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Protein

Acyloxyacyl hydrolase

Gene

Aoah

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi183Calcium 1Combined sources1 Publication1
Metal bindingi185Calcium 1Combined sources1 Publication1
Metal bindingi185Calcium 2Combined sources1 Publication1
Metal bindingi187Calcium 1Combined sources1 Publication1
Metal bindingi187Calcium 2Combined sources1 Publication1
Metal bindingi189Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi204Calcium 1Combined sources1 Publication1
Metal bindingi204Calcium 2Combined sources1 Publication1
Metal bindingi206Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi207Calcium 1Combined sources1 Publication1
Metal bindingi209Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi212Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi222Calcium 3Combined sources1 Publication1
Metal bindingi226Calcium 3Combined sources1 Publication1
Metal bindingi228Calcium 3Combined sources1 Publication1
Metal bindingi230Calcium 3Combined sources1 Publication1
Metal bindingi232Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi244Calcium 3Combined sources1 Publication1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei2621 Publication1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei344LipopolysaccharideBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processLipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.1.77 3474

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Aoah1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1350928 Aoah

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi262S → A: Loss of catalytic activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 22By similarityAdd BLAST22
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000004181223 – 33By similarityAdd BLAST11
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000004181334 – 155Acyloxyacyl hydrolase small subunitBy similarityAdd BLAST122
ChainiPRO_0000041814156 – 574Acyloxyacyl hydrolase large subunitBy similarityAdd BLAST419

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi40 ↔ 113PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi43 ↔ 107PROSITE-ProRule annotationCombined sources1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi58N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi69 ↔ 82PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi122 ↔ 452Combined sources1 Publication
Disulfide bondi122 ↔ 452Interchain (between small and large subunit)By similarity
Disulfide bondi159 ↔ 168Combined sources1 Publication
Disulfide bondi205 ↔ 229Combined sources1 Publication
Glycosylationi206N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi248 ↔ 328Combined sources1 Publication
Disulfide bondi375 ↔ 458Combined sources1 Publication
Glycosylationi408N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi465N-linked (GlcNAc...) asparagineCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Cleaved into a large and a small subunit.By similarity
The small subunit is N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O35298

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O35298

PRoteomics IDEntifications database

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PRIDEi
O35298

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O35298

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O35298

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000021322 Expressed in 57 organ(s), highest expression level in bone marrow macrophage

CleanEx database of gene expression profiles

More...
CleanExi
MM_AOAH

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O35298 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O35298 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer of the large and small subunits; disulfide-linked.2 Publications

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1574
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5W7DX-ray1.75A23-574[»]
5W7EX-ray1.83A/B23-574[»]
5W7FX-ray2.80A/B23-574[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O35298

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O35298

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini36 – 117Saposin B-typePROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni37 – 69Important for enzyme activity, localization to cytoplasmic vesicles, and protein stabilityBy similarityAdd BLAST33
Regioni172 – 176Lipopolysaccharide bindingBy similarity5

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IFCC Eukaryota
ENOG410XTCS LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000008427

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000008100

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004254

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O35298

KEGG Orthology (KO)

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KOi
K01065

Identification of Orthologs from Complete Genome Data

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OMAi
DPKDGIP

Database of Orthologous Groups

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OrthoDBi
692811at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O35298

TreeFam database of animal gene trees

More...
TreeFami
TF329246

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039676 AOAH
IPR001087 GDSL
IPR008138 SapB_2
IPR011001 Saposin-like
IPR008139 SaposinB_dom

The PANTHER Classification System

More...
PANTHERi
PTHR15010 PTHR15010, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00657 Lipase_GDSL, 1 hit
PF03489 SapB_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00741 SapB, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47862 SSF47862, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50015 SAP_B, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i10B32C3BE772FB68
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5FW74Q5FW74_MOUSE
Acyloxyacyl hydrolase
Aoah
145Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF018172 mRNA Translation: AAB81182.1
AK084452 mRNA Translation: BAC39187.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS26266.1

NCBI Reference Sequences

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RefSeqi
NP_001268783.1, NM_001281854.1
NP_036184.1, NM_012054.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.314046

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000021757; ENSMUSP00000021757; ENSMUSG00000021322

Database of genes from NCBI RefSeq genomes

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GeneIDi
27052

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:27052

UCSC genome browser

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UCSCi
uc007ppu.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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

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...

PTM databases

iPTMnetiO35298
PhosphoSitePlusiO35298

Proteomic databases

MaxQBiO35298
PaxDbiO35298
PRIDEiO35298

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
313
MGIiMGI:1350928 Aoah

Phylogenomic databases

eggNOGiENOG410IFCC Eukaryota
ENOG410XTCS LUCA
GeneTreeiENSGT00390000008427
HOGENOMiHOG000008100
HOVERGENiHBG004254
InParanoidiO35298
KOiK01065
OMAiDPKDGIP
OrthoDBi692811at2759
PhylomeDBiO35298
TreeFamiTF329246

Enzyme and pathway databases

BRENDAi3.1.1.77 3474

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Aoah mouse

Protein Ontology

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PROi
PR:O35298

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000021322 Expressed in 57 organ(s), highest expression level in bone marrow macrophage
CleanExiMM_AOAH
ExpressionAtlasiO35298 baseline and differential
GenevisibleiO35298 MM

Family and domain databases

InterProiView protein in InterPro
IPR039676 AOAH
IPR001087 GDSL
IPR008138 SapB_2
IPR011001 Saposin-like
IPR008139 SaposinB_dom
PANTHERiPTHR15010 PTHR15010, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAOAH_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O35298
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: January 1, 1998
Last modified: January 16, 2019
This is version 118 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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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