UniProt Accession

 ECI2_MOUSE; Q9WUR2; Q99M61; Q9D785 

Genbank Protein ID

 AF153613; AK009478; BC001983 

Genbank Nucleotide ID

 AAD34174.1; BAB26315.2; AAH01983.1 

Protein Name

 Enoyl-CoA delta isomerase 2, mitochondrial 

Protein Synonyms/Alias

 Delta(3),delta(2)-enoyl-CoA isomerase; D3,D2-enoyl-CoA isomerase; Dodecenoyl-CoA isomerase; Peroxisomal 3,2-trans-enoyl-CoA isomerase; pECI 

Gene Name

 Eci2 

Gene Synonyms/Alias

 Peci 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
49	ENALNQVKLLKKDPG	acetylation	[1]
49	ENALNQVKLLKKDPG	ubiquitination	[2]
52	LNQVKLLKKDPGNEV	acetylation	[1]
60	KDPGNEVKLRLYALY	acetylation	[1, 3]
68	LRLYALYKQATEGPC	acetylation	[1]
79	EGPCNMPKPGMLDFV	acetylation	[1]
88	GMLDFVNKAKWDAWN	acetylation	[1]
90	LDFVNKAKWDAWNAL	acetylation	[1]
90	LDFVNKAKWDAWNAL	ubiquitination	[2]
102	NALGSLPKETARQNY	acetylation	[1]
127	SEAPSQGKRGADEKA	acetylation	[1]
133	GKRGADEKARESKDI	acetylation	[1]
138	DEKARESKDILVTSE	acetylation	[1]
158	ITFNRPTKKNAISFQ	acetylation	[1]
159	TFNRPTKKNAISFQM	ubiquitination	[2]
286	CSSYTFPKMMGSAKA	ubiquitination	[2]
356	IRKNEKEKLYAVNAE	acetylation	[1]

Reference

 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647] 

Functional Description

 Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates (By similarity). 

Sequence Annotation

 DOMAIN 37 122 ACB.
 REGION 64 68 Acyl-CoA binding (By similarity).
 REGION 149 319 ECH-like.
 MOTIF 389 391 Microbody targeting signal (Potential).
 BINDING 90 90 Acyl-CoA (By similarity).
 BINDING 109 109 Acyl-CoA (By similarity).
 MOD_RES 49 49 N6-acetyllysine (By similarity).
 MOD_RES 60 60 N6-acetyllysine.
 MOD_RES 90 90 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; Alternative splicing; Complete proteome; Isomerase; Mitochondrion; Peroxisome; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 391 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
 GO:0005777; C:peroxisome; IDA:HGNC.
 GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:EC.
 GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
 GO:0006635; P:fatty acid beta-oxidation; IEA:Compara.
 GO:0009062; P:fatty acid catabolic process; ISS:UniProtKB. 

Interpro

 IPR022408; Acyl-CoA-binding_prot_CS.
 IPR000582; Acyl-CoA-binding_protein.
 IPR001753; Crotonase_core_superfam.
 IPR014352; FERM/acyl-CoA-bd_prot_3-hlx. 

Pfam

 PF00887; ACBP
 PF00378; ECH 

SMART

  

PROSITE

 PS00880; ACB_1
 PS51228; ACB_2 

PRINTS

 PR00689; ACOABINDINGP.