ECHD2_MOUSE
ID ECHD2_MOUSE Reviewed; 296 AA.
AC Q3TLP5; A2APS6; Q3TKJ7; Q3TV08; Q3U553; Q8R3K4; Q9DBD3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Enoyl-CoA hydratase domain-containing protein 2, mitochondrial;
DE Flags: Precursor;
GN Name=Echdc2; Synonyms=D4Ertd765e;
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 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, Mammary gland, Stomach, and Thymus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC 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 [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND IDENTIFICATION BY MASS
RP 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-101, 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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TLP5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TLP5-2; Sequence=VSP_029179;
CC Name=3;
CC IsoId=Q3TLP5-3; Sequence=VSP_029178;
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25104.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB23757.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE32227.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK005030; BAB23757.1; ALT_FRAME; mRNA.
DR EMBL; AK153878; BAE32227.1; ALT_FRAME; mRNA.
DR EMBL; AK160482; BAE35813.1; -; mRNA.
DR EMBL; AK166388; BAE38747.1; -; mRNA.
DR EMBL; AK166965; BAE39148.1; -; mRNA.
DR EMBL; AL844206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX293563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025104; AAH25104.1; ALT_INIT; mRNA.
DR CCDS; CCDS18447.2; -. [Q3TLP5-1]
DR RefSeq; NP_001241683.1; NM_001254754.1. [Q3TLP5-3]
DR RefSeq; NP_081004.2; NM_026728.4. [Q3TLP5-1]
DR RefSeq; XP_011238875.1; XM_011240573.1. [Q3TLP5-3]
DR RefSeq; XP_017175803.1; XM_017320314.1. [Q3TLP5-3]
DR AlphaFoldDB; Q3TLP5; -.
DR SMR; Q3TLP5; -.
DR BioGRID; 206580; 2.
DR STRING; 10090.ENSMUSP00000051268; -.
DR iPTMnet; Q3TLP5; -.
DR PhosphoSitePlus; Q3TLP5; -.
DR EPD; Q3TLP5; -.
DR jPOST; Q3TLP5; -.
DR MaxQB; Q3TLP5; -.
DR PaxDb; Q3TLP5; -.
DR PeptideAtlas; Q3TLP5; -.
DR PRIDE; Q3TLP5; -.
DR ProteomicsDB; 275433; -. [Q3TLP5-1]
DR ProteomicsDB; 275434; -. [Q3TLP5-2]
DR ProteomicsDB; 275435; -. [Q3TLP5-3]
DR Antibodypedia; 19158; 99 antibodies from 19 providers.
DR Ensembl; ENSMUST00000052999; ENSMUSP00000051268; ENSMUSG00000028601. [Q3TLP5-1]
DR Ensembl; ENSMUST00000116307; ENSMUSP00000112009; ENSMUSG00000028601. [Q3TLP5-2]
DR Ensembl; ENSMUST00000116309; ENSMUSP00000112011; ENSMUSG00000028601. [Q3TLP5-1]
DR GeneID; 52430; -.
DR KEGG; mmu:52430; -.
DR UCSC; uc008uat.3; mouse. [Q3TLP5-1]
DR CTD; 55268; -.
DR MGI; MGI:1289238; Echdc2.
DR VEuPathDB; HostDB:ENSMUSG00000028601; -.
DR eggNOG; KOG1679; Eukaryota.
DR GeneTree; ENSGT00940000158798; -.
DR HOGENOM; CLU_009834_7_6_1; -.
DR InParanoid; Q3TLP5; -.
DR OMA; WRSVAFS; -.
DR OrthoDB; 1123666at2759; -.
DR PhylomeDB; Q3TLP5; -.
DR TreeFam; TF314276; -.
DR BioGRID-ORCS; 52430; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Echdc2; mouse.
DR PRO; PR:Q3TLP5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3TLP5; protein.
DR Bgee; ENSMUSG00000028601; Expressed in right kidney and 224 other tissues.
DR ExpressionAtlas; Q3TLP5; baseline and differential.
DR Genevisible; Q3TLP5; MM.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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 Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
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; Fatty acid metabolism; Lipid metabolism;
KW Lyase; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..296
FT /note="Enoyl-CoA hydratase domain-containing protein 2,
FT mitochondrial"
FT /id="PRO_0000309460"
FT SITE 146
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 166
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 101
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 101
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029178"
FT VAR_SEQ 126..156
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_029179"
FT CONFLICT 14
FT /note="S -> P (in Ref. 1; BAE32227/BAE38747 and 3;
FT AAH25104)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="L -> V (in Ref. 1; BAE38747 and 3; AAH25104)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="R -> G (in Ref. 1; BAB23757)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="N -> H (in Ref. 1; BAE32227/BAE38747 and 3;
FT AAH25104)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="V -> A (in Ref. 1; BAE32227/BAE38747 and 3;
FT AAH25104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 31852 MW; 1AF23979BDFDA4B3 CRC64;
MLRVLPRALR LPCSWRFSGA RDCASHATTR TPEIQVQALT GPNQGITEIL MNRPNARNAL
GNVFVSELLE ALAQLREDQQ VRVLLFRSAV KGVFCAGADL KEREQMSDVE VGTFVQRLRG
LMSEIAAFPV PTIAAMDGFA LGGGLELALA CDLRIAASSA VMGLIETTRG LLPGAGGTQR
LPRCLGVALA KELIFTGRRL NGAQARELGL VNHAVAQNEE GNAAYHRALA LAQEILPQAP
IAVRLGKVAI DRGMEVDIAS GMAIEQMCYA QNIPTQDRLE GMAAFREKRA PKFVGK
