Aoah acyloxyacyl hydrolase [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Aoahprovided by MGI
Official Full Name: acyloxyacyl hydrolaseprovided by MGI
Primary source: MGI:MGI:1350928
See related: Ensembl:ENSMUSG00000021322 AllianceGenome:MGI:1350928
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: 4930433E13Rik
Summary: This genes encodes an enzyme that catalyzes the hydrolysis of acyloxylacyl-linked fatty acyl chains from bacterial lipopolysaccharides. The encoded protein modulates host inflammatory response to gram-negative bacteria. The proprotein is further cleaved into a large and small chain that interact in a heterodimer. Alternative splicing results in multiple transcript variants for this gene. [provided by RefSeq, Aug 2013]
Expression: Biased expression in kidney adult (RPKM 8.7), liver E18 (RPKM 1.4) and 6 other tissues See more
Orthologs: human all
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Genomic context

Location:: 13 A2; 13 7.49 cM

Exon count:: 27

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	13	NC_000079.7 (20978273..21220787)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	13	NC_000079.6 (20794103..21036617)

Chromosome 13 - NC_000079.7 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: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Acyloxyacyl hydrolase promotes pulmonary defense by preventing alveolar macrophage tolerance.
Title: Acyloxyacyl hydrolase promotes pulmonary defense by preventing alveolar macrophage tolerance.
Acyloxyacyl hydrolase deficiency induces chronic inflammation and bone loss in male mice.
Title: Acyloxyacyl hydrolase deficiency induces chronic inflammation and bone loss in male mice.
HSPA12A attenuates lipopolysaccharide-induced liver injury through inhibiting caspase-11-mediated hepatocyte pyroptosis via PGC-1alpha-dependent acyloxyacyl hydrolase expression.
Title: HSPA12A attenuates lipopolysaccharide-induced liver injury through inhibiting caspase-11-mediated hepatocyte pyroptosis via PGC-1α-dependent acyloxyacyl hydrolase expression.
AOAH remodels arachidonic acid-containing phospholipid pools in a model of interstitial cystitis pain: A MAPP Network study.
Title: AOAH remodels arachidonic acid-containing phospholipid pools in a model of interstitial cystitis pain: A MAPP Network study.
AOAH regulates bladder function and the AOAH-Crf axis is a therapeutic target for treating voiding dysfunction.
Title: Acyloxyacyl hydrolase regulates voiding activity.
By inactivating commensal LPS, AOAH thus prevents desensitization of lung epithelial cells. An enzyme that prevents severe lung inflammation/injury in Gram-negative bacterial pneumonia has the seemingly paradoxical effect of predisposing to a Th2-mediated airway disease.
Title: LPS inactivation by a host lipase allows lung epithelial cell sensitization for allergic asthma.
AOAH modulates pelvic pain severity, suggesting that allelic variation in Aoah influences pelvic pain in interstitial cystitis.
Title: Acyloxyacyl hydrolase modulates pelvic pain severity.
Alveolar macrophages increase AOAH expression upon exposure to lipopolysaccharide and that Aoah+/+ mice recover more rapidly than do Aoah-/- mice from acute lung injury induced by nasally instilled lipopolysaccharide or Klebsiella pneumonia.
Title: Acyloxyacyl hydrolase promotes the resolution of lipopolysaccharide-induced acute lung injury.
AOAH has a role in modulating microbiota signals that drive Th17 polarization and influence mucosal T-cell immunity
Title: Altered inactivation of commensal LPS due to acyloxyacyl hydrolase deficiency in colonic dendritic cells impairs mucosal Th17 immunity.
role in clearing and catabolizing both free LPS and the LPS in circulating LPS-lipoprotein complexes
Title: Hepatic uptake and deacylation of the LPS in bloodborne LPS-lipoprotein complexes.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (4)
Targeted (1) 1 citation

General gene information

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Markers

AF018172 (e-PCR)
- UniSTS:160265

38.MMHAP14FLE5.seq (e-PCR)
- UniSTS:124263

RH142109 (e-PCR)
- UniSTS:125078

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables acyloxyacyl hydrolase activity	IBA Inferred from Biological aspect of Ancestor more info
enables acyloxyacyl hydrolase activity	IDA Inferred from Direct Assay more info	PubMed
enables acyloxyacyl hydrolase activity	ISO Inferred from Sequence Orthology more info
enables calcium ion binding	IBA Inferred from Biological aspect of Ancestor more info
enables calcium ion binding	IDA Inferred from Direct Assay more info	PubMed
enables calcium ion binding	ISO Inferred from Sequence Orthology more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables hydrolase activity, acting on ester bonds	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in fatty acid metabolic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within lipid metabolic process	IEA Inferred from Electronic Annotation more info
involved_in lipopolysaccharide catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in lipopolysaccharide catabolic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within lipopolysaccharide metabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of inflammatory response	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within negative regulation of inflammatory response	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasmic vesicle	IEA Inferred from Electronic Annotation more info
located_in extracellular region	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: acyloxyacyl hydrolase

