00000003031.3; ENSECAP00000002171.2; ENSECAG00000003182.3.
DR   VGNC; VGNC:56380; PDXP.
DR   GeneTree; ENSGT00940000162045; -.
DR   HOGENOM; CLU_043473_3_1_1; -.
DR   InParanoid; F6XPF7; -.
DR   OMA; MDGVLIH; -.
DR   OrthoDB; 217676at2759; -.
DR   TreeFam; TF314344; -.
DR   Proteomes; UP000002281; Chromosome 28.
DR   Bgee; ENSECAG00000003182; Expressed in prefrontal cortex and 21 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR   GO; GO:0032154; C:cleavage furrow; IEA:Ensembl.
DR   GO; GO:0070938; C:contractile ring; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0033883; F:pyridoxal phosphatase activity; IBA:GO_Central.
DR   GO; GO:0031247; P:actin rod assembly; IEA:Ensembl.
DR   GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
DR   GO; GO:0016311; P:dephosphorylation; IEA:Ensembl.
DR   GO; GO:0030836; P:positive regulation of actin filament depolymerization; IEA:Ensembl.
DR   GO; GO:0032361; P:pyridoxal phosphate catabolic process; IEA:Ensembl.
DR   GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IEA:Ensembl.
DR   CDD; cd07510; HAD_Pase_UmpH-like; 1.
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; IPR006349; PGP_euk.
DR   NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR   NCBIfam; TIGR01452; PGP_euk; 1.
DR   PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR19288:SF94; CHRONOPHIN; 1.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   Pfam; PF13242; Hydrolase_like; 1.
DR   PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR   SFLD; SFLDG01139; C2.A:_Pyridoxal_Phosphate_Phos; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000915};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281}.
FT   ACT_SITE        25
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        27
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         25
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         27
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         58..60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   296 AA;  31696 MW;  65D57B89B81B642B CRC64;
     MARCERLRGA AVRDVLGRAQ GVLFDCDGVL WNGERAVPGA PELLQRLARA GKAALFVSNN
     SRRARPELAL RFARLGFGGL RAEQLFSSAL CAARLLRQRL LGPPGAPGAV FVLGGEGLRA
     ELRAAGLRLA GDPGEDPGAA PRVRAVLVGY DEHFSFAKLS EACAHLRDPD CLLVATDRDP
     WHPLSDGSRT PGTGSLTAAV ETASGRQALV VGKPSPYMFE CITEHFSVDP ARTLMVGDRL
     ETDILFGHRC GMTTVLTLTG VSRLEEAEAY LAAGQHDLVP HYYVESIADL MEGLED
//
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