Tag | Content |
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CPLM ID | CPLM-004236 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Enoyl-CoA hydratase, mitochondrial |
Protein Synonyms/Alias | Enoyl-CoA hydratase 1; Short-chain enoyl-CoA hydratase; SCEH |
Gene Name | Echs1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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40 | FQYIITEKKGKNSSV | acetylation | [1] | 101 | FAAGADIKEMQNRTF | acetylation | [1] | 115 | FQDCYSGKFLSHWDH | acetylation | [1] | 204 | RISAQDAKQAGLVSK | acetylation | [1] | 288 | EKRKANFKDH***** | 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 | Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate. |
Sequence Annotation | REGION 98 101 Substrate binding. BINDING 141 141 Substrate; via amide nitrogen. MOD_RES 101 101 N6-acetyllysine (By similarity). |
Keyword | 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Fatty acid metabolism; Lipid metabolism; Lyase; Mitochondrion; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 290 AA |
Protein Sequence | MAALRALLPR ACNSLLSPVR CPEFRRFASG ANFQYIITEK KGKNSSVGLI QLNRPKALNA 60 LCNGLIEELN QALETFEEDP AVGAIVLTGG EKAFAAGADI KEMQNRTFQD CYSGKFLSHW 120 DHITRIKKPV IAAVNGYALG GGCELAMMCD IIYAGEKAQF GQPEILLGTI PGAGGTQRLT 180 RAVGKSLAME MVLTGDRISA QDAKQAGLVS KIFPVETLVE EAIQCAEKIA NNSKIIVAMA 240 KESVNAAFEM TLTEGNKLEK KLFYSTFATD DRREGMSAFV EKRKANFKDH 290 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |