ECHD1_MOUSE
ID ECHD1_MOUSE Reviewed; 322 AA.
AC Q9D9V3; Q3U8C0; Q3UM30; Q8C185; Q9CTC5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ethylmalonyl-CoA decarboxylase;
DE EC=4.1.1.94 {ECO:0000269|PubMed:22016388};
DE AltName: Full=Enoyl-CoA hydratase domain-containing protein 1;
DE AltName: Full=Methylmalonyl-CoA decarboxylase;
DE Short=MMCD;
GN Name=Echdc1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Mammary gland, Skin, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Egg;
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, 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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=22016388; DOI=10.1074/jbc.m111.281527;
RA Linster C.L., Noel G., Stroobant V., Vertommen D., Vincent M.F.,
RA Bommer G.T., Veiga-da-Cunha M., Van Schaftingen E.;
RT "Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
RT proofreading.";
RL J. Biol. Chem. 286:42992-43003(2011).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-232 AND LYS-316, 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-232, 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: Decarboxylates ethylmalonyl-CoA, a potentially toxic
CC metabolite, to form butyryl-CoA, suggesting it might be involved in
CC metabolite proofreading. Also has methylmalonyl-CoA decarboxylase
CC activity at lower level. {ECO:0000269|PubMed:22016388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-ethylmalonyl-CoA + H(+) = butanoyl-CoA + CO2;
CC Xref=Rhea:RHEA:32131, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:60909; EC=4.1.1.94;
CC Evidence={ECO:0000269|PubMed:22016388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32132;
CC Evidence={ECO:0000305|PubMed:22016388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-methylmalonyl-CoA + H(+) = CO2 + propanoyl-CoA;
CC Xref=Rhea:RHEA:61340, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57392; EC=4.1.1.94;
CC Evidence={ECO:0000269|PubMed:22016388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61341;
CC Evidence={ECO:0000305|PubMed:22016388};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.96 uM for (S)-ethylmalonyl-CoA (in absence of ATP)
CC {ECO:0000269|PubMed:22016388};
CC KM=6.5 uM for (S)-ethylmalonyl-CoA (in presence of 5 mM ATP)
CC {ECO:0000269|PubMed:22016388};
CC KM=3.1 uM for (S)-methylmalonyl-CoA (in absence of ATP)
CC {ECO:0000269|PubMed:22016388};
CC KM=15.1 uM for (S)-methylmalonyl-CoA (in presence of 5 mM ATP)
CC {ECO:0000269|PubMed:22016388};
CC Note=kcat is 10 sec(-1) for (S)-ethylmalonyl-CoA as substrate (in
CC presence of 5 mM ATP). kcat is 1.68 sec(-1) for (S)-methylmalonyl-CoA
CC as substrate (in presence of 5 mM ATP).
CC {ECO:0000269|PubMed:22016388};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:22016388}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D9V3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D9V3-2; Sequence=VSP_022499;
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AK003965; BAB23096.1; -; mRNA.
DR EMBL; AK006444; BAB24592.2; -; mRNA.
DR EMBL; AK028775; BAC26112.1; -; mRNA.
DR EMBL; AK145162; BAE26268.1; -; mRNA.
DR EMBL; AK150932; BAE29969.1; -; mRNA.
DR EMBL; AK152285; BAE31098.1; -; mRNA.
DR EMBL; AK153454; BAE32007.1; -; mRNA.
DR EMBL; AK166589; BAE38876.1; -; mRNA.
DR EMBL; AK166634; BAE38907.1; -; mRNA.
DR EMBL; AK166660; BAE38924.1; -; mRNA.
DR EMBL; BC066183; AAH66183.1; -; mRNA.
DR CCDS; CCDS23760.1; -. [Q9D9V3-1]
DR CCDS; CCDS48528.1; -. [Q9D9V3-2]
DR RefSeq; NP_001103665.1; NM_001110195.1. [Q9D9V3-2]
DR RefSeq; NP_080131.4; NM_025855.4. [Q9D9V3-1]
DR AlphaFoldDB; Q9D9V3; -.
