MPPD2_MOUSE
ID MPPD2_MOUSE Reviewed; 294 AA.
AC Q9CZJ0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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; AK012553; BAB28313.1; -; mRNA.
DR CCDS; CCDS50654.1; -.
DR RefSeq; NP_001137155.1; NM_001143683.1.
DR RefSeq; NP_084113.1; NM_029837.1.
DR RefSeq; XP_011238143.1; XM_011239841.1.
DR AlphaFoldDB; Q9CZJ0; -.
DR SMR; Q9CZJ0; -.
DR STRING; 10090.ENSMUSP00000106692; -.
DR iPTMnet; Q9CZJ0; -.
DR PhosphoSitePlus; Q9CZJ0; -.
DR MaxQB; Q9CZJ0; -.
DR PaxDb; Q9CZJ0; -.
DR PRIDE; Q9CZJ0; -.
DR ProteomicsDB; 291438; -.
DR Antibodypedia; 12780; 201 antibodies from 24 providers.
DR Ensembl; ENSMUST00000016530; ENSMUSP00000016530; ENSMUSG00000016386.
DR Ensembl; ENSMUST00000111063; ENSMUSP00000106692; ENSMUSG00000016386.
DR GeneID; 77015; -.
DR KEGG; mmu:77015; -.
DR UCSC; uc008llm.2; mouse.
DR CTD; 744; -.
DR MGI; MGI:1924265; Mpped2.
DR VEuPathDB; HostDB:ENSMUSG00000016386; -.
DR eggNOG; KOG3947; Eukaryota.
DR GeneTree; ENSGT00390000007681; -.
DR InParanoid; Q9CZJ0; -.
DR OMA; HYLEYES; -.
DR OrthoDB; 1301937at2759; -.
DR PhylomeDB; Q9CZJ0; -.
DR TreeFam; TF314305; -.
DR BioGRID-ORCS; 77015; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Mpped2; mouse.
DR PRO; PR:Q9CZJ0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CZJ0; protein.
DR Bgee; ENSMUSG00000016386; Expressed in rostral migratory stream and 209 other tissues.
DR ExpressionAtlas; Q9CZJ0; baseline and differential.
DR Genevisible; Q9CZJ0; MM.
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_0000053406"
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; 33374 MW; 43B2BC1AAAD27020 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
RRIRPKLHVF GGIHEGYGIM TDGYTTYINA STCTVSFQPT NPPIIFDLPN PQGS
