Reviewed,
UniProtKB/Swiss-Prot Q80WC9 (ACSF4_MOUSE)
Last modified
November 3, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Acyl-CoA synthetase family member 4 EC=6.2.1.- Alternative name(s): Putative aminoadipate-semialdehyde dehydrogenase EC=1.2.1.31 2-aminoadipic 6-semialdehyde dehydrogenase Protein LYS2 homolog | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 1100 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA By similarity. Putative 2-aminoadipic 6-semialdehyde dehydrogenase, which may be involved in lysine catabolism. |
| Catalytic activity | L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H. |
| Induction | According to Ref.1, it is up-regulated by lysine-rich diet, while according to Ref.6 levels of expression are not significantly changed even when diets differed markedly in PQQ and lysine content. Ref.1 Ref.6 |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. Contains 1 acyl carrier domain. |
| Caution | According to Ref.1, it may bind pyrroloquinoline quinone (PQQ) cofactor. However, their conclusions are based on prediction tools and indirect results and are not confirmed by Ref.4 and Ref.5. The relevance of PQQ-binding is therefore unclear in vivo. In invertebrates, aminoadipate-semialdehyde dehydrogenase reaction is a key step of the L-lysine biosynthesis pathway, which is not fully conserved in vertebrates. It has been suggested by Ref.1 that this protein participates in the reverse reaction (i.e. in lysine catabolism), however the relevance of this catalytic activity in vivo remains unclear. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid metabolism Lipid metabolism |
| Coding sequence diversity | Alternative splicing |
| Ligand | ATP-binding NAD Nucleotide-binding Phosphopantetheine |
| Molecular function | Ligase Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | fatty acid metabolic process Inferred from sequence or structural similarity. Source: UniProtKB oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW L-aminoadipate-semialdehyde dehydrogenase activityInferred from electronic annotation. Source: EC acid-thiol ligase activityInferred from sequence or structural similarity. Source: UniProtKB acyl carrier activityInferred from electronic annotation. Source: InterPro phosphopantetheine bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q80WC9-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q80WC9-2) The sequence of this isoform differs from the canonical sequence as follows: 368-1100: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 3 (identifier: Q80WC9-3) The sequence of this isoform differs from the canonical sequence as follows: 223-1100: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1100 | 1100 | Acyl-CoA synthetase family member 4 | PRO_0000315804 | |||||
Regions | |||||||||
| Domain | 554 – 628 | 75 | Acyl carrier | ||||||
| Nucleotide binding | 197 – 205 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 427 | 1 | ATP By similarity | ||||||
| Binding site | 441 | 1 | ATP By similarity | ||||||
| Binding site | 526 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 591 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 223 – 1100 | 878 | Missing in isoform 3. | VSP_030714 | |||||
| Alternative sequence | 368 – 1100 | 733 | Missing in isoform 2. | VSP_030715 | |||||
Sequences
| ||||||||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Nutritional biochemistry: a new redox-cofactor vitamin for mammals." Kasahara T., Kato T. Nature 422:832-832(2003) [PubMed: 12712191] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POSSIBLE FUNCTION, INDUCTION. |
| [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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-645 (ISOFORM 1). Strain: C57BL/6J. Tissue: Brain cortex and Hypothalamus. |
| [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] (ISOFORMS 1 AND 2). Tissue: Olfactory epithelium. |
| [4] | "Biochemistry: role of PQQ as a mammalian enzyme cofactor?" Felton L.M., Anthony C. Nature 433:E10-E10(2005) [PubMed: 15689995] [Abstract] Cited for: COMMENT ON PUBMED:12712191 RESULTS. |
| [5] | "Biochemistry: is pyrroloquinoline quinone a vitamin?" Rucker R., Storms D., Sheets A., Tchaparian E., Fascetti A. Nature 433:E10-E11(2005) [PubMed: 15689994] [Abstract] Cited for: COMMENT ON PUBMED:12712191 RESULTS. |
| [6] | "Pyrroloquinoline quinone nutritional status alters lysine metabolism and modulates mitochondrial DNA content in the mouse and rat." Bauerly K.A., Storms D.H., Harris C.B., Hajizadeh S., Sun M.Y., Cheung C.P., Satre M.A., Fascetti A.J., Tchaparian E., Rucker R.B. Biochim. Biophys. Acta 1760:1741-1748(2006) [PubMed: 17029795] [Abstract] Cited for: INDUCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AB095954 mRNA. Translation: BAC75954.1. AK038779 mRNA. Translation: BAE43303.1. AK043807 mRNA. Translation: BAC31660.1. BC094507 mRNA. Translation: AAH94507.1. BC128330 mRNA. Translation: AAI28331.1. | |
| IPI | IPI00265000. IPI00880667. IPI00880979. |
| RefSeq | NP_776126.1. |
| UniGene | Mm.39271 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q80WC9. |
PTM databases | |
| PhosphoSite | Q80WC9. |
Proteomic databases | |
| PRIDE | Q80WC9. |
Genome annotation databases | |
| Ensembl | ENSMUST00000069709; ENSMUSP00000069279; ENSMUSG00000055923; Mus musculus. [Genome view] ENSMUST00000120963; ENSMUSP00000113792; ENSMUSG00000055923; Mus musculus. [Genome view] |
| GeneID | 231326. |
| KEGG | mmu:231326. |
| UCSC | uc008xvi.1. mouse. uc008xvk.1. mouse. |
Organism-specific databases | |
| CTD | 231326. |
| MGI | MGI:2442517. Aasdh. |
Phylogenomic databases | |
| HOGENOM | Q80WC9. |
| HOVERGEN | Q80WC9. |
| OMA | TMRATGD. |
Enzyme and pathway databases | |
| BRENDA | 1.2.1.31. 244. |
Gene expression databases | |
| ArrayExpress | Q80WC9. |
| Bgee | Q80WC9. |
| CleanEx | MM_AASDH. |
| Genevestigator | Q80WC9. |
Family and domain databases | |
| InterPro | IPR009081. Acyl_carrier_prot-like. IPR000873. AMP-dep_Synth/Lig. IPR006162. PPantetheine_attach_site. IPR018391. PQQ_beta_propeller_repeat. IPR002372. PQQ_repeat. IPR011047. Quino_AlcDH-like. [Graphical view] |
| Gene3D | G3DSA:2.140.10.10. Quinoprotein_alc_DH-like. 1 hit. |
| Pfam | PF00501. AMP-binding. 1 hit. PF01011. PQQ. 1 hit. [Graphical view] |
| SMART | SM00564. PQQ. 6 hits. [Graphical view] |
| PROSITE | PS50075. ACP_DOMAIN. 1 hit. PS00455. AMP_BINDING. 1 hit. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 380501. |
| SOURCE | Search... |
Entry information
| Entry name | ACSF4_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q80WC9 Secondary accession number(s): Q3V3L2, Q505K4, Q8BRP4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


