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Protein

Acyloxyacyl hydrolase

Gene

Aoah

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS) (PubMed:12810692, PubMed:15155618, PubMed:17322564, PubMed:19860560). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (PubMed:17322564, PubMed:19860560, PubMed:28622363). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (PubMed:18779055).6 Publications

Catalytic activityi

3-(acyloxy)acyl group of bacterial toxin = 3-hydroxyacyl group of bacterial toxin + a fatty acid.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei262By similarity1

GO - Molecular functioni

  • acyloxyacyl hydrolase activity Source: MGI

GO - Biological processi

  • lipopolysaccharide metabolic process Source: MGI
  • negative regulation of inflammatory response Source: MGI

Keywordsi

Molecular functionHydrolase

Enzyme and pathway databases

BRENDAi3.1.1.77 3474

Names & Taxonomyi

Protein namesi
Recommended name:
Acyloxyacyl hydrolase1 Publication (EC:3.1.1.775 Publications)
Cleaved into the following 2 chains:
Acyloxyacyl hydrolase small subunitBy similarity
Acyloxyacyl hydrolase large subunitBy similarity
Gene namesi
Name:Aoah1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1350928 Aoah

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasmic vesicle, Secreted

Pathology & Biotechi

Disruption phenotypei

Animals develop significant and prolonged hepatosplenomegaly in response to bacterial lipopolysaccharide (LPS) challenge (PubMed:17322564). Both liver and spleen show increased accumulation of leukocytes (PubMed:17322564). Significantly reduced deacylation of LPS in liver and spleen, in peritoneal macrophages, and in bone marrow-derived dendritic cells (PubMed:12810692, PubMed:17322564, PubMed:18779055). Increased lung injury, delayed neutrophil clearance, and prolonged recovery time in response to intranasal LPS administration (PubMed:28622363). Alveolar macrophages show persistent activation and cytokine levels in lung remain elevated 4-7 days after LPS administration (PubMed:28622363). Impaired response to a second infection challenge, with reduced production of the pro-inflammatory chemokines CCL5/RANTES, TNF and IL6 by peritoneal macrophages and reduced survival rates, indicating a prolonged state of immune tolerance (PubMed:18779055). This immune tolerant state can perisist for two months or longer (PubMed:18779055).4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22By similarityAdd BLAST22
PropeptideiPRO_000004181223 – 33By similarityAdd BLAST11
ChainiPRO_000004181334 – 155Acyloxyacyl hydrolase small subunitBy similarityAdd BLAST122
ChainiPRO_0000041814156 – 574Acyloxyacyl hydrolase large subunitBy similarityAdd BLAST419

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi40 ↔ 113PROSITE-ProRule annotation
Disulfide bondi43 ↔ 107PROSITE-ProRule annotation
Glycosylationi58N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi69 ↔ 82PROSITE-ProRule annotation

Post-translational modificationi

The small subunit is N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiO35298
PaxDbiO35298
PRIDEiO35298

PTM databases

iPTMnetiO35298
PhosphoSitePlusiO35298

Expressioni

Tissue specificityi

Detected in peritoneal macrophages (at protein level) (PubMed:17322564, PubMed:28622363). Strongly expressed in kidney cortex, where it may be produced by proximal tubule cells (PubMed:15155618). In liver, expressed at high levels in Kupffer cells (PubMed:17322564). Expressed by dendritic cells (PubMed:12810692). Detected at low levels in alveolar macrophages (PubMed:28622363).4 Publications

Inductioni

Strongly up-regulated in alveolar macrophages in response to bacterial lipopolysaccharides (LPS).1 Publication

Gene expression databases

BgeeiENSMUSG00000021322
CleanExiMM_AOAH
ExpressionAtlasiO35298 baseline and differential
GenevisibleiO35298 MM

