MAOX_MOUSE
ID MAOX_MOUSE Reviewed; 572 AA.
AC P06801; Q9DBF9;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=NADP-dependent malic enzyme;
DE Short=NADP-ME;
DE EC=1.1.1.40 {ECO:0000250|UniProtKB:P48163};
DE AltName: Full=Malic enzyme 1;
GN Name=Me1; Synonyms=Mod-1, Mod1;
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 [MRNA].
RX PubMed=3805042; DOI=10.1016/s0021-9258(19)75671-3;
RA Bagchi S., Wise L.S., Brown M.L., Bregman D., Sul H.S., Rubin C.S.;
RT "Structure and expression of murine malic enzyme mRNA. Differentiation-
RT dependent accumulation of two forms of malic enzyme mRNA in 3T3-L1 cells.";
RL J. Biol. Chem. 262:1558-1565(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=3541755; DOI=10.1111/j.1749-6632.1986.tb15522.x;
RA Bagchi S., Wise L.S., Brown M.L., Sul H.S., Bregman D.B., Rubin C.S.;
RT "Regulation and structure of murine malic enzyme mRNA.";
RL Ann. N. Y. Acad. Sci. 478:77-92(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Testis;
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).
RN [4]
RP PROTEIN SEQUENCE OF 428-445, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of (S)-malate in the
CC presence of NADP(+) and divalent metal ions, and decarboxylation of
CC oxaloacetate. {ECO:0000250|UniProtKB:P48163}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate;
CC Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40;
CC Evidence={ECO:0000250|UniProtKB:P48163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18254;
CC Evidence={ECO:0000250|UniProtKB:P48163};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18255;
CC Evidence={ECO:0000250|UniProtKB:P48163};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526; EC=1.1.1.40;
CC Evidence={ECO:0000250|UniProtKB:P48163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15642;
CC Evidence={ECO:0000250|UniProtKB:P48163};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P48163};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P48163};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000250|UniProtKB:P48163};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P48163}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48163}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; J02652; AAA39727.1; -; mRNA.
DR EMBL; M26756; AAA39489.1; -; mRNA.
DR EMBL; AK004980; BAB23716.1; -; mRNA.
DR EMBL; AK077968; BAC37086.1; -; mRNA.
DR CCDS; CCDS23383.1; -.
DR PIR; A26683; DEMSMX.
DR RefSeq; NP_001185862.1; NM_001198933.1.
DR RefSeq; NP_032641.2; NM_008615.2.
DR AlphaFoldDB; P06801; -.
DR SMR; P06801; -.
DR BioGRID; 201464; 6.
DR IntAct; P06801; 2.
DR MINT; P06801; -.
DR STRING; 10090.ENSMUSP00000034989; -.
DR iPTMnet; P06801; -.
DR MetOSite; P06801; -.
DR PhosphoSitePlus; P06801; -.
DR REPRODUCTION-2DPAGE; P06801; -.
DR SWISS-2DPAGE; P06801; -.
DR CPTAC; non-CPTAC-3724; -.
DR EPD; P06801; -.
DR jPOST; P06801; -.
DR MaxQB; P06801; -.
DR PaxDb; P06801; -.
DR PeptideAtlas; P06801; -.
DR PRIDE; P06801; -.
DR ProteomicsDB; 252726; -.
DR Antibodypedia; 1633; 379 antibodies from 32 providers.
DR DNASU; 17436; -.
DR Ensembl; ENSMUST00000034989; ENSMUSP00000034989; ENSMUSG00000032418.
DR GeneID; 17436; -.
DR KEGG; mmu:17436; -.
DR UCSC; uc009qxs.2; mouse.
DR CTD; 4199; -.
DR MGI; MGI:97043; Me1.
DR VEuPathDB; HostDB:ENSMUSG00000032418; -.
DR eggNOG; KOG1257; Eukaryota.
DR GeneTree; ENSGT00950000183134; -.
DR HOGENOM; CLU_011405_5_2_1; -.
DR InParanoid; P06801; -.
DR OMA; GDACLQY; -.
DR OrthoDB; 435571at2759; -.
DR PhylomeDB; P06801; -.
DR TreeFam; TF300537; -.
DR BRENDA; 1.1.1.40; 3474.
DR Reactome; R-MMU-70268; Pyruvate metabolism.
DR BioGRID-ORCS; 17436; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Me1; mouse.
DR PRO; PR:P06801; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P06801; protein.
DR Bgee; ENSMUSG00000032418; Expressed in gonadal fat pad and 248 other tissues.
DR ExpressionAtlas; P06801; baseline and differential.
DR Genevisible; P06801; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IDA:MGI.
DR GO; GO:0004470; F:malic enzyme activity; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; ISO:MGI.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0006108; P:malate metabolic process; ISS:UniProtKB.
DR GO; GO:0006734; P:NADH metabolic process; ISO:MGI.
DR GO; GO:0006739; P:NADP metabolic process; ISO:MGI.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR GO; GO:1902031; P:regulation of NADP metabolic process; ISO:MGI.
DR GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
DR Gene3D; 3.40.50.10380; -; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR015884; Malic_enzyme_CS.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..572
FT /note="NADP-dependent malic enzyme"
FT /id="PRO_0000160193"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 246
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 269
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P23368"
FT BINDING 269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 301..318
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 269
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P48163"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 408
FT /note="N -> S (in Ref. 1; AAA39727 and 2; AAA39489)"
FT /evidence="ECO:0000305"
FT CONFLICT 418..419
FT /note="EQ -> DE (in Ref. 1; AAA39727 and 2; AAA39489)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="A -> R (in Ref. 1; AAA39727 and 2; AAA39489)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 63954 MW; D6BBF93FBEDAB1BE CRC64;
MEPRAPRRRH THQRGYLLTR DPHLNKDLAF TLEERQQLNI HGLLPPCIIS QELQVLRIIK
NFERLNSDFD RYLLLMDLQD RNEKLFYSVL MSDVEKFMPI VYTPTVGLAC QQYSLAFRKP
RGLFISIHDK GHIASVLNAW PEDVVKAIVV TDGERILGLG DLGCNGMGIP VGKLALYTAC
GGVNPQQCLP ITLDVGTENE ELLKDPLYIG LRHRRVRGPE YDAFLDEFME AASSKYGMNC
LIQFEDFANR NAFRLLNKYR NKYCTFNDDI QGTASVAVAG LLAALRITKN KLSDQTVLFQ
GAGEAALGIA HLVVMAMEKE GLSKENARKK IWLVDSKGLI VKGRASLTEE KEVFAHEHEE
MKNLEAIVQK IKPTALIGVA AIGGAFTEQI LKDMAAFNER PIIFALSNPT SKAECSAEQC
YKVTKGRAIF ASGSPFDPVT LPDGRTLFPG QGNNSYVFPG VALGVVACGL RHIDDKVFLT
TAEVISQQVS DKHLQEGRLY PPLNTIRGVS LKIAVKIVQD AYKEKMATVY PEPQNKEEFV
SSQMYSTNYD QILPDCYPWP AEVQKIQTKV NQ
