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
//