ID   MPPD2_HUMAN             Reviewed;         294 AA.
AC   Q15777; D3DQZ5; E9PB10; Q59GE6;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 173.
DE   RecName: Full=Metallophosphoesterase MPPED2;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:B1WBP0};
DE   AltName: Full=Fetal brain protein 239;
DE            Short=239FB;
DE   AltName: Full=Metallophosphoesterase domain-containing protein 2;
GN   Name=MPPED2; Synonyms=C11orf8, FAM1B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=7527372; DOI=10.1007/bf00206960;
RA   Schwartz F., Neve R., Eisenman R., Gessler M., Bruns G.;
RT   "A WAGR region gene between PAX-6 and FSHB expressed in fetal brain.";
RL   Hum. Genet. 94:658-664(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8666403; DOI=10.1006/geno.1995.9973;
RA   Schwartz F., Eisenman R., Knoll J., Gessler M., Bruns G.;
RT   "cDNA sequence, genomic organization, and evolutionary conservation of a
RT   novel gene from the WAGR region.";
RL   Genomics 29:526-532(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon, Kidney, and Stomach;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   -!- INTERACTION:
CC       Q15777; Q9NWD9: BEX4; NbExp=3; IntAct=EBI-2350461, EBI-15105944;
CC       Q15777; Q8TC20: CAGE1; NbExp=3; IntAct=EBI-2350461, EBI-10196469;
CC       Q15777; Q8TC20-4: CAGE1; NbExp=3; IntAct=EBI-2350461, EBI-11522698;
CC       Q15777; Q5TYM5: FAM72A; NbExp=3; IntAct=EBI-2350461, EBI-10237116;
CC       Q15777; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-2350461, EBI-10961706;
CC       Q15777; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-2350461, EBI-12516603;
CC       Q15777; Q8N1F7: NUP93; NbExp=3; IntAct=EBI-2350461, EBI-1042703;
CC       Q15777; Q9Y244: POMP; NbExp=3; IntAct=EBI-2350461, EBI-696895;
CC       Q15777; Q8N443: RIBC1; NbExp=3; IntAct=EBI-2350461, EBI-10265323;
CC       Q15777; P48443: RXRG; NbExp=6; IntAct=EBI-2350461, EBI-712405;
CC       Q15777; Q15645: TRIP13; NbExp=8; IntAct=EBI-2350461, EBI-358993;
CC       Q15777; Q08AM6: VAC14; NbExp=6; IntAct=EBI-2350461, EBI-2107455;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q15777-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15777-2; Sequence=VSP_045627;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in fetal brain.
CC   -!- SIMILARITY: Belongs to the UPF0046 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92400.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U57911; AAC50564.1; -; mRNA.
DR   EMBL; AB209163; BAD92400.1; ALT_INIT; mRNA.
DR   EMBL; AL136088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL356240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471064; EAW68256.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68257.1; -; Genomic_DNA.
DR   EMBL; BC031582; AAH31582.1; -; mRNA.
DR   CCDS; CCDS44560.1; -. [Q15777-2]
DR   CCDS; CCDS7870.1; -. [Q15777-1]
DR   RefSeq; NP_001138871.1; NM_001145399.1. [Q15777-2]
DR   RefSeq; NP_001575.1; NM_001584.2. [Q15777-1]
DR   RefSeq; XP_005253167.1; XM_005253110.3.
DR   RefSeq; XP_005253168.1; XM_005253111.2. [Q15777-1]
DR   RefSeq; XP_005253169.1; XM_005253112.1.
DR   RefSeq; XP_016873721.1; XM_017018232.1.
DR   AlphaFoldDB; Q15777; -.
DR   SMR; Q15777; -.
DR   BioGRID; 107202; 20.
DR   IntAct; Q15777; 15.
DR   MINT; Q15777; -.
DR   STRING; 9606.ENSP00000350833; -.
DR   PhosphoSitePlus; Q15777; -.
DR   BioMuta; MPPED2; -.
DR   DMDM; 3023214; -.
DR   EPD; Q15777; -.
DR   MassIVE; Q15777; -.
DR   MaxQB; Q15777; -.
DR   PaxDb; 9606-ENSP00000350833; -.
DR   PeptideAtlas; Q15777; -.
DR   ProteomicsDB; 19118; -.
DR   ProteomicsDB; 60757; -. [Q15777-1]
DR   Pumba; Q15777; -.
DR   Antibodypedia; 12780; 214 antibodies from 24 providers.
DR   DNASU; 744; -.
DR   Ensembl; ENST00000358117.10; ENSP00000350833.4; ENSG00000066382.17. [Q15777-1]
DR   Ensembl; ENST00000448418.6; ENSP00000388258.2; ENSG00000066382.17. [Q15777-2]
DR   GeneID; 744; -.
DR   KEGG; hsa:744; -.
DR   MANE-Select; ENST00000358117.10; ENSP00000350833.4; NM_001584.3; NP_001575.1.
DR   UCSC; uc001msq.4; human. [Q15777-1]
DR   AGR; HGNC:1180; -.
DR   CTD; 744; -.
DR   DisGeNET; 744; -.
DR   GeneCards; MPPED2; -.
DR   HGNC; HGNC:1180; MPPED2.
DR   HPA; ENSG00000066382; Tissue enhanced (cervix, thyroid gland).
DR   MIM; 600911; gene.
DR   neXtProt; NX_Q15777; -.
DR   OpenTargets; ENSG00000066382; -.
DR   PharmGKB; PA25499; -.
DR   VEuPathDB; HostDB:ENSG00000066382; -.
DR   eggNOG; KOG3947; Eukaryota.
DR   GeneTree; ENSGT00390000007681; -.
DR   HOGENOM; CLU_041441_1_0_1; -.
DR   InParanoid; Q15777; -.
DR   OMA; NIPTLGM; -.
DR   OrthoDB; 5471007at2759; -.
DR   PhylomeDB; Q15777; -.
DR   TreeFam; TF314305; -.
DR   PathwayCommons; Q15777; -.
DR   SignaLink; Q15777; -.
DR   BioGRID-ORCS; 744; 14 hits in 1145 CRISPR screens.
DR   ChiTaRS; MPPED2; human.
DR   GenomeRNAi; 744; -.
DR   Pharos; Q15777; Tbio.
DR   PRO; PR:Q15777; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q15777; Protein.
DR   Bgee; ENSG00000066382; Expressed in ventricular zone and 180 other cell types or tissues.
DR   ExpressionAtlas; Q15777; baseline and differential.
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   CDD; cd07379; MPP_239FB; 1.
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   PANTHER; PTHR12905; METALLOPHOSPHOESTERASE; 1.
DR   PANTHER; PTHR12905:SF13; METALLOPHOSPHOESTERASE MPPED2; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF035808; Pdiesterase_Brain_239; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   Genevisible; Q15777; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cobalt; Hydrolase; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..294
FT                   /note="Metallophosphoesterase MPPED2"
FT                   /id="PRO_0000053405"
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"
FT   VAR_SEQ         256..294
FT                   /note="GYGIMTDGYTTYINASTCTVSFQPTNPPIIFDLPNPQGS -> VNPVSISKA
FT                   LRTKICSLPSKTS (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_045627"
FT   VARIANT         67
FT                   /note="H -> R (in dbSNP:rs11556749)"
FT                   /id="VAR_052487"
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
//