Full text data of PHOSPHO1
PHOSPHO1
[Confidence: low (only semi-automatic identification from reviews)]
Phosphoethanolamine/phosphocholine phosphatase; 3.1.3.75
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosphoethanolamine/phosphocholine phosphatase; 3.1.3.75
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8TCT1
ID PHOP1_HUMAN Reviewed; 267 AA.
AC Q8TCT1; E9PAM0; Q17RU6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2002, sequence version 1.
DT 22-JAN-2014, entry version 85.
DE RecName: Full=Phosphoethanolamine/phosphocholine phosphatase;
DE EC=3.1.3.75;
GN Name=PHOSPHO1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12464021; DOI=10.1046/j.1365-2052.2002.00900.x;
RA Houston B., Paton I.R., Burt D.W., Farquharson C.;
RT "Chromosomal localization of the chicken and mammalian orthologues of
RT the orphan phosphatase PHOSPHO1 gene.";
RL Anim. Genet. 33:451-454(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=18471996; DOI=10.1016/j.bbrc.2008.04.163;
RA Roberts S.J., Owen H.C., Farquharson C.;
RT "Identification of a novel splice variant of the haloacid
RT dehalogenase: PHOSPHO1.";
RL Biochem. Biophys. Res. Commun. 371:872-876(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-111 (ISOFORM 3).
RC TISSUE=Colon, and Medulla oblongata;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ENZYME ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15175005; DOI=10.1042/BJ20040511;
RA Roberts S.J., Stewart A.J., Sadler P.J., Farquharson C.;
RT "Human PHOSPHO1 exhibits high specific phosphoethanolamine and
RT phosphocholine phosphatase activities.";
RL Biochem. J. 382:59-65(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15050893; DOI=10.1016/j.bone.2003.12.023;
RA Houston B., Stewart A.J., Farquharson C.;
RT "PHOSPHO1 -- a novel phosphatase specifically expressed at sites of
RT mineralisation in bone and cartilage.";
RL Bone 34:629-637(2004).
RN [7]
RP SIMILARITY TO HAD-LIKE HYDROLASE SUPERFAMILY.
RX PubMed=14983068; DOI=10.1093/protein/gzg126;
RA Stewart A.J., Schmid R., Blindauer C.A., Paisey S.J., Farquharson C.;
RT "Comparative modelling of human PHOSPHO1 reveals a new group of
RT phosphatases within the haloacid dehalogenase superfamily.";
RL Protein Eng. 16:889-895(2003).
RN [8]
RP MUTAGENESIS OF ASP-32; ASP-43; ASP-123 AND ASP-203.
RX PubMed=16054448; DOI=10.1016/j.bbapap.2005.06.009;
RA Roberts S.J., Stewart A.J., Schmid R., Blindauer C.A., Bond S.R.,
RA Sadler P.J., Farquharson C.;
RT "Probing the substrate specificities of human PHOSPHO1 and PHOSPHO2.";
RL Biochim. Biophys. Acta 1752:73-82(2005).
CC -!- FUNCTION: Phosphatase that has a high activity toward
CC phosphoethanolamine (PEA) and phosphocholine (PCho). Involved in
CC the generation of inorganic phosphate for bone mineralization.
CC -!- CATALYTIC ACTIVITY: O-phosphoethanolamine + H(2)O = ethanolamine +
CC phosphate.
CC -!- CATALYTIC ACTIVITY: Phosphocholine + H(2)O = choline + phosphate.
CC -!- COFACTOR: Magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for PEA;
CC KM=11.4 uM for PCho;
CC pH dependence:
CC Optimum pH is 6.7;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TCT1-1; Sequence=Displayed;
CC Name=2; Synonyms=PHOSPHO1-3a;
CC IsoId=Q8TCT1-2; Sequence=VSP_040624;
CC Name=3;
CC IsoId=Q8TCT1-3; Sequence=VSP_045709;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed at sites of mineralization in bone
CC and cartilage. Highly expressed in osteoblast cell line SaOS-2
CC which produces a mineralized matrix, but not in MG-63 cell line,
CC which do not mineralize.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ457189; CAD29803.1; -; mRNA.
DR EMBL; AC004797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029931; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC117187; AAI17188.1; -; mRNA.
DR RefSeq; NP_001137276.1; NM_001143804.1.
DR RefSeq; NP_848595.1; NM_178500.3.
DR RefSeq; XP_005257164.1; XM_005257107.1.
DR RefSeq; XP_005257165.1; XM_005257108.1.
DR RefSeq; XP_005257166.1; XM_005257109.1.
DR UniGene; Hs.405607; -.
DR ProteinModelPortal; Q8TCT1; -.
DR STRING; 9606.ENSP00000406909; -.
DR ChEMBL; CHEMBL6113; -.
