PHOP1_CHICK
ID PHOP1_CHICK Reviewed; 268 AA.
AC O73884;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phosphoethanolamine/phosphocholine phosphatase;
DE EC=3.1.3.75 {ECO:0000250|UniProtKB:Q8TCT1};
DE AltName: Full=3X11A;
GN Name=PHOSPHO1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9990301; DOI=10.1016/s0167-4889(98)00153-0;
RA Houston B., Seawright E., Jefferies D., Hoogland E., Lester D.,
RA Whitehead C., Farquharson C.;
RT "Identification and cloning of a novel phosphatase expressed at high levels
RT in differentiating growth plate chondrocytes.";
RL Biochim. Biophys. Acta 1448:500-506(1999).
RN [2]
RP FUNCTION, AND 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).
CC -!- FUNCTION: Phosphatase that has a high activity toward
CC phosphoethanolamine (PEA) and phosphocholine (PCho) (By similarity).
CC Involved in the generation of inorganic phosphate for bone
CC mineralization (PubMed:15050893). {ECO:0000250|UniProtKB:Q8TCT1,
CC ECO:0000269|PubMed:15050893}.
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 -!- TISSUE SPECIFICITY: Expressed at sites of mineralization in bone and
CC cartilage. Highly expressed in hypertrophic chondrocytes compared to
CC non-chondrogenic tissues. Expressed in chondrocytes but not in heart,
CC liver, lung, kidney, spleen, muscle, adipose tissues not duodenum. In
CC diaphyseal cortical bone, it is expressed in the osteoid layer of the
CC periosteum, forming surfaces of growing osteons, and newly formed
CC osteocytes, whereas it is not expressed in the endosteum and closed
CC osteons. In growth plate cartilage, it is limited to the early
CC hypertrophic chondrocytes and the ossification groove of Ranvier.
CC Highly expressed on the mineralization surfaces of the cartilage
CC remnants and trabecular bone within the primary spongiosa. Expressed in
CC 17-day-old embryonic calvaria, the osteoid present on the
CC intramembranous and periosteal bone surfaces but not in soft tissues
CC examined. {ECO:0000269|PubMed:15050893, ECO:0000269|PubMed:9990301}.
CC -!- INDUCTION: Up-regulated 5-fold during chondrocyte terminal
CC differentiation. {ECO:0000269|PubMed:9990301}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO
CC family. {ECO:0000305}.
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DR EMBL; AJ006529; CAA07090.1; -; mRNA.
DR RefSeq; NP_990176.1; NM_204845.2.
DR AlphaFoldDB; O73884; -.
DR STRING; 9031.ENSGALP00000001955; -.
DR PaxDb; O73884; -.
DR GeneID; 395650; -.
DR KEGG; gga:395650; -.
DR CTD; 162466; -.
DR VEuPathDB; HostDB:geneid_395650; -.
DR eggNOG; KOG3120; Eukaryota.
DR InParanoid; O73884; -.
DR OrthoDB; 1454608at2759; -.
DR PhylomeDB; O73884; -.
DR BRENDA; 3.1.3.75; 1306.
DR PRO; PR:O73884; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0065010; C:extracellular membrane-bounded organelle; IDA:MGI.
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:0035630; P:bone mineralization involved in bone maturation; IBA:GO_Central.
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..268
FT /note="Phosphoethanolamine/phosphocholine phosphatase"
FT /id="PRO_0000068831"
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT ACT_SITE 34
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
SQ SEQUENCE 268 AA; 30443 MW; 68852F21D9EE0024 CRC64;
MKRCCEGVGL PCLFKGVGMA SSRPPKYLLV FDFDGTIINE SSDDSIVRAA PGQALPEHIR
QSFREGFYNE YMQRVLAYMG DQGVKMGDFK AVYENIPLSP GMPDLFQFLS KNHELFEIIL
ISDANMFGIE CKLRAAGFYS LFRKIFSNPS SFDKRGYFTL GPYHSHKCLD CPANTCKRKI
LTEYLAERAQ EEVEFERVFY VGDGANDFCP SVTLTSADVA FPRKGYPMHQ MTQEMEKKQP
GTFQATVVPW ESATEVARYL QELLKKKC
