ACOT11 acyl-CoA thioesterase 11 [Homo sapiens (human)] - Gene

Summary

Official Symbol: ACOT11provided by HGNC
Official Full Name: acyl-CoA thioesterase 11provided by HGNC
Primary source: HGNC:HGNC:18156
See related: Ensembl:ENSG00000162390 MIM:606803; AllianceGenome:HGNC:18156
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: BFIT; THEA; THEM1; STARD14
Summary: This gene encodes a member of the acyl-CoA thioesterase family which catalyse the conversion of activated fatty acids to the corresponding non-esterified fatty acid and coenzyme A. Expression of a mouse homolog in brown adipose tissue is induced by low temperatures and repressed by warm temperatures. Higher levels of expression of the mouse homolog has been found in obesity-resistant mice compared with obesity-prone mice, suggesting a role of acyl-CoA thioesterase 11 in obesity. Alternative splicing results in transcript variants. [provided by RefSeq, Nov 2010]
Expression: Biased expression in kidney (RPKM 35.3), small intestine (RPKM 20.0) and 9 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 1p32.3

Exon count:: 18

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (54548228..54639192)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (54431560..54519420)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (55013901..55104865)

Chromosome 1 - NC_000001.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Allosteric regulation of thioesterase superfamily member 1 by lipid sensor domain binding fatty acids and lysophosphatidylcholine.
Title: Allosteric regulation of thioesterase superfamily member 1 by lipid sensor domain binding fatty acids and lysophosphatidylcholine.
The N-terminal region of human fat inducible thioesterase variant 2 constitutes a mitochondrial location signal sequence, which undergoes mitochondrion-dependent posttranslational cleavage.
Title: Human brown fat inducible thioesterase variant 2 cellular localization and catalytic function.
Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)
Title: Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
Observational study of gene-disease association. (HuGE Navigator)
Title: Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)
Title: Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
BFIT supports the transition of thermogenic brown adipose tissue towards increased metabolic activity, probably through alteration of intracellular fatty acyl-CoA concentration.
Title: BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown adipose tissue: cloning, organization of the human gene and assessment of a potential link to obesity.

Submit: New GeneRIF Correction

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

NoName (e-PCR)
- UniSTS:9484

D8S2279 (e-PCR)
- UniSTS:473907

D3S1611 (e-PCR), detects polymorphism
- UniSTS:31568

D11S3430 (e-PCR)
- UniSTS:152671

SHGC-74880 (e-PCR)
- UniSTS:41831

D15S1477 (e-PCR)
- UniSTS:474482

AL033766 (e-PCR)
- UniSTS:93618

GDB:335751 (e-PCR)
- UniSTS:156601

THEA__5252 (e-PCR)
- UniSTS:464604

AL033560 (e-PCR)
- UniSTS:94174

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables carboxylic ester hydrolase activity	IEA Inferred from Electronic Annotation more info
enables fatty acyl-CoA hydrolase activity	IDA Inferred from Direct Assay more info	PubMed
enables fatty acyl-CoA hydrolase activity	TAS Traceable Author Statement more info	PubMed
enables lipid binding	IEA Inferred from Electronic Annotation more info
enables long-chain fatty acyl-CoA hydrolase activity	IBA Inferred from Biological aspect of Ancestor more info
enables long-chain fatty acyl-CoA hydrolase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in acyl-CoA metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in fatty acid metabolic process	IEA Inferred from Electronic Annotation more info
involved_in fatty acid metabolic process	NAS Non-traceable Author Statement more info	PubMed
involved_in intracellular signal transduction	NAS Non-traceable Author Statement more info	PubMed
involved_in negative regulation of cold-induced thermogenesis	ISS Inferred from Sequence or Structural Similarity more info	PubMed
involved_in response to cold	ISS Inferred from Sequence or Structural Similarity more info	PubMed
involved_in response to temperature stimulus	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info
located_in cytosol	TAS Traceable Author Statement more info
located_in extracellular exosome	HDA more info	PubMed
located_in mitochondrial matrix	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: acyl-coenzyme A thioesterase 11

Names: START domain containing 14; StAR-related lipid transfer (START) domain containing 14; acyl-CoA thioester hydrolase 11; adipose-associated thioesterase; brown fat-inducible thioesterase; palmitoyl-coenzyme A thioesterase; thioesterase superfamily member 1; thioesterase, adipose associated

NP_056362.1

EC 3.1.2.2

NP_671517.1

EC 3.1.2.2

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_015547.4 → NP_056362.1 acyl-coenzyme A thioesterase 11 isoform 1

See identical proteins and their annotated locations for NP_056362.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes the longer isoform (BFIT1) of this protein.

Source sequence(s)

AF416921, AL590093, DA121227

Consensus CDS

CCDS592.1

UniProtKB/Swiss-Prot

B1AQ22, D3DQ50, O75187, Q52LP1, Q53ER9, Q8WXI4, Q96DI1, Q9H883

Related

ENSP00000360366.3, ENST00000371316.3

Conserved Domains (2) summary

cd08913
Location:344 → 583

START_STARD14-like; Lipid-binding START domain of mammalian STARDT14 and related proteins

cd03442
Location:213 → 336

BFIT_BACH; Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, ...
NM_147161.4 → NP_671517.1 acyl-coenzyme A thioesterase 11 isoform 2

See identical proteins and their annotated locations for NP_671517.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) uses alternate exons in the 3' coding region and UTR, compared to variant 1. The encoded isoform (BFIT2) has a distinct C-terminus compared to isoform BFIT1.

Source sequence(s)

AK023937, AL590093

Consensus CDS

CCDS593.1

UniProtKB/Swiss-Prot

Q8WXI4

Related

ENSP00000340260.2, ENST00000343744.7

Conserved Domains (2) summary

cd08913
Location:344 → 583

START_STARD14-like; Lipid-binding START domain of mammalian STARDT14 and related proteins

cd03442
Location:213 → 336

BFIT_BACH; Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, ...