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Reviewed, UniProtKB/Swiss-Prot P28039 (AOAH_HUMAN)

Last modified November 3, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acyloxyacyl hydrolase
    EC=3.1.1.77
Cleaved into the following 2 chains:
    1- Recommended name:
            Acyloxyacyl hydrolase small subunit
    2- Recommended name:
            Acyloxyacyl hydrolase large subunit
Gene names
Name: AOAH
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides.

Catalytic activity

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

Subunit structure

Heterodimer.

Post-translational modification

Both subunits contain a number of cysteine residues that may form disulfide bridges.

Sequence similarities

Contains 1 saposin B-type domain.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processinflammatory response Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionacyloxyacyl hydrolase activity

Inferred from electronic annotation. Source: EC

lipoprotein lipase activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 3411
PRO_0000020739
Chain35 – 156122Acyloxyacyl hydrolase small subunit
PRO_0000020740
Chain157 – 575419Acyloxyacyl hydrolase large subunit
PRO_0000020741

Regions

Domain37 – 11882Saposin B-type

Sites

Active site2631 Potential

Amino acid modifications

Glycosylation591N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential
Disulfide bond41 ↔ 114 By similarity
Disulfide bond44 ↔ 108 By similarity
Disulfide bond70 ↔ 83 By similarity
Disulfide bond123 ↔ ?

Natural variations

Natural variant281D → N: dbSNP rs11976480.
VAR_050663
Natural variant1661A → T: dbSNP rs3735384.
VAR_020133
Natural variant2661A → G: dbSNP rs3735386.
VAR_033513

Experimental info

Sequence conflict2221W → C in BAD97196. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P28039-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: E3B3853DBD308AF7

FASTA57565,105
        10         20         30         40         50         60 
MQSPWKILTV APLFLLLSLQ SSASPANDDQ SRPSLSNGHT CVGCVLVVSV IEQLAQVHNS 

        70         80         90        100        110        120 
TVQASMERLC SYLPEKLFLK TTCYLVIDKF GSDIIKLLSA DMNADVVCHT LEFCKQNTGQ 

       130        140        150        160        170        180 
PLCHLYPLPK ETWKFTLQKA RQIVKKSPIL KYSRSGSDIC SLPVLAKICQ KIKLAMEQSV 

       190        200        210        220        230        240 
PFKDVDSDKY SVFPTLRGYH WRGRDCNDSD ESVYPGRRPN NWDVHQDSNC NGIWGVDPKD 

       250        260        270        280        290        300 
GVPYEKKFCE GSQPRGIILL GDSAGAHFHI SPEWITASQM SLNSFINLPT ALTNELDWPQ 

       310        320        330        340        350        360 
LSGATGFLDS TVGIKEKSIY LRLWKRNHCN HRDYQNISRN GASSRNLKKF IESLSRNKVL 

       370        380        390        400        410        420 
DYPAIVIYAM IGNDVCSGKS DPVPAMTTPE KLYSNVMQTL KHLNSHLPNG SHVILYGLPD 

       430        440        450        460        470        480 
GTFLWDNLHN RYHPLGQLNK DMTYAQLYSF LNCLQVSPCH GWMSSNKTLR TLTSERAEQL 

       490        500        510        520        530        540 
SNTLKKIAAS EKFTNFNLFY MDFAFHEIIQ EWQKRGGQPW QLIEPVDGFH PNEVALLLLA 

       550        560        570 
DHFWKKVQLQ WPQILGKENP FNPQIKQVFG DQGGH 

« Hide

References

« Hide 'large scale' references
[1]"Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides."
Hagen F.S., Grant F.J., Kuijper J.L., Slaughter C.A., Moomaw C.R., Orth K., O'Hara P.J., Munford R.S.
Biochemistry 30:8415-8423(1991) [PubMed: 1883828] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-49 AND 157-185.
[2]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Synovial cell.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
+Additional computationally mapped references.

Cross-references

Sequence databases

M62840 mRNA. Translation: AAA35506.1.
AK223476 mRNA. Translation: BAD97196.1.
BC025698 mRNA. Translation: AAH25698.1.
IPIIPI00000731.
PIRA40292.
RefSeqNP_001628.1.
UniGeneHs.488007

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP28039.

Proteomic databases

PRIDEP28039.

Genome annotation databases

EnsemblENST00000258749; ENSP00000258749; ENSG00000136250; Homo sapiens. [Genome view]
ENST00000414637; ENSP00000416472; ENSG00000136250; Homo sapiens. [Genome view]
ENST00000431169; ENSP00000405683; ENSG00000136250; Homo sapiens. [Genome view]
ENST00000435386; ENSP00000416051; ENSG00000136250; Homo sapiens. [Genome view]
GeneID313.
KEGGhsa:313.
UCSCuc003tfh.2. human.

Organism-specific databases

CTD313.
GeneCardsGC07M036519.
H-InvDBHIX0006604.
HGNCHGNC:548. AOAH.
MIM102593. gene.
PharmGKBPA24838.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP28039.
HOVERGENP28039.
OMARNHCNHR.

Enzyme and pathway databases

BRENDA3.1.1.77. 247.

Gene expression databases

ArrayExpressP28039.
BgeeP28039.
CleanExHS_AOAH.
GenevestigatorP28039.
GermOnlineENSG00000136250. Homo sapiens.

Family and domain databases

InterProIPR001087. Lipase_GDSL.
IPR008265. Lipase_GDSL_AS.
IPR008138. SapB_2.
IPR011001. Saposin-like.
IPR008139. SaposinB.
[Graphical view]
Gene3DG3DSA:1.10.225.10. Saposin_like. 1 hit.
PfamPF00657. Lipase_GDSL. 1 hit.
PF03489. SapB_2. 1 hit.
[Graphical view]
SMARTSM00741. SapB. 1 hit.
[Graphical view]
PROSITEPS01098. LIPASE_GDSL_SER. False negative.
PS50015. SAP_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio1273.
SOURCESearch...

Entry information

Entry nameAOAH_HUMAN
AccessionPrimary (citable) accession number: P28039
Secondary accession number(s): Q53F13
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 3, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents