Seroatlas · Protein domains

Hotdog acyl-CoA thioesterase (ACOT)-type domain

IPR033120

Definition

The HotDog domain is widespread in eukaryotes, bacteria, and archaea and is involved in a range of cellular processes, from thioester hydrolysis, to phenylacetic acid degradation and transcriptional regulation of fatty acid biosynthesis. The HotDog domain has a mixed α+β fold structure, which adopts a five- to seven-stranded antiparallel β-sheet as the 'bun' wrapping around a central α-helix sausage PMID:15307895. The largest HotDog domain subfamily represents over a hundred acyl-CoA thioesterases (ACOTs) that are widespread throughout the prokaryotic kingdom, with members also found in eukaryotes. This group of enzymes catalyze the hydrolysis of acyl-CoA thioesters to free fatty acids and coenzyme A (CoA- SH). The subfamily includes thioesterases with activity towards medium and long chain acyl-CoAs (medium chain acyl-CoA hydrolase and cytosolic long-chain acyl-CoA hydrolase/brain acyl-CoA hydrolase (BACH) respectively) and also cytoplasmic acetyl-CoA hydrolase (CACH), which hydrolyzes acetyl-CoA to acetate and CoA-SH. Brown-fat-inducible thioesterase (BFIT), a cold-induced protein found in brown adipose tissue (BAT) is also included in this group. Both BFIT and CACH possess a StAR-related lipid-transfer (START) domain that is involved in lipid binding, consistent with the role of BFIT and CACH in lipid metabolism. Duplication of the HotDog domain and recruitment of the START domain seems to be a mammalian innovation PMID:15307895. The HotDog ACOT-type domain consists of a five-stranded β-sheet with topology beta1/beta3/beta4/beta5/beta2 that wraps around a central five-turn α helix, alpha1, positioned between beta1 and beta2 [[cite:PMID:19303060], [cite:PMID:17563367], [cite:PMID:25002576]].

5 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

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