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O35298 (AOAH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyloxyacyl hydrolase

EC=3.1.1.77
Gene names
Name:Aoah
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length574 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.

Subcellular location

Secreted 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 3311 By similarity
PRO_0000041812
Chain34 – 155122Acyloxyacyl hydrolase small subunit
PRO_0000041813
Chain156 – 574419Acyloxyacyl hydrolase large subunit
PRO_0000041814

Regions

Domain36 – 11782Saposin B-type

Sites

Active site2621 Potential

Amino acid modifications

Glycosylation581N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation4081N-linked (GlcNAc...) Potential
Glycosylation4651N-linked (GlcNAc...) Potential
Disulfide bond40 ↔ 113 By similarity
Disulfide bond43 ↔ 107 By similarity
Disulfide bond69 ↔ 82 By similarity

Sequences

Sequence LengthMass (Da)Tools
O35298 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 10B32C3BE772FB68

FASTA57465,155
        10         20         30         40         50         60 
MKFPWKVFKT TLLLLLLSHS LASVPSEDQP GDSYSHGQSC LGCVVLVSVI EQLAEVHNSS 

        70         80         90        100        110        120 
VQVAMERLCS YLPEKLFLKT ACYFLVQTFG SDIIKLLDEA MKADVVCYAL EFCKRGAVQP 

       130        140        150        160        170        180 
QCHLYPLPQE AWESALEKAR QVLRRSSTMK YPRSGRNICS LPFLTKICQK IELSIKKAVP 

       190        200        210        220        230        240 
FKDIDSDKHS VFPTLRGYHW RGRDCNDSDK TVYPGRRPDN WDIHQDSNCN GIWGIDPKDG 

       250        260        270        280        290        300 
IPYEKKFCEG SQPRGIILLG DSAGAHFHIP PEWLTASQMS VNSFLNLPSA LTDELNWPQL 

       310        320        330        340        350        360 
SGVTGFLDST SGIEEKSIYH RLRKRNHCNH RDYQSISKNG ASSRNLKNFI ESLSRNQASD 

       370        380        390        400        410        420 
HPAIVLYAMI GNDVCNSKAD TVPEMTTPEQ MYANVMQTLT HLNSHLPNGS HVILYGLPDG 

       430        440        450        460        470        480 
TFLWDSLHNR YHPLGQLNKD VTYAQFFSFL RCLQLNPCNG WMSSNKTLRT LTSERAEQLS 

       490        500        510        520        530        540 
NTLKKIATTE TFANFDLFYV DFAFHEIIED WQKRGGQPWQ LIEPVDGFHP NEVASLLQAN 

       550        560        570 
RVWEKIQLQW PHVLGKENPF NSQIEEVFGD QGGH 

« Hide

References

« Hide 'large scale' 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: C57B1/6.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF018172 mRNA. Translation: AAB81182.1.
AK084452 mRNA. Translation: BAC39187.1.
RefSeqNP_001268783.1. NM_001281854.1.
NP_036184.1. NM_012054.4.
UniGeneMm.314046.

3D structure databases

ProteinModelPortalO35298.
SMRO35298. Positions 38-114.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteO35298.

Proteomic databases

PaxDbO35298.
PRIDEO35298.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021757; ENSMUSP00000021757; ENSMUSG00000021322.
GeneID27052.
KEGGmmu:27052.
UCSCuc007ppu.1. mouse.

Organism-specific databases

CTD313.
MGIMGI:1350928. Aoah.

Phylogenomic databases

eggNOGNOG47076.
GeneTreeENSGT00390000008427.
HOGENOMHOG000008100.
HOVERGENHBG004254.
InParanoidO35298.
KOK01065.
OMADKYSVFP.
OrthoDBEOG75MVVQ.
PhylomeDBO35298.
TreeFamTF329246.

Enzyme and pathway databases

BRENDA3.1.1.77. 3474.

Gene expression databases

BgeeO35298.
CleanExMM_AOAH.
GenevestigatorO35298.

Family and domain databases

Gene3D1.10.225.10. 1 hit.
3.40.50.1110. 2 hits.
InterProIPR001087. Lipase_GDSL.
IPR008138. SapB_2.
IPR011001. Saposin-like.
IPR008139. SaposinB.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
PfamPF00657. Lipase_GDSL. 1 hit.
PF03489. SapB_2. 1 hit.
[Graphical view]
SMARTSM00741. SapB. 1 hit.
[Graphical view]
SUPFAMSSF47862. SSF47862. 1 hit.
PROSITEPS50015. SAP_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAOAH. mouse.
NextBio304987.
PROO35298.
SOURCESearch...

Entry information

Entry nameAOAH_MOUSE
AccessionPrimary (citable) accession number: O35298
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot