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2, 4-dienoyl-CoA reductase 1 (DECR1) is an auxiliary enzyme of β-oxidation, and it participates in the metabolism of polyunsaturated fatty enoyl-CoA esters. The full-length cDNA of DECR1 was first cloned from Mashen pig liver, and bioinformatics analysis were then conducted to predicted the physicochemical property, homologous analysis, modification sites and structure of DECR1 protein. Sequence analysis showed that the full-length cDNA of DECR1 was 2352 bp long with an open reading frame (ORF) of 987 bp encoding 328 amino acid residues. Homologous analysis showed that the amino acids of Mashen pig DECR1 shared 99%, 88% , 88% , 87%, 87%, 87%, 87% and 83% identity to Sus scrofa (Predicted), Bos taurus, Homo sapiens, Macaca mulatta, Pan troglodytes, Equus caballus, Canis and Mus musculus, respectively. Bioinformatics analysis showed that DECR1 was a trans-membrane protein, and molecular mass, theoretical point, aliphatic index, estimated half-life, and instability index were 35.43 kDa, 9.37, 85.70, 30 h and 29.06, respectively. Predicted DECR1 have 10 Ser, 6 Thr and 1 Tyr phosphorylation sites. Structure prediction showed that DECR1 consisted of 39.3% α-helix, 11.6% β-extended strand and 49.1% random coil in binary structure, and 2 three and a half α-helices and two 310-helices in three-dimensional structure.