ID   PHOP1_DANRE             Reviewed;         279 AA.
AC   Q6DBV4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable phosphatase phospho1;
DE            EC=3.1.3.75 {ECO:0000250|UniProtKB:Q8TCT1};
GN   Name=phospho1; ORFNames=zgc:92423;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphatase that has a high activity toward
CC       phosphoethanolamine (PEA) and phosphocholine (PCho). Involved in the
CC       generation of inorganic phosphate for bone mineralization.
CC       {ECO:0000250|UniProtKB:Q8TCT1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + phosphoethanolamine = ethanolamine + phosphate;
CC         Xref=Rhea:RHEA:16089, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57603, ChEBI:CHEBI:58190; EC=3.1.3.75;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + phosphocholine = choline + phosphate;
CC         Xref=Rhea:RHEA:10492, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:295975; EC=3.1.3.75;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT1};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8TCT1};
CC   -!- SUBCELLULAR LOCATION: Extracellular vesicle
CC       {ECO:0000250|UniProtKB:Q8R2H9}. Note=Localizes to special class of
CC       extracellular vesicles, named matrix vesicles (MVs), which are released
CC       by osteogenic cells. {ECO:0000250|UniProtKB:Q8R2H9}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO
CC       family. {ECO:0000305}.
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DR   EMBL; BC078347; AAH78347.1; -; mRNA.
DR   RefSeq; NP_001003461.1; NM_001003461.1.
DR   AlphaFoldDB; Q6DBV4; -.
DR   STRING; 7955.ENSDARP00000055833; -.
DR   PaxDb; Q6DBV4; -.
DR   GeneID; 100002812; -.
DR   KEGG; dre:100002812; -.
DR   CTD; 162466; -.
DR   ZFIN; ZDB-GENE-040801-198; phospho1.
DR   eggNOG; KOG3120; Eukaryota.
DR   InParanoid; Q6DBV4; -.
DR   OrthoDB; 1454608at2759; -.
DR   PhylomeDB; Q6DBV4; -.
DR   Reactome; R-DRE-1483191; Synthesis of PC.
DR   Reactome; R-DRE-1483213; Synthesis of PE.
DR   PRO; PR:Q6DBV4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0065010; C:extracellular membrane-bounded organelle; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0052731; F:phosphocholine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0052732; F:phosphoethanolamine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0030282; P:bone mineralization; ISS:UniProtKB.
DR   GO; GO:0030500; P:regulation of bone mineralization; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 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   PANTHER; PTHR20889; PTHR20889; 1.
DR   Pfam; PF06888; Put_Phosphatase; 1.
DR   PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Metal-binding; Mineral balance; Reference proteome.
FT   CHAIN           1..279
FT                   /note="Probable phosphatase phospho1"
FT                   /id="PRO_0000068832"
FT   ACT_SITE        41
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT   ACT_SITE        43
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT   BINDING         41
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT   BINDING         43
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT   BINDING         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GD0"
SQ   SEQUENCE   279 AA;  31403 MW;  518AFBC0FAB29E32 CRC64;
     MRDSVFNCCV SPPHPPGAAA AERRSRSPAP QNHSRFLMFF DFDETLVDEC SDDSMVSAAP
     GGVLPGWLKD TYRPGRYNEY MQRVLAYLSE QGVTPAAIRA TVEKLPPCPG IPALMHFLLS
     QPSRDFEVVC VSDANTVFIE TWLQHMGFQP LFLRIFTNPA HFDDNGVLQL RPFHSHECLR
     CPANMCKAVV VRQYVAQRIR ERGGRPYQKV LYMGDGANDF CPSLTLSPGD VAFPRRDFPM
     HKLIQEMGEA KPGEFKASVV PWKSGEDVVN TLRKILERT