DR SMR; Q9D9V3; -.
DR BioGRID; 206721; 12.
DR IntAct; Q9D9V3; 1.
DR STRING; 10090.ENSMUSP00000020034; -.
DR iPTMnet; Q9D9V3; -.
DR PhosphoSitePlus; Q9D9V3; -.
DR SwissPalm; Q9D9V3; -.
DR EPD; Q9D9V3; -.
DR jPOST; Q9D9V3; -.
DR MaxQB; Q9D9V3; -.
DR PaxDb; Q9D9V3; -.
DR PeptideAtlas; Q9D9V3; -.
DR PRIDE; Q9D9V3; -.
DR ProteomicsDB; 275431; -. [Q9D9V3-1]
DR ProteomicsDB; 275432; -. [Q9D9V3-2]
DR Antibodypedia; 32755; 137 antibodies from 20 providers.
DR Ensembl; ENSMUST00000020034; ENSMUSP00000020034; ENSMUSG00000019883. [Q9D9V3-1]
DR Ensembl; ENSMUST00000160399; ENSMUSP00000125553; ENSMUSG00000019883. [Q9D9V3-2]
DR GeneID; 52665; -.
DR KEGG; mmu:52665; -.
DR UCSC; uc007esw.2; mouse. [Q9D9V3-1]
DR CTD; 55862; -.
DR MGI; MGI:1277169; Echdc1.
DR VEuPathDB; HostDB:ENSMUSG00000019883; -.
DR eggNOG; KOG1680; Eukaryota.
DR GeneTree; ENSGT00880000138038; -.
DR HOGENOM; CLU_009834_7_6_1; -.
DR InParanoid; Q9D9V3; -.
DR OMA; HKQMGLV; -.
DR OrthoDB; 1234730at2759; -.
DR PhylomeDB; Q9D9V3; -.
DR TreeFam; TF315986; -.
DR BioCyc; MetaCyc:MON-17103; -.
DR BRENDA; 4.1.1.94; 3474.
DR SABIO-RK; Q9D9V3; -.
DR BioGRID-ORCS; 52665; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Echdc1; mouse.
DR PRO; PR:Q9D9V3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D9V3; protein.
DR Bgee; ENSMUSG00000019883; Expressed in aorta tunica adventitia and 254 other tissues.
DR ExpressionAtlas; Q9D9V3; baseline and differential.
DR Genevisible; Q9D9V3; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016831; F:carboxy-lyase activity; IDA:UniProtKB.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Lyase; Reference proteome.
FT CHAIN 1..322
FT /note="Ethylmalonyl-CoA decarboxylase"
FT /id="PRO_0000273247"
FT MOD_RES 232
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 232
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 316
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022499"
FT CONFLICT 2
FT /note="R -> K (in Ref. 1; BAC26112)"
FT /evidence="ECO:0000305"
FT CONFLICT 4
FT /note="C -> F (in Ref. 1; BAE26268)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="R -> Q (in Ref. 1; BAC26112)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="K -> Q (in Ref. 1; BAE26268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35467 MW; B25E26FEF0611EB1 CRC64;
MRRCEVNSKP ISEYFGIPCE NREMAKCLLT SSLSVRTKLL QTGVSLYNTS HGFHEEEVKK
ILEQFPGGSI DLLKKQNGIG ILTLNNPNKM NAFSGVMMLQ LLERVIELEN WTEGKGLIIH
GAKNTFCSGS DLNAVKALST PESGVALSMF MQNTLTRFMR LPLISVALVQ GWAMGGGAEL
TTACDFRLMT EESVIRFVHK EMGIVPSWGG TSRLVEIIGS RQALKVLSGT LKLDSKEALN
IGLTDEVLQP SDETTALEQA QEWLEKFVSG PPQVIRGLKK SVCSARELYI EEALQNERDV
LETLWGGPAN LEAIAKKGKH TK