Interactioni

Subunit structurei

Heterodimer of the large and small subunits; disulfide-linked.1 Publication

Structurei

Secondary structure

1574
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 57Combined sources22
Helixi61 – 71Combined sources11
Helixi75 – 77Combined sources3
Helixi78 – 97Combined sources20
Turni98 – 100Combined sources3
Helixi103 – 109Combined sources7
Helixi129 – 145Combined sources17
Helixi164 – 176Combined sources13
Beta strandi191 – 194Combined sources4
Turni198 – 200Combined sources3
Helixi220 – 222Combined sources3
Beta strandi223 – 225Combined sources3
Beta strandi229 – 231Combined sources3
Turni237 – 239Combined sources3
Helixi243 – 248Combined sources6
Beta strandi255 – 260Combined sources6
Turni262 – 266Combined sources5
Helixi271 – 273Combined sources3
Helixi276 – 278Combined sources3
Helixi281 – 284Combined sources4
Helixi287 – 292Combined sources6
Turni293 – 295Combined sources3
Helixi298 – 300Combined sources3
Turni302 – 304Combined sources3
Helixi318 – 325Combined sources8
Helixi327 – 329Combined sources3
Beta strandi333 – 337Combined sources5
Turni343 – 345Combined sources3
Helixi346 – 348Combined sources3
Helixi350 – 352Combined sources3
Turni357 – 359Combined sources3
Beta strandi363 – 368Combined sources6
Turni372 – 374Combined sources3
Helixi381 – 384Combined sources4
Helixi388 – 405Combined sources18
Beta strandi410 – 415Combined sources6
Helixi422 – 427Combined sources6
Helixi433 – 435Combined sources3
Turni436 – 439Combined sources4
Helixi443 – 452Combined sources10
Turni459 – 461Combined sources3
Beta strandi462 – 464Combined sources3
Helixi466 – 487Combined sources22
Beta strandi493 – 500Combined sources8
Helixi504 – 513Combined sources10
Helixi518 – 521Combined sources4
Turni524 – 526Combined sources3
Beta strandi527 – 530Combined sources4
Helixi532 – 549Combined sources18
Helixi551 – 554Combined sources4
Helixi561 – 568Combined sources8
Turni569 – 572Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5W7DX-ray1.75A23-574[»]
5W7EX-ray1.83A/B23-574[»]
5W7FX-ray2.80A/B23-574[»]
ProteinModelPortaliO35298
SMRiO35298
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 117Saposin B-typePROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni37 – 69Important for enzyme activity, localization to cytoplasmic vesicles, and protein stabilityBy similarityAdd BLAST33

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFCC Eukaryota
ENOG410XTCS LUCA
GeneTreeiENSGT00390000008427
HOGENOMiHOG000008100
HOVERGENiHBG004254
InParanoidiO35298
KOiK01065
OMAiSNCNGIW
OrthoDBiEOG091G03MF
PhylomeDBiO35298
TreeFamiTF329246

Family and domain databases

InterProiView protein in InterPro
IPR001087 GDSL
IPR011001 Saposin-like
IPR008139 SaposinB_dom
PfamiView protein in Pfam
PF00657 Lipase_GDSL, 1 hit
SMARTiView protein in SMART
SM00741 SapB, 1 hit
SUPFAMiSSF47862 SSF47862, 1 hit
PROSITEiView protein in PROSITE
PS50015 SAP_B, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35298-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFPWKVFKT TLLLLLLSHS LASVPSEDQP GDSYSHGQSC LGCVVLVSVI
60 70 80 90 100
EQLAEVHNSS VQVAMERLCS YLPEKLFLKT ACYFLVQTFG SDIIKLLDEA
110 120 130 140 150
MKADVVCYAL EFCKRGAVQP QCHLYPLPQE AWESALEKAR QVLRRSSTMK
160 170 180 190 200
YPRSGRNICS LPFLTKICQK IELSIKKAVP FKDIDSDKHS VFPTLRGYHW
210 220 230 240 250
RGRDCNDSDK TVYPGRRPDN WDIHQDSNCN GIWGIDPKDG IPYEKKFCEG
260 270 280 290 300
SQPRGIILLG DSAGAHFHIP PEWLTASQMS VNSFLNLPSA LTDELNWPQL
310 320 330 340 350
SGVTGFLDST SGIEEKSIYH RLRKRNHCNH RDYQSISKNG ASSRNLKNFI
360 370 380 390 400
ESLSRNQASD HPAIVLYAMI GNDVCNSKAD TVPEMTTPEQ MYANVMQTLT
410 420 430 440 450
HLNSHLPNGS HVILYGLPDG TFLWDSLHNR YHPLGQLNKD VTYAQFFSFL
460 470 480 490 500
RCLQLNPCNG WMSSNKTLRT LTSERAEQLS NTLKKIATTE TFANFDLFYV
510 520 530 540 550
DFAFHEIIED WQKRGGQPWQ LIEPVDGFHP NEVASLLQAN RVWEKIQLQW
560 570
PHVLGKENPF NSQIEEVFGD QGGH
Length:574
Mass (Da):65,155
Last modified:January 1, 1998 - v1
Checksum:i10B32C3BE772FB68
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF018172 mRNA Translation: AAB81182.1
AK084452 mRNA Translation: BAC39187.1
CCDSiCCDS26266.1
RefSeqiNP_001268783.1, NM_001281854.1
NP_036184.1, NM_012054.4
UniGeneiMm.314046

Genome annotation databases

EnsembliENSMUST00000021757; ENSMUSP00000021757; ENSMUSG00000021322
GeneIDi27052
KEGGimmu:27052
UCSCiuc007ppu.2 mouse

Similar proteinsi

Entry informationi

Entry nameiAOAH_MOUSE
AccessioniPrimary (citable) accession number: O35298
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: January 1, 1998
Last modified: March 28, 2018
This is version 113 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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