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Reviewed, UniProtKB/Swiss-Prot O18823 (AOAH_RABIT)

Last modified September 1, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

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

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Heterodimer By similarity.

Post-translational modification

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

Sequence similarities

Contains 1 saposin B-type domain.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processlipid metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionacyloxyacyl hydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 349 By similarity
PRO_0000041815
Chain35 – 156122Acyloxyacyl hydrolase small subunit
PRO_0000041816
Chain157 – 575419Acyloxyacyl hydrolase large subunit
PRO_0000041817

Regions

Domain36 – 11782Saposin B-type

Sites

Active site2621 Potential

Amino acid modifications

Glycosylation581N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential
Disulfide bond40 ↔ 113 By similarity
Disulfide bond43 ↔ 107 By similarity
Disulfide bond69 ↔ 82 By similarity

Sequences

Sequence LengthMass (Da)Tools
O18823-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 5AB2CDADE568492B

FASTA57565,053
        10         20         30         40         50         60 
MKSPWRILVV SPLLLLPLHS STSRAHDNQP GTIRSDHYTC VGCVLVVSVI EQLAQVHNST 

        70         80         90        100        110        120 
VQASMERLCS YLPEEWVLKT ACYMMVHVFG ADIIKLFDKD VNADVVCHTL EFCKQEPGQP 

       130        140        150        160        170        180 
LCHLYPLPKE SWKFTLEKAR HIVKQSPIMK YTRSGAGICS LPFLAKICQK IKLAIKNSVP 

       190        200        210        220        230        240 
IKDVDSDKYS IFPTLRGYHW RGRDCNDSDK TVYPGRRPDN WDAHRDSNCN GIWGVDPKDG 

       250        260        270        280        290        300 
IPYEKKFCEG SQPRGIILLG DSAGAHFHIP PEWLTVSQMS VNSFLNLPTA VTNELDWPQL 

       310        320        330        340        350        360 
SGTTGFLDSA SKIKENSIYL RLRKRNRCNH RDYQNISKNG ASSRNVKSLI ESLSRNQLLD 

       370        380        390        400        410        420 
HPAIVIYAMI GNDVCNGRKT DPVSAMTTPE QLYANVLKML EALNSHLPTG SHVILYGLAH 

       430        440        450        460        470        480 
GAFLWDTLHS RYHPLGQLNK DVTYTQLYSF LGCLQVSPCP GWMSANETLR ALTSERAQQL 

       490        500        510        520        530        540 
SETLRKIAAS KKFTNFNLFY LDFAFQEVVE EWQKMGGQPW ELIEAVDGFH PNEVALLLFA 

       550        560        570 
DQLWEKVQRQ WPDVLGKENP FNPQIEEVFG DQGGH 

« Hide

References

[1]"Human, murine, and lapine acyloxyacyl hydrolases share unique structural features."
Munford R.S., Fosmire S., Varley A.W., Staab J.F.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.

Cross-references

Sequence databases

AF018173 mRNA. Translation: AAB81183.1.
RefSeqNP_001075494.1.
UniGeneOcu.2181

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID100008662.

Organism-specific databases

CTD100008662.

Phylogenomic databases

HOVERGENO18823.

Enzyme and pathway databases

BRENDA3.1.1.77. 255.

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...

Entry information

Entry nameAOAH_RABIT
AccessionPrimary (citable) accession number: O18823
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: January 1, 1998
Last modified: September 1, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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