NP_001268783.1

EC 3.1.1.77

NP_036184.1

EC 3.1.1.77

XP_011242611.1

EC 3.1.1.77

XP_011242612.1

EC 3.1.1.77

XP_011242613.1

EC 3.1.1.77

XP_017171010.1

EC 3.1.1.77

XP_030103147.1

EC 3.1.1.77

XP_036013955.1

EC 3.1.1.77

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_001281854.1 → NP_001268783.1 acyloxyacyl hydrolase isoform 2 preproprotein

See identical proteins and their annotated locations for NP_001268783.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) lacks multiple 3' coding exons and contains an alternate 3' exon, resulting in a distinct 3' coding region and 3' UTR, compared to variant 1. The encoded isoform (2) is shorter and has a distinct C-terminus, compared to isoform 1.

Source sequence(s)

AC123062, AC165956, AK084452, AK150886

Consensus CDS

CCDS88418.1

UniProtKB/TrEMBL

Q5FW74

Related

ENSMUSP00000152286.2, ENSMUST00000221982.2

Conserved Domains (2) summary

smart00741
Location:39 → 113

SapB; Saposin (B) Domains

pfam03489
Location:82 → 113

SapB_2; Saposin-like type B, region 2
NM_012054.4 → NP_036184.1 acyloxyacyl hydrolase isoform 1 preproprotein

See identical proteins and their annotated locations for NP_036184.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longer transcript and encodes the longer isoform (1).

Source sequence(s)

AA763211, AC165956, AK084452

Consensus CDS

CCDS26266.1

UniProtKB/Swiss-Prot

O35298

UniProtKB/TrEMBL

Q3TAY1, Q3V0A4, Q4FK10

Related

ENSMUSP00000021757.4, ENSMUST00000021757.5

Conserved Domains (4) summary

smart00741
Location:39 → 113

SapB; Saposin (B) Domains

cd01826
Location:243 → 545

acyloxyacyl_hydrolase_like; Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a leukocyte-secreted enzyme that deacetylates bacterial lipopolysaccharides.

pfam03489
Location:82 → 113

SapB_2; Saposin-like type B, region 2

pfam11617
Location:204 → 232

Cu-binding_MopE; Putative metal-binding motif

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000079.7 Reference GRCm39 C57BL/6J

Range

20978273..21220787

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_011244309.1 → XP_011242611.1 acyloxyacyl hydrolase isoform X1

UniProtKB/TrEMBL

Q3TAY1, Q3V0A4, Q4FK10

Conserved Domains (3) summary

smart00741
Location:39 → 113

SapB; Saposin (B) Domains

cd01826
Location:243 → 533

acyloxyacyl_hydrolase_like; Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a leukocyte-secreted enzyme that deacetylates bacterial lipopolysaccharides.

pfam11617
Location:204 → 232

Cu-binding_MopE; Putative metal-binding motif
XM_017315521.1 → XP_017171010.1 acyloxyacyl hydrolase isoform X2

UniProtKB/TrEMBL

Q3TAY1, Q3V0A4, Q4FK10

Conserved Domains (3) summary

smart00741
Location:39 → 113

SapB; Saposin (B) Domains

pfam11617
Location:204 → 232

Cu-binding_MopE; Putative metal-binding motif

cl01053
Location:243 → 513

SGNH_hydrolase; or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical ...
XM_011244310.1 → XP_011242612.1 acyloxyacyl hydrolase isoform X3

UniProtKB/TrEMBL

Q3TAY1, Q3V0A4, Q4FK10

Conserved Domains (3) summary

smart00741
Location:39 → 113

SapB; Saposin (B) Domains

pfam11617
Location:204 → 232

Cu-binding_MopE; Putative metal-binding motif

cl01053
Location:243 → 508

SGNH_hydrolase; or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical ...
XM_036158062.1 → XP_036013955.1 acyloxyacyl hydrolase isoform X6

Conserved Domains (3) summary

smart00741
Location:39 → 113

SapB; Saposin (B) Domains

pfam11617
Location:204 → 232

Cu-binding_MopE; Putative metal-binding motif

cl01053
Location:243 → 282

SGNH_hydrolase; or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical ...
XM_011244311.1 → XP_011242613.1 acyloxyacyl hydrolase isoform X4

UniProtKB/TrEMBL

Q3TDB1

Conserved Domains (2) summary

cd01826
Location:143 → 433

acyloxyacyl_hydrolase_like; Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a leukocyte-secreted enzyme that deacetylates bacterial lipopolysaccharides.

pfam11617
Location:104 → 132

Cu-binding_MopE; Putative metal-binding motif
XM_030247287.1 → XP_030103147.1 acyloxyacyl hydrolase isoform X5

Conserved Domains (2) summary

pfam11617
Location:56 → 84

Cu-binding_MopE; Putative metal-binding motif

cl01053
Location:95 → 385

SGNH_hydrolase; or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical ...