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Protein

Acyloxyacyl hydrolase

Gene

AOAH

Organism
Homo sapiens (Human)
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 (PubMed:1883828, PubMed:8089145, PubMed:29343645). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (By similarity). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (By similarity).By similarity3 Publications

Catalytic activityi

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

Cofactori

Ca2+1 PublicationNote: Binds 3 Ca2+ ions per subunit. The calcium ions probably have a structural role.1 Publication

Enzyme regulationi

Inhibited by EDTA.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi184Calcium 11 Publication1
Metal bindingi186Calcium 11 Publication1
Metal bindingi186Calcium 21 Publication1
Metal bindingi188Calcium 11 Publication1
Metal bindingi188Calcium 21 Publication1
Metal bindingi190Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi205Calcium 11 Publication1
Metal bindingi205Calcium 21 Publication1
Metal bindingi207Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi208Calcium 11 Publication1
Metal bindingi210Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi213Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi223Calcium 31 Publication1
Metal bindingi227Calcium 31 Publication1
Metal bindingi229Calcium 31 Publication1
Metal bindingi231Calcium 31 Publication1
Metal bindingi233Calcium 3; via carbonyl oxygen1 Publication1
Metal bindingi245Calcium 31 Publication1
Active sitei2632 Publications1
Binding sitei345LipopolysaccharideBy similarity1

GO - Molecular functioni

  • acyloxyacyl hydrolase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB

GO - Biological processi

  • fatty acid metabolic process Source: UniProtKB
  • lipopolysaccharide catabolic process Source: UniProtKB

Keywordsi

Molecular functionHydrolase
Biological processLipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.77 2681

Names & Taxonomyi

Protein namesi
Recommended name:
Acyloxyacyl hydrolase1 Publication (EC:3.1.1.773 Publications)
Cleaved into the following 2 chains:
Acyloxyacyl hydrolase small subunit1 Publication
Acyloxyacyl hydrolase large subunit1 Publication
Gene namesi
Name:AOAH1 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000136250.11
HGNCiHGNC:548 AOAH
MIMi102593 gene
neXtProtiNX_P28039

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi61T → A: Loss of glycosylation. No effect on enzyme activity or localization to cytoplasmic vesicles. 1 Publication1
Mutagenesisi173K → E: No effect on enzyme activity. 1 Publication1
Mutagenesisi263S → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi263S → L: Nearly abolishes catalytic activity. 1 Publication1
Mutagenesisi345R → E: No effect on enzyme activity; when associated with E-379. 1 Publication1
Mutagenesisi372G → M: Loss of enzyme activity with lipopolysaccharide, due to steric hindrance. No effect on activity with small, synthetic substrate. 1 Publication1
Mutagenesisi379K → E: No effect on enzyme activity; when associated with E-345. 1 Publication1
Mutagenesisi419P → M: Loss of enzyme activity with lipopolysaccharide, due to steric hindrance. No effect on activity with small, synthetic substrate. 1 Publication1

Organism-specific databases

DisGeNETi313
OpenTargetsiENSG00000136250
PharmGKBiPA24838

Chemistry databases

GuidetoPHARMACOLOGYi2873

Polymorphism and mutation databases

BioMutaiAOAH
DMDMi113976

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
PropeptideiPRO_000002073924 – 341 PublicationAdd BLAST11
ChainiPRO_000002074035 – 156Acyloxyacyl hydrolase small subunit1 PublicationAdd BLAST122
ChainiPRO_0000020741157 – 575Acyloxyacyl hydrolase large subunit1 PublicationAdd BLAST419

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 114PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi44 ↔ 108PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi59N-linked (GlcNAc...) asparagineCombined sources1 Publication1 Publication1
Disulfide bondi70 ↔ 83PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi123 ↔ 453Interchain (between small and large subunit)Combined sources1 Publication
Disulfide bondi160 ↔ 169Combined sources1 Publication
Disulfide bondi206 ↔ 230Combined sources1 Publication
Glycosylationi207N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi249 ↔ 329Combined sources1 Publication
Disulfide bondi376 ↔ 459Combined sources1 Publication
Glycosylationi466N-linked (GlcNAc...) asparagineCombined sources1 Publication1

