Q8VD66 (ABHD4_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 77.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Abhydrolase domain-containing protein 4 EC=3.1.1.- Alternative name(s): Alpha/beta-hydrolase 4 Lyso-N-acylphosphatidylethanolamine lipase | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 342 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains. Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine. Ref.3 |
| Tissue specificity | Highest levels in the CNS and in testis, intermediate levels in liver and kidney. Hardly detectable in heart. Ref.3 |
| Sequence similarities | Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily. |
| Caution | Thr-291 is present instead of the conserved His which is expected to be an active site residue. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation Lipid metabolism |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 342 | 342 | Abhydrolase domain-containing protein 4 | PRO_0000080865 | |||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "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.  Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. |
| [2] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye. |
| [3] | "Endocannabinoid biosynthesis proceeding through glycerophospho-N-acyl ethanolamine and a role for alpha/beta hydrolase 4 in this pathway." Simon G.M., Cravatt B.F. J. Biol. Chem. 281:26465-26472(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AK049366 mRNA. Translation: BAC33711.1. BC017532 mRNA. Translation: AAH17532.1. |
| IPI | IPI00122628. |
| RefSeq | NP_001192110.1. NM_001205181.1. NP_598837.2. NM_134076.2. |
| UniGene | Mm.28771. |
3D structure databases | |
| ProteinModelPortal | Q8VD66. |
| SMR | Q8VD66. Positions 71-169. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10090.ENSMUSP00000044134. |
Protein family/group databases | |
| MEROPS | S33.013. |
PTM databases | |
| PhosphoSite | Q8VD66. |
Proteomic databases | |
| PaxDb | Q8VD66. |
| PRIDE | Q8VD66. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 105501. |
| KEGG | mmu:105501. |
| UCSC | uc007tvo.2. mouse. |
Organism-specific databases | |
| CTD | 63874. |
| MGI | MGI:1915938. Abhd4. |
Phylogenomic databases | |
| eggNOG | COG0596. |
| HOVERGEN | HBG054445. |
| InParanoid | Q8VD66. |
| KO | K13698. |
| OrthoDB | EOG4NVZKQ. |
Gene expression databases | |
| ArrayExpress | Q8VD66. |
| Bgee | Q8VD66. |
| CleanEx | MM_ABHD4. |
| Genevestigator | Q8VD66. |
| GermOnline | ENSMUSG00000040997. Mus musculus. |
Family and domain databases | |
| InterPro | IPR000073. AB_hydrolase_1. [Graphical view] |
| PRINTS | PR00111. ABHYDROLASE. |
| ProtoNet | Search... |
Other | |
| NextBio | 357734. |
| SOURCE | Search... |
Entry information
| Entry name | ABHD4_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8VD66 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |