MCEE_MOUSE
ID MCEE_MOUSE Reviewed; 178 AA.
AC Q9D1I5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Methylmalonyl-CoA epimerase, mitochondrial {ECO:0000305};
DE EC=5.1.99.1 {ECO:0000250|UniProtKB:Q96PE7};
DE AltName: Full=DL-methylmalonyl-CoA racemase;
DE Flags: Precursor;
GN Name=Mcee {ECO:0000312|MGI:MGI:1920974};
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
RC Pancreas;
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).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-152, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Methylmalonyl-CoA epimerase involved in propionyl-CoA
CC metabolism. {ECO:0000250|UniProtKB:Q96PE7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA;
CC Xref=Rhea:RHEA:20553, ChEBI:CHEBI:57326, ChEBI:CHEBI:57327;
CC EC=5.1.99.1; Evidence={ECO:0000250|UniProtKB:Q96PE7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20555;
CC Evidence={ECO:0000250|UniProtKB:Q96PE7};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA epimerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK003511; BAB22828.1; -; mRNA.
DR EMBL; BC038157; AAH38157.1; -; mRNA.
DR CCDS; CCDS21334.1; -.
DR RefSeq; NP_082902.1; NM_028626.1.
DR AlphaFoldDB; Q9D1I5; -.
DR SMR; Q9D1I5; -.
DR STRING; 10090.ENSMUSP00000047855; -.
DR iPTMnet; Q9D1I5; -.
DR PhosphoSitePlus; Q9D1I5; -.
DR EPD; Q9D1I5; -.
DR jPOST; Q9D1I5; -.
DR MaxQB; Q9D1I5; -.
DR PaxDb; Q9D1I5; -.
DR PeptideAtlas; Q9D1I5; -.
DR PRIDE; Q9D1I5; -.
DR ProteomicsDB; 295978; -.
DR Antibodypedia; 31195; 203 antibodies from 22 providers.
DR DNASU; 73724; -.
DR Ensembl; ENSMUST00000037205; ENSMUSP00000047855; ENSMUSG00000033429.
DR GeneID; 73724; -.
DR KEGG; mmu:73724; -.
DR UCSC; uc009hgi.1; mouse.
DR CTD; 84693; -.
DR MGI; MGI:1920974; Mcee.
DR VEuPathDB; HostDB:ENSMUSG00000033429; -.
DR eggNOG; KOG2944; Eukaryota.
DR GeneTree; ENSGT00940000153941; -.
DR HOGENOM; CLU_046006_5_0_1; -.
DR InParanoid; Q9D1I5; -.
DR OMA; IHHICYE; -.
DR OrthoDB; 1543116at2759; -.
DR PhylomeDB; Q9D1I5; -.
DR TreeFam; TF313417; -.
DR Reactome; R-MMU-71032; Propionyl-CoA catabolism.
DR BioGRID-ORCS; 73724; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Mcee; mouse.
DR PRO; PR:Q9D1I5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D1I5; protein.
DR Bgee; ENSMUSG00000033429; Expressed in right kidney and 255 other tissues.
DR ExpressionAtlas; Q9D1I5; baseline and differential.
DR Genevisible; Q9D1I5; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004493; F:methylmalonyl-CoA epimerase activity; ISO:MGI.
DR GO; GO:0046491; P:L-methylmalonyl-CoA metabolic process; ISO:MGI.
DR CDD; cd07249; MMCE; 1.
DR Gene3D; 3.10.180.10; -; 1.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR017515; MeMalonyl-CoA_epimerase.
DR InterPro; IPR037523; VOC.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR03081; metmalonyl_epim; 1.
DR PROSITE; PS51819; VOC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cobalt; Isomerase; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 39..178
FT /note="Methylmalonyl-CoA epimerase, mitochondrial"
FT /id="PRO_0000012284"
FT DOMAIN 49..178
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 52
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250"
FT MOD_RES 116
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 152
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 152
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 178 AA; 19017 MW; 0A496AF10455D379 CRC64;
MRRVVKAAAL AAGATGLFSR VQTSVAIGRS FSTPQSQFQE SSPVWKLGRL NHVAVAVPDL
EKASSFYRDV LGAQVSEVVP LPEHGVSVVF VNLGNTKMEL LHPLGSDSPI TGFLQKNKAG
GMHHVCIEVD NISAAVMDLK KKKIRSLSDE AKIGAHGKPV IFLHPKDCGG VLVELEQA
