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Database: UniProt
Entry: A0A3Q2HA82_HORSE
LinkDB: A0A3Q2HA82_HORSE
Original site: A0A3Q2HA82_HORSE 
ID   A0A3Q2HA82_HORSE        Unreviewed;       249 AA.
AC   A0A3Q2HA82;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 2.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Phosphoethanolamine/phosphocholine phosphatase 1 {ECO:0000313|Ensembl:ENSECAP00000030521.2};
GN   Name=PHOSPHO1 {ECO:0000313|Ensembl:ENSECAP00000030521.2,
GN   ECO:0000313|VGNC:VGNC:21399};
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:ENSECAP00000030521.2, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000030521.2, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030521.2,
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:ENSECAP00000030521.2}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030521.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRSR:PIRSR031051-3};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO
CC       family. {ECO:0000256|ARBA:ARBA00008541}.
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DR   AlphaFoldDB; A0A3Q2HA82; -.
DR   Ensembl; ENSECAT00000034688.2; ENSECAP00000030521.2; ENSECAG00000016583.4.
DR   Ensembl; ENSECAT00000111356.1; ENSECAP00000081045.1; ENSECAG00000016583.4.
DR   Ensembl; ENSECAT00000133105.1; ENSECAP00000079259.1; ENSECAG00000016583.4.
DR   Ensembl; ENSECAT00000138426.1; ENSECAP00000086376.1; ENSECAG00000016583.4.
DR   Ensembl; ENSECAT00000139645.1; ENSECAP00000055522.1; ENSECAG00000016583.4.
DR   Ensembl; ENSECAT00000140996.1; ENSECAP00000069524.1; ENSECAG00000016583.4.
DR   CTD; 162466; -.
DR   VGNC; VGNC:21399; PHOSPHO1.
DR   GeneTree; ENSGT00390000007741; -.
DR   OrthoDB; 372892at2759; -.
DR   Proteomes; UP000002281; Chromosome 11.
DR   Bgee; ENSECAG00000016583; Expressed in bone marrow and 21 other cell types or tissues.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   CDD; cd16418; HAD_Pase; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR016965; Pase_PHOSPHO-typ.
DR   NCBIfam; TIGR01489; DKMTPPase-SF; 1.
DR   NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR   PANTHER; PTHR20889; PHOSPHATASE, ORPHAN 1, 2; 1.
DR   PANTHER; PTHR20889:SF2; PHOSPHOETHANOLAMINE_PHOSPHOCHOLINE PHOSPHATASE; 1.
DR   Pfam; PF06888; Put_Phosphatase; 1.
DR   PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR031051-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR031051-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281}.
FT   ACT_SITE        14
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT   ACT_SITE        16
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT   BINDING         25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT   BINDING         185
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
SQ   SEQUENCE   249 AA;  27753 MW;  3020D827B33CE7DB CRC64;
     MAAQGAPRFL LTFDFDETIV DENSDDSIVR AAPGQRLPES LRATYREGFY NEYMQRVFKY
     LGEQGVRPRD LRAIYEAIPL SPGMGDLLQF VAKQGASFEV ILISDANTFG VESALRAAGH
     HGLFRRIFSN PAGPDARGLL ALRPFHTHSC ARCPANMCKH KVLSDYLRER AHDGVHFERL
     FYVGDGANDF CPTGLLAGGD VAFPRRGYPM HRLIQEAQKA EPSSFRATVV PWETAADVRV
     HLQQVLKTS
//
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