Post-translational modificationi

Cleaved into a large and a small subunit.3 Publications
The small subunit is N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP28039
PaxDbiP28039
PeptideAtlasiP28039
PRIDEiP28039
ProteomicsDBi54435
54436 [P28039-2]

PTM databases

iPTMnetiP28039
PhosphoSitePlusiP28039

Expressioni

Gene expression databases

BgeeiENSG00000136250
CleanExiHS_AOAH
ExpressionAtlasiP28039 baseline and differential
GenevisibleiP28039 HS

Organism-specific databases

HPAiHPA021666
HPA026716

Interactioni

Subunit structurei

Heterodimer of the large and small subunits; disulfide-linked.3 Publications

Protein-protein interaction databases

IntActiP28039, 2 interactors
STRINGi9606.ENSP00000258749

Structurei

Secondary structure

1575
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 57Combined sources20
Helixi62 – 72Combined sources11
Helixi76 – 78Combined sources3
Helixi79 – 99Combined sources21
Helixi104 – 110Combined sources7
Beta strandi118 – 120Combined sources3
Helixi130 – 143Combined sources14
Helixi159 – 161Combined sources3
Helixi165 – 178Combined sources14
Beta strandi192 – 198Combined sources7
Turni199 – 201Combined sources3
Helixi221 – 223Combined sources3
Beta strandi224 – 226Combined sources3
Beta strandi230 – 232Combined sources3
Turni238 – 240Combined sources3
Helixi244 – 249Combined sources6
Beta strandi256 – 261Combined sources6
Turni263 – 267Combined sources5
Helixi272 – 274Combined sources3
Helixi277 – 279Combined sources3
Helixi282 – 285Combined sources4
Helixi288 – 293Combined sources6
Turni294 – 296Combined sources3
Helixi299 – 301Combined sources3
Turni303 – 305Combined sources3
Beta strandi311 – 313Combined sources3
Helixi319 – 326Combined sources8
Helixi328 – 330Combined sources3
Beta strandi334 – 338Combined sources5
Turni344 – 346Combined sources3
Helixi347 – 349Combined sources3
Helixi351 – 353Combined sources3
Turni358 – 360Combined sources3
Beta strandi364 – 369Combined sources6
Turni373 – 375Combined sources3
Beta strandi379 – 381Combined sources3
Turni383 – 385Combined sources3
Helixi389 – 404Combined sources16
Beta strandi411 – 416Combined sources6
Helixi423 – 428Combined sources6
Helixi434 – 436Combined sources3
Turni437 – 440Combined sources4
Helixi444 – 454Combined sources11
Turni460 – 462Combined sources3
Beta strandi463 – 465Combined sources3
Helixi467 – 490Combined sources24
Beta strandi496 – 501Combined sources6
Helixi505 – 514Combined sources10
Helixi519 – 522Combined sources4
Turni525 – 527Combined sources3
Beta strandi528 – 531Combined sources4
Helixi533 – 550Combined sources18
Helixi552 – 555Combined sources4
Helixi562 – 569Combined sources8
Turni570 – 573Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5W78X-ray2.27A24-152[»]
B153-575[»]
5W7CX-ray2.23A/B24-152[»]
C/D153-575[»]
ProteinModelPortaliP28039
SMRiP28039
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 118Saposin B-typePROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni38 – 70Important for enzyme activity, localization to cytoplasmic vesicles, and protein stability1 PublicationAdd BLAST33
Regioni173 – 177Lipopolysaccharide bindingBy similarity5

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFCC Eukaryota
ENOG410XTCS LUCA
GeneTreeiENSGT00390000008427
HOGENOMiHOG000008100
HOVERGENiHBG004254
InParanoidiP28039
KOiK01065
PhylomeDBiP28039
TreeFamiTF329246

