ID   MPPD2_PONAB             Reviewed;         294 AA.
AC   Q5REB1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Metallophosphoesterase MPPED2;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:B1WBP0};
DE   AltName: Full=Metallophosphoesterase domain-containing protein 2;
GN   Name=MPPED2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Displays low metallophosphoesterase activity (in vitro). May
CC       play a role in the development of the nervous system.
CC       {ECO:0000250|UniProtKB:B1WBP0}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:B1WBP0};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000250|UniProtKB:B1WBP0};
CC   -!- ACTIVITY REGULATION: Inhibited by nmolar levels of AMP and GMP.
CC       {ECO:0000250|UniProtKB:B1WBP0}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:B1WBP0}.
CC   -!- SIMILARITY: Belongs to the UPF0046 family. {ECO:0000305}.
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DR   EMBL; CR857621; CAH89896.1; -; mRNA.
DR   RefSeq; NP_001124887.1; NM_001131415.1.
DR   RefSeq; XP_009244782.1; XM_009246507.1.
DR   AlphaFoldDB; Q5REB1; -.
DR   SMR; Q5REB1; -.
DR   STRING; 9601.ENSPPYP00000003897; -.
DR   Ensembl; ENSPPYT00000004045; ENSPPYP00000003897; ENSPPYG00000003395.
DR   GeneID; 100171752; -.
DR   KEGG; pon:100171752; -.
DR   CTD; 744; -.
DR   eggNOG; KOG3947; Eukaryota.
DR   GeneTree; ENSGT00390000007681; -.
DR   HOGENOM; CLU_041441_1_0_1; -.
DR   InParanoid; Q5REB1; -.
DR   OMA; HYLEYES; -.
DR   OrthoDB; 1301937at2759; -.
DR   TreeFam; TF314305; -.
DR   Proteomes; UP000001595; Chromosome 11.
DR   GO; GO:0016208; F:AMP binding; ISS:UniProtKB.
DR   GO; GO:0019002; F:GMP binding; ISS:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; ISS:UniProtKB.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR024201; Calcineurin-like_Pesterase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF035808; Pdiesterase_Brain_239; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   2: Evidence at transcript level;
KW   Cobalt; Hydrolase; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..294
FT                   /note="Metallophosphoesterase MPPED2"
FT                   /id="PRO_0000053407"
FT   BINDING         65
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:B1WBP0"
FT   BINDING         67
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:B1WBP0"
FT   BINDING         86
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:B1WBP0"
FT   BINDING         86
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B1WBP0"
FT   BINDING         117..118
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:B1WBP0"
FT   BINDING         117
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B1WBP0"
FT   BINDING         213
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B1WBP0"
FT   BINDING         225..226
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:B1WBP0"
FT   BINDING         252..255
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:B1WBP0"
FT   BINDING         254
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:B1WBP0"
SQ   SEQUENCE   294 AA;  33360 MW;  43B2BC0DA1BFD1F0 CRC64;
     MAHGIPSQGK VTITVDEYSS NPTQAFTHYN INQSRFQPPH VHMVDPIPYD TPKPAGHTRF
     VCISDTHSRT DGIQMPYGDI LLHTGDFTEL GLPSEVKKFN DWLGNLPYEY KIVIAGNHEL
     TFDKEFMADL VKQDYYRFPS VSKLKPEDFD NVQSLLTNSI YLQDSEVTVK GFRIYGAPWT
     PWFNGWGFNL PRGQSLLDKW NLIPEGIDIL MTHGPPLGFR DWVPKELQRV GCVELLNTVQ
     RRVRPKLHVF GGIHEGYGIM TDGYTTYINA STCTVSFQPT NPPIIFDLPN PQGS