DR DrugBank; DB00122; Choline.
DR PhosphoSite; Q8TCT1; -.
DR DMDM; 74715842; -.
DR PaxDb; Q8TCT1; -.
DR PRIDE; Q8TCT1; -.
DR Ensembl; ENST00000310544; ENSP00000311925; ENSG00000173868.
DR Ensembl; ENST00000413580; ENSP00000406909; ENSG00000173868.
DR Ensembl; ENST00000514112; ENSP00000427694; ENSG00000173868.
DR GeneID; 162466; -.
DR KEGG; hsa:162466; -.
DR UCSC; uc002ios.2; human.
DR CTD; 162466; -.
DR GeneCards; GC17M047300; -.
DR HGNC; HGNC:16815; PHOSPHO1.
DR HPA; HPA053016; -.
DR neXtProt; NX_Q8TCT1; -.
DR PharmGKB; PA33276; -.
DR eggNOG; NOG331523; -.
DR HOGENOM; HOG000231038; -.
DR HOVERGEN; HBG080058; -.
DR InParanoid; Q8TCT1; -.
DR KO; K06124; -.
DR OMA; ARCPANM; -.
DR OrthoDB; EOG7BZVTZ; -.
DR PhylomeDB; Q8TCT1; -.
DR BioCyc; MetaCyc:HS16266-MONOMER; -.
DR BRENDA; 3.1.3.75; 2681.
DR Reactome; REACT_111217; Metabolism.
DR GenomeRNAi; 162466; -.
DR NextBio; 88177; -.
DR PRO; PR:Q8TCT1; -.
DR ArrayExpress; Q8TCT1; -.
DR Bgee; Q8TCT1; -.
DR CleanEx; HS_PHOSPHO1; -.
DR Genevestigator; Q8TCT1; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052731; F:phosphocholine phosphatase activity; EXP:Reactome.
DR GO; GO:0052732; F:phosphoethanolamine phosphatase activity; EXP:Reactome.
DR GO; GO:0016462; F:pyrophosphatase activity; IDA:MGI.
DR GO; GO:0035630; P:bone mineralization involved in bone maturation; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; TAS:Reactome.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR006383; HAD-SF_hydro_IB_PSP-like.
DR InterPro; IPR016965; Pase_PHOSPHO-typ.
DR InterPro; IPR006384; PyrdxlP_Pase-rel.
DR Pfam; PF06888; Put_Phosphatase; 1.
DR PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
DR TIGRFAMs; TIGR01488; HAD-SF-IB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Hydrolase; Magnesium;
KW Metal-binding; Mineral balance; Reference proteome.
FT CHAIN 1 267 Phosphoethanolamine/phosphocholine
FT phosphatase.
FT /FTId=PRO_0000068829.
FT ACT_SITE 32 32 Nucleophile (Probable).
FT ACT_SITE 34 34 Proton donor (By similarity).
FT METAL 32 32 Magnesium (Probable).
FT METAL 34 34 Magnesium (By similarity).
FT METAL 203 203 Magnesium (Probable).
FT BINDING 43 43 Substrate (Probable).
FT BINDING 123 123 Substrate (Probable).
FT VAR_SEQ 1 15 MSGCFPVSGLRCLSR -> MCQRLWPANQPLPGGLLPRPLS
FT LAPSSSSSCCSPPCSQ (in isoform 2).
FT /FTId=VSP_040624.
FT VAR_SEQ 1 15 MSGCFPVSGLRCLSR -> MCQRLWPWPANQPLPGGLLPRP
FT LSLAPSSSSSCCSPPCSQ (in isoform 3).
FT /FTId=VSP_045709.
FT MUTAGEN 32 32 D->N: Abolishes phosphatase activity.
FT MUTAGEN 43 43 D->N: Strongly reduces reactivity toward
FT PEA and PCho substrates. Abolishes
FT phosphatase activity; when associated
FT with N-123.
FT MUTAGEN 123 123 D->N: Strongly reduces reactivity toward
FT PEA and PCho substrates. Abolishes
FT phosphatase activity; when associated
FT with N-43.
FT MUTAGEN 203 203 D->S: Abolishes phosphatase activity.
SQ SEQUENCE 267 AA; 29713 MW; 539F65C749D39E81 CRC64;
MSGCFPVSGL RCLSRDGRMA AQGAPRFLLT FDFDETIVDE NSDDSIVRAA PGQRLPESLR
ATYREGFYNE YMQRVFKYLG EQGVRPRDLS AIYEAIPLSP GMSDLLQFVA KQGACFEVIL
ISDANTFGVE SSLRAAGHHS LFRRILSNPS GPDARGLLAL RPFHTHSCAR CPANMCKHKV
LSDYLRERAH DGVHFERLFY VGDGANDFCP MGLLAGGDVA FPRRGYPMHR LIQEAQKAEP
SSFRASVVPW ETAADVRLHL QQVLKSC
//
ID PHOP1_HUMAN Reviewed; 267 AA.