Family and domain databases

InterProiView protein in InterPro
IPR001087 GDSL
IPR008138 SapB_2
IPR011001 Saposin-like
IPR008139 SaposinB_dom
PfamiView protein in Pfam
PF00657 Lipase_GDSL, 1 hit
PF03489 SapB_2, 1 hit
SMARTiView protein in SMART
SM00741 SapB, 1 hit
SUPFAMiSSF47862 SSF47862, 1 hit
PROSITEiView protein in PROSITE
PS50015 SAP_B, 1 hit

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P28039-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQSPWKILTV APLFLLLSLQ SSASPANDDQ SRPSLSNGHT CVGCVLVVSV
60 70 80 90 100
IEQLAQVHNS TVQASMERLC SYLPEKLFLK TTCYLVIDKF GSDIIKLLSA
110 120 130 140 150
DMNADVVCHT LEFCKQNTGQ PLCHLYPLPK ETWKFTLQKA RQIVKKSPIL
160 170 180 190 200
KYSRSGSDIC SLPVLAKICQ KIKLAMEQSV PFKDVDSDKY SVFPTLRGYH
210 220 230 240 250
WRGRDCNDSD ESVYPGRRPN NWDVHQDSNC NGIWGVDPKD GVPYEKKFCE
260 270 280 290 300
GSQPRGIILL GDSAGAHFHI SPEWITASQM SLNSFINLPT ALTNELDWPQ
310 320 330 340 350
LSGATGFLDS TVGIKEKSIY LRLWKRNHCN HRDYQNISRN GASSRNLKKF
360 370 380 390 400
IESLSRNKVL DYPAIVIYAM IGNDVCSGKS DPVPAMTTPE KLYSNVMQTL
410 420 430 440 450
KHLNSHLPNG SHVILYGLPD GTFLWDNLHN RYHPLGQLNK DMTYAQLYSF
460 470 480 490 500
LNCLQVSPCH GWMSSNKTLR TLTSERAEQL SNTLKKIAAS EKFTNFNLFY
510 520 530 540 550
MDFAFHEIIQ EWQKRGGQPW QLIEPVDGFH PNEVALLLLA DHFWKKVQLQ
560 570
WPQILGKENP FNPQIKQVFG DQGGH
Length:575
Mass (Da):65,105
Last modified:August 1, 1992 - v1
Checksum:iE3B3853DBD308AF7
GO
Isoform 2 (identifier: P28039-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-74: Missing.

Note: No experimental confirmation available.
Show »
Length:543
Mass (Da):61,647
Checksum:iBE14624794189A57
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti222W → C in BAD97196 (Ref. 6) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05066328D → N2 PublicationsCorresponds to variant dbSNP:rs2228410Ensembl.1
Natural variantiVAR_020133166A → T. Corresponds to variant dbSNP:rs3735384Ensembl.1
Natural variantiVAR_033513266A → G. Corresponds to variant dbSNP:rs3735386Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04257143 – 74Missing in isoform 2. 1 PublicationAdd BLAST32

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62840 mRNA Translation: AAA35506.1
AK297016 mRNA Translation: BAH12476.1
AK223476 mRNA Translation: BAD97196.1
AC083876 Genomic DNA No translation available.
AC087069 Genomic DNA No translation available.
CH236951 Genomic DNA Translation: EAL23977.1
CH471073 Genomic DNA Translation: EAW94073.1
BC025698 mRNA Translation: AAH25698.1
CCDSiCCDS5448.1 [P28039-1]
CCDS55102.1 [P28039-2]
PIRiA40292
RefSeqiNP_001170977.1, NM_001177506.1
NP_001170978.1, NM_001177507.1 [P28039-2]
NP_001628.1, NM_001637.3 [P28039-1]
UniGeneiHs.488007
Hs.689297

Genome annotation databases

EnsembliENST00000612871; ENSP00000484305; ENSG00000136250 [P28039-2]
ENST00000617537; ENSP00000483783; ENSG00000136250 [P28039-1]
GeneIDi313
KEGGihsa:313
UCSCiuc032zjw.2 human [P28039-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiAOAH_HUMAN
AccessioniPrimary (citable) accession number: P28039
Secondary accession number(s): A4D1Y5, B7Z490, Q53F13
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 20, 2018
This is version 155 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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