(data stored in ACNUC7421 zone)

SWISSPROT: 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   30-AUG-2017, entry version 86.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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;
RC   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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND IDENTIFICATION BY
RP   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.,
RA   Zhang Y., 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
RP   MASS 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.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria 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         Note=Gene prediction based on EST data. No experimental
CC         confirmation available.;
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; Positions=7; Evidence={ECO:0000305};
CC       Sequence=BAE32227.1; Type=Frameshift; Positions=10; Evidence={ECO:0000305};
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; BX293563; CAM22565.1; -; Genomic_DNA.
DR   EMBL; AL844206; CAM22565.1; JOINED; Genomic_DNA.
DR   EMBL; BX293563; CAM22566.1; -; Genomic_DNA.
DR   EMBL; AL844206; CAM22566.1; JOINED; Genomic_DNA.
DR   EMBL; AL844206; CAM27079.1; -; Genomic_DNA.
DR   EMBL; BX293563; CAM27079.1; JOINED; Genomic_DNA.
DR   EMBL; AL844206; CAM27080.1; -; Genomic_DNA.
DR   EMBL; BX293563; CAM27080.1; JOINED; 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   UniGene; Mm.270783; -.
DR   ProteinModelPortal; Q3TLP5; -.
DR   SMR; Q3TLP5; -.
DR   IntAct; Q3TLP5; 3.
DR   MINT; MINT-4128191; -.
DR   STRING; 10090.ENSMUSP00000051268; -.
DR   PhosphoSitePlus; Q3TLP5; -.
DR   MaxQB; Q3TLP5; -.
DR   PaxDb; Q3TLP5; -.
DR   PeptideAtlas; Q3TLP5; -.
DR   PRIDE; Q3TLP5; -.
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   eggNOG; KOG1679; Eukaryota.
DR   eggNOG; COG1024; LUCA.
DR   GeneTree; ENSGT00890000139344; -.
DR   HOVERGEN; HBG106714; -.
DR   InParanoid; Q3TLP5; -.
DR   OMA; RENATIY; -.
DR   OrthoDB; EOG091G0Q9K; -.
DR   PhylomeDB; Q3TLP5; -.
DR   TreeFam; TF314276; -.
DR   PRO; PR:Q3TLP5; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000028601; -.
DR   CleanEx; MM_ECHDC2; -.
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.
DR   InterPro; IPR014748; Crontonase_C.
DR   InterPro; IPR001753; Crotonase_core_superfam.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q3TLP5.
DR   SWISS-2DPAGE; Q3TLP5.
KW   Acetylation; Alternative splicing; Complete proteome;
KW   Fatty acid metabolism; Lipid metabolism; Lyase; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     17       Mitochondrion. {ECO:0000255}.
FT   CHAIN        18    296       Enoyl-CoA hydratase domain-containing
FT                                protein 2, mitochondrial.
FT                                /FTId=PRO_0000309460.
FT   SITE        146    146       Important for catalytic activity.
FT                                {ECO:0000250}.
FT   SITE        166    166       Important for catalytic activity.
FT                                {ECO:0000250}.
FT   MOD_RES     101    101       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     101    101       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   VAR_SEQ       1    105       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_029178.
FT   VAR_SEQ     126    156       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_029179.
FT   CONFLICT     14     14       S -> P (in Ref. 1; BAE32227/BAE38747 and
FT                                3; AAH25104). {ECO:0000305}.
FT   CONFLICT     50     50       L -> V (in Ref. 1; BAE38747 and 3;
FT                                AAH25104). {ECO:0000305}.
FT   CONFLICT     53     53       R -> G (in Ref. 1; BAB23757).
FT                                {ECO:0000305}.
FT   CONFLICT     55     55       N -> H (in Ref. 1; BAE32227/BAE38747 and
FT                                3; AAH25104). {ECO:0000305}.
FT   CONFLICT    130    130       V -> A (in Ref. 1; BAE32227/BAE38747 and
FT                                3; AAH25104). {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
//

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