AC Q8TCT1; E9PAM0; Q17RU6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2002, sequence version 1.
DT 22-JAN-2014, entry version 85.
DE RecName: Full=Phosphoethanolamine/phosphocholine phosphatase;
DE EC=3.1.3.75;
GN Name=PHOSPHO1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12464021; DOI=10.1046/j.1365-2052.2002.00900.x;
RA Houston B., Paton I.R., Burt D.W., Farquharson C.;
RT "Chromosomal localization of the chicken and mammalian orthologues of
RT the orphan phosphatase PHOSPHO1 gene.";
RL Anim. Genet. 33:451-454(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=18471996; DOI=10.1016/j.bbrc.2008.04.163;
RA Roberts S.J., Owen H.C., Farquharson C.;
RT "Identification of a novel splice variant of the haloacid
RT dehalogenase: PHOSPHO1.";
RL Biochem. Biophys. Res. Commun. 371:872-876(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-111 (ISOFORM 3).
RC TISSUE=Colon, and Medulla oblongata;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ENZYME ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15175005; DOI=10.1042/BJ20040511;
RA Roberts S.J., Stewart A.J., Sadler P.J., Farquharson C.;
RT "Human PHOSPHO1 exhibits high specific phosphoethanolamine and
RT phosphocholine phosphatase activities.";
RL Biochem. J. 382:59-65(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15050893; DOI=10.1016/j.bone.2003.12.023;
RA Houston B., Stewart A.J., Farquharson C.;
RT "PHOSPHO1 -- a novel phosphatase specifically expressed at sites of
RT mineralisation in bone and cartilage.";
RL Bone 34:629-637(2004).
RN [7]
RP SIMILARITY TO HAD-LIKE HYDROLASE SUPERFAMILY.
RX PubMed=14983068; DOI=10.1093/protein/gzg126;
RA Stewart A.J., Schmid R., Blindauer C.A., Paisey S.J., Farquharson C.;
RT "Comparative modelling of human PHOSPHO1 reveals a new group of
RT phosphatases within the haloacid dehalogenase superfamily.";
RL Protein Eng. 16:889-895(2003).
RN [8]
RP MUTAGENESIS OF ASP-32; ASP-43; ASP-123 AND ASP-203.
RX PubMed=16054448; DOI=10.1016/j.bbapap.2005.06.009;
RA Roberts S.J., Stewart A.J., Schmid R., Blindauer C.A., Bond S.R.,
RA Sadler P.J., Farquharson C.;
RT "Probing the substrate specificities of human PHOSPHO1 and PHOSPHO2.";
RL Biochim. Biophys. Acta 1752:73-82(2005).
CC -!- FUNCTION: Phosphatase that has a high activity toward
CC phosphoethanolamine (PEA) and phosphocholine (PCho). Involved in
CC the generation of inorganic phosphate for bone mineralization.
CC -!- CATALYTIC ACTIVITY: O-phosphoethanolamine + H(2)O = ethanolamine +
CC phosphate.
CC -!- CATALYTIC ACTIVITY: Phosphocholine + H(2)O = choline + phosphate.
CC -!- COFACTOR: Magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for PEA;
CC KM=11.4 uM for PCho;
CC pH dependence:
CC Optimum pH is 6.7;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TCT1-1; Sequence=Displayed;
CC Name=2; Synonyms=PHOSPHO1-3a;
CC IsoId=Q8TCT1-2; Sequence=VSP_040624;
CC Name=3;
CC IsoId=Q8TCT1-3; Sequence=VSP_045709;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed at sites of mineralization in bone
CC and cartilage. Highly expressed in osteoblast cell line SaOS-2
CC which produces a mineralized matrix, but not in MG-63 cell line,
CC which do not mineralize.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ457189; CAD29803.1; -; mRNA.
DR EMBL; AC004797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029931; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC117187; AAI17188.1; -; mRNA.
DR RefSeq; NP_001137276.1; NM_001143804.1.
DR RefSeq; NP_848595.1; NM_178500.3.
DR RefSeq; XP_005257164.1; XM_005257107.1.
DR RefSeq; XP_005257165.1; XM_005257108.1.
DR RefSeq; XP_005257166.1; XM_005257109.1.
DR UniGene; Hs.405607; -.
DR ProteinModelPortal; Q8TCT1; -.
DR STRING; 9606.ENSP00000406909; -.
DR ChEMBL; CHEMBL6113; -.
DR DrugBank; DB00122; Choline.
DR PhosphoSite; Q8TCT1; -.
DR DMDM; 74715842; -.
