Tag | Content |
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CPLM ID | CPLM-014173 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
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 | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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49 | ENAMNQVKLLKKDPG | acetylation | [1] | 52 | MNQVKLLKKDPGNEV | acetylation | [1] | 60 | KDPGNEVKLRLYALY | acetylation | [1] | 79 | EGPCTMPKPGVFDFV | acetylation | [1] | 90 | FDFVNKAKWDAWNAL | acetylation | [1] | 138 | DGKAQESKGILVTSE | acetylation | [1] | 336 | TRLKTYAKLPPNSMR | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
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. |
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 (By similarity). 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 | MAAVTWSRAR CWCPSLLQVL RLPVTKLHLG RPAMRATQQD FENAMNQVKL LKKDPGNEVK 60 LRLYALYKQA TEGPCTMPKP GVFDFVNKAK WDAWNALGSL PKETARQNYV DLVSSLSSSS 120 EASSQGKGGA DGKAQESKGI LVTSEGGITK ITFNRPSKKN AITFQMYQDI ILALKNASTD 180 DTVITVFTGA GDYYSSGNDL TNFTSASGGM EEAANKGAIV LREFVNTFID FPKPLVAVVN 240 GPAVGISVTL LGLFDAVYAS DRATFHTPFS HLGQSPEACS SYTFPKMMGS AKAAEMLLFG 300 KKLTAREAWA QGLVTEVFPE STFETEVWTR LKTYAKLPPN SMRISKELIR KNEKEKLHAV 360 NEEECTTLRA RWLSEECINA IMSFVTRKPK L 391 |
Gene Ontology | GO:0005739; C:mitochondrion; IDA:RGD. GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell. GO:0005777; C:peroxisome; IDA:RGD. GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:EC. GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro. GO:0016863; F:intramolecular oxidoreductase activity, transposing C=C bonds; IDA:RGD. GO:0006635; P:fatty acid beta-oxidation; IDA:RGD. |
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