(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Metazoa: NE > Eumetazoa: NE > Bilateria: NE > Deuterostomia: NE > Chordata: NE > Craniata: NE > Vertebrata: NE > Gnathostomata: NE > Teleostomi: NE > Euteleostomi: NE > Sarcopterygii: NE > Dipnotetrapodomorpha: NE > Tetrapoda: NE > Amniota: NE > Mammalia: NE > Theria: NE > Eutheria: NE > Boreoeutheria: NE > Laurasiatheria: NE > Perissodactyla: NE > Equidae: NE > Equus [genus]: NE > Equus [subgenus]: NE > Equus caballus: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MQSWGTIICIRILLRFLLLWVLIGNSHTEEDIIITTKNGKVRGMNLPVLG GTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSNIWNATKYANSCYQNTDQS FPGFLGSEMWNPNTELSEDCLYLNVWIPAPKPKNATVMIWIYGGGFQTGT SSLPVYDGKFLARVERVIVVSMNYRVGALGFLALSENPEAPGNMGLFDQQ LALQWVQKNIAAFGGNPRSVTLFGESAGAASVSLHLLSPRSQPLFTRAIL QSGSSNAPWAVTSLYEARNRTLTLAKRMGCSRDNETEMIKCLRDKDPQEI LLNEVFVVPYDTLLSVNFGPTVDGDFLTDMPDTLLQLGQFKRTQILVGVN KDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPRVSEFGRESILFH YMDWLDDQRAENYREALDDVVGDYNIICPALEFTKKFSELGNDAFFYYFE HRSTKLPWPEWMGVMHGYEIEFVFGLPLERRVNYTKAEEILSRSIMKRWA NFAKYGNPNGTQSNSTRWPVFKSTEQKYLTLNTESPKVYTKLRAQQCRFW TLFFPKVLELTGNIDEAEREWKAGFHRWNNYMMDWKNQFNDYTSKKESCS DF
We report a high-quality draft sequence of the genome of the horse (Equus caballus). The genome is relatively repetitive but has little segmental duplication. Chromosomes appear to have undergone few historical rearrangements: 53% of equine chromosomes show conserved synteny to a single human chromosome. Equine chromosome 11 is shown to have an evolutionary new centromere devoid of centromeric satellite DNA, suggesting that centromeric function may arise before satellite repeat accumulation. Linkage disequilibrium, showing the influences of early domestication of large herds of female horses, is intermediate in length between dog and human, and there is long-range haplotype sharing among breeds.
Title: Isolation and characterization of a cDNA encoding a horse liver butyrylcholinesterase: evidence for CPT-11 drug activation Wierdl M, Morton CL, Danks MK, Potter PM Ref: Biochemical Pharmacology, 59:773, 2000 : PubMed
Butyrylcholinesterases (BuChEs; acylcholine acylhydrolase; EC 3.1.1.8) have been demonstrated to convert the anticancer agent CPT-11 (irinotecan, 7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyloxycamptothecin) into its active metabolite SN-38 (7-ethyl-10-hydroxycamptothecin). In addition, significant differences in the extent of drug metabolism have been observed with BuChEs derived from different species. In an attempt to understand these differences, we have isolated the cDNA encoding a horse BuChE. Based upon the NH2-terminal amino acid sequence of a purified horse BuChE, we designed degenerate primers to amplify the coding sequence from horse liver cDNA. Following polymerase chain reaction and rapid amplification of the cDNA ends, we generated an 1850-bp DNA fragment, containing an 1806-bp open reading frame. The cDNA encodes a protein of 602 amino acid residues, including a 28-amino-acid NH2-terminal signal peptide. Furthermore, the DNA sequence and the deduced amino acid sequence revealed extensive homology to butyrylcholinesterase genes from several other species. In vitro transcription-translation of the cDNA produced a 66-kDa protein, identical to the size of native horse serum BuChE following removal of carbohydrate residues with endoglycosidase F. Additionally, transient expression of the cDNA in Cos-7 cells yielded extracts that exhibited cholinesterase activity and demonstrated a Km value for butyrylthiocholine of 106+/-9 nM. This extract converted the anticancer drug CPT-11 into SN-38, demonstrating that this drug can be activated by enzymes other than carboxylesterases.
Title: Amino Acid Sequence of Horse Serum Butyrylcholinesterase Moorad DR, Luo C, Saxena A, Doctor BP, Garcia GE Ref: In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases, (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.:145, 1998 : PubMed
Equus caballus, Horse mRNA for triacylglycerol lipase