DR PaxDb; Q8TCT1; -.
DR PRIDE; Q8TCT1; -.
DR Ensembl; ENST00000310544; ENSP00000311925; ENSG00000173868.
DR Ensembl; ENST00000413580; ENSP00000406909; ENSG00000173868.
DR Ensembl; ENST00000514112; ENSP00000427694; ENSG00000173868.
DR GeneID; 162466; -.
DR KEGG; hsa:162466; -.
DR UCSC; uc002ios.2; human.
DR CTD; 162466; -.
DR GeneCards; GC17M047300; -.
DR HGNC; HGNC:16815; PHOSPHO1.
DR HPA; HPA053016; -.
DR neXtProt; NX_Q8TCT1; -.
DR PharmGKB; PA33276; -.
DR eggNOG; NOG331523; -.
DR HOGENOM; HOG000231038; -.
DR HOVERGEN; HBG080058; -.
DR InParanoid; Q8TCT1; -.
DR KO; K06124; -.
DR OMA; ARCPANM; -.
DR OrthoDB; EOG7BZVTZ; -.
DR PhylomeDB; Q8TCT1; -.
DR BioCyc; MetaCyc:HS16266-MONOMER; -.
DR BRENDA; 3.1.3.75; 2681.
DR Reactome; REACT_111217; Metabolism.
DR GenomeRNAi; 162466; -.
DR NextBio; 88177; -.
DR PRO; PR:Q8TCT1; -.
DR ArrayExpress; Q8TCT1; -.
DR Bgee; Q8TCT1; -.
DR CleanEx; HS_PHOSPHO1; -.
DR Genevestigator; Q8TCT1; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052731; F:phosphocholine phosphatase activity; EXP:Reactome.
DR GO; GO:0052732; F:phosphoethanolamine phosphatase activity; EXP:Reactome.
DR GO; GO:0016462; F:pyrophosphatase activity; IDA:MGI.
DR GO; GO:0035630; P:bone mineralization involved in bone maturation; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; TAS:Reactome.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR006383; HAD-SF_hydro_IB_PSP-like.
DR InterPro; IPR016965; Pase_PHOSPHO-typ.
DR InterPro; IPR006384; PyrdxlP_Pase-rel.
DR Pfam; PF06888; Put_Phosphatase; 1.
DR PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
DR TIGRFAMs; TIGR01488; HAD-SF-IB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Hydrolase; Magnesium;
KW Metal-binding; Mineral balance; Reference proteome.
FT CHAIN 1 267 Phosphoethanolamine/phosphocholine
FT phosphatase.
FT /FTId=PRO_0000068829.
FT ACT_SITE 32 32 Nucleophile (Probable).
FT ACT_SITE 34 34 Proton donor (By similarity).
FT METAL 32 32 Magnesium (Probable).
FT METAL 34 34 Magnesium (By similarity).
FT METAL 203 203 Magnesium (Probable).
FT BINDING 43 43 Substrate (Probable).
FT BINDING 123 123 Substrate (Probable).
FT VAR_SEQ 1 15 MSGCFPVSGLRCLSR -> MCQRLWPANQPLPGGLLPRPLS
FT LAPSSSSSCCSPPCSQ (in isoform 2).
FT /FTId=VSP_040624.
FT VAR_SEQ 1 15 MSGCFPVSGLRCLSR -> MCQRLWPWPANQPLPGGLLPRP
FT LSLAPSSSSSCCSPPCSQ (in isoform 3).
FT /FTId=VSP_045709.
FT MUTAGEN 32 32 D->N: Abolishes phosphatase activity.
FT MUTAGEN 43 43 D->N: Strongly reduces reactivity toward
FT PEA and PCho substrates. Abolishes
FT phosphatase activity; when associated
FT with N-123.
FT MUTAGEN 123 123 D->N: Strongly reduces reactivity toward
FT PEA and PCho substrates. Abolishes
FT phosphatase activity; when associated
FT with N-43.
FT MUTAGEN 203 203 D->S: Abolishes phosphatase activity.
SQ SEQUENCE 267 AA; 29713 MW; 539F65C749D39E81 CRC64;
MSGCFPVSGL RCLSRDGRMA AQGAPRFLLT FDFDETIVDE NSDDSIVRAA PGQRLPESLR
ATYREGFYNE YMQRVFKYLG EQGVRPRDLS AIYEAIPLSP GMSDLLQFVA KQGACFEVIL
ISDANTFGVE SSLRAAGHHS LFRRILSNPS GPDARGLLAL RPFHTHSCAR CPANMCKHKV
LSDYLRERAH DGVHFERLFY VGDGANDFCP MGLLAGGDVA FPRRGYPMHR LIQEAQKAEP
SSFRASVVPW ETAADVRLHL QQVLKSC
//