MAON_MOUSE
ID MAON_MOUSE Reviewed; 604 AA.
AC Q8BMF3; Q499F4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=NADP-dependent malic enzyme, mitochondrial;
DE Short=NADP-ME;
DE EC=1.1.1.40;
DE AltName: Full=Malic enzyme 3;
DE Flags: Precursor;
GN Name=Me3;
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=Olfactory bulb;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Neural stem cell;
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).
RN [3]
RP PROTEIN SEQUENCE OF 71-92 AND 481-506, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, and Kidney;
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 -!- 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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; AK032196; BAC27751.1; -; mRNA.
DR EMBL; BC099935; AAH99935.1; -; mRNA.
DR CCDS; CCDS21443.1; -.
DR RefSeq; NP_852072.2; NM_181407.4.
DR RefSeq; XP_006507252.1; XM_006507189.3.
DR RefSeq; XP_006507253.1; XM_006507190.3.
DR AlphaFoldDB; Q8BMF3; -.
DR SMR; Q8BMF3; -.
DR BioGRID; 224624; 3.
DR IntAct; Q8BMF3; 1.
DR MINT; Q8BMF3; -.
DR STRING; 10090.ENSMUSP00000032856; -.
DR iPTMnet; Q8BMF3; -.
DR PhosphoSitePlus; Q8BMF3; -.
DR SwissPalm; Q8BMF3; -.
DR jPOST; Q8BMF3; -.
DR MaxQB; Q8BMF3; -.
DR PaxDb; Q8BMF3; -.
DR PeptideAtlas; Q8BMF3; -.
DR PRIDE; Q8BMF3; -.
DR ProteomicsDB; 295814; -.
DR Antibodypedia; 31451; 139 antibodies from 25 providers.
DR DNASU; 109264; -.
DR Ensembl; ENSMUST00000032856; ENSMUSP00000032856; ENSMUSG00000030621.
DR GeneID; 109264; -.
DR KEGG; mmu:109264; -.
DR UCSC; uc009igd.1; mouse.
DR CTD; 10873; -.
DR MGI; MGI:1916679; Me3.
DR VEuPathDB; HostDB:ENSMUSG00000030621; -.
DR eggNOG; KOG1257; Eukaryota.
DR GeneTree; ENSGT00950000183134; -.
DR HOGENOM; CLU_011405_5_2_1; -.
DR InParanoid; Q8BMF3; -.
DR OMA; DDLYVGW; -.
DR OrthoDB; 435571at2759; -.
DR PhylomeDB; Q8BMF3; -.
DR TreeFam; TF300537; -.
DR Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR BioGRID-ORCS; 109264; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Me3; mouse.
DR PRO; PR:Q8BMF3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BMF3; protein.
DR Bgee; ENSMUSG00000030621; Expressed in interventricular septum and 169 other tissues.
DR ExpressionAtlas; Q8BMF3; baseline and differential.
DR Genevisible; Q8BMF3; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0004470; F:malic enzyme activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0070401; F:NADP+ binding; ISO:MGI.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; ISS:UniProtKB.
DR GO; GO:0006090; P:pyruvate metabolic process; 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 Direct protein sequencing; Metal-binding; Mitochondrion; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..604
FT /note="NADP-dependent malic enzyme, mitochondrial"
FT /id="PRO_0000018540"
FT REGION 28..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 304
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06801"
FT CONFLICT 113
FT /note="L -> H (in Ref. 1; BAC27751)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="G -> D (in Ref. 1; BAC27751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 604 AA; 67098 MW; F667B01B116A5918 CRC64;
MGAALGTGAR LTSVPRIACS SLRRQAPSAP AQGCHSKSGP PRPVPLKKRG YDVTRNPHLN
KGMAFTLEER LQLGIHGLIP PCFLSQDVQL LRIMRYYENQ QSDLDKYIIL MTLQDRNEKL
FYRVLTSDVE KFMPIVYTPT VGLACQHYGL TFRRPRGLFI TIHDKGHIAT MLNSWPEDNI
KAVVVTDGER ILGLGDLGCY GMGIPVGKLA LYTACGGVNP QQCLPVLLDV GTNNEELLRD
PLYIGLKHQR VRGEEYDDLL DEFMQAVTDK FGINCLIQFE DFANANAFRL LNKYRNKYCM
FNDDIQGTAS VAVAGILAAL RITKNRLSNH VFVFQGAGEA AMGIAHLLVM ALEKEGIPKT
EAIKKIWMVD SKGLIVKGRS HLNHEKEMFA QDHPEVNSLE EVVRLVKPTA IIGVAAIAGA
FTEQILRDMA SFHERPIVFA LSNPTSKAEC TAEKCYRVTE GRGIFASGSP FKSVTLEDGR
TFTPGQGNNA YVFPGVALGV IAGGIRHIPD EIFLLTAEQI AQEVSEQHLS QGRLYPPLST
IRDVSLRIAV KVLDYAYKHN LASYYPEPKD KEAFVKSLIY TPDYDSFSLD TYSWPKEAMS
VQKV
