Reviewed,
UniProtKB/Swiss-Prot P13516 (ACOD1_MOUSE)
Last modified
June 16, 2009.
Version 92.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Acyl-CoA desaturase 1 EC=1.14.19.1 Alternative name(s): Stearoyl-CoA desaturase 1 Fatty acid desaturase 1 Delta(9)-desaturase 1 | ||
| 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 | 355 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O2 and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA. |
| Catalytic activity | Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O. |
| Cofactor | Iron. |
| Subcellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein Probable. |
| Domain | The histidine box domains may contain the active site and/or be involved in metal ion binding. |
| Sequence similarities | Belongs to the fatty acid desaturase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Transmembrane |
| Ligand | Iron |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | brown fat cell differentiation Inferred from direct assay. Source: MGI fatty acid biosynthetic processInferred from mutant phenotype. Source: MGI oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW white fat cell differentiationInferred from direct assay. Source: MGI |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW stearoyl-CoA 9-desaturase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 355 | 355 | Acyl-CoA desaturase 1 | PRO_0000185397 | |||||
Regions | |||||||||
| Transmembrane | 72 – 92 | 21 | Potential | ||||||
| Transmembrane | 94 – 114 | 21 | Potential | ||||||
| Transmembrane | 219 – 239 | 21 | Potential | ||||||
| Transmembrane | 311 – 331 | 21 | Potential | ||||||
| Motif | 116 – 121 | 6 | Histidine box-1 | ||||||
| Motif | 153 – 157 | 5 | Histidine box-2 | ||||||
| Motif | 294 – 298 | 5 | Histidine box-3 | ||||||
Experimental info | |||||||||
| Sequence conflict | 97 | 1 | C → A in AAA40103. Ref.1 | ||||||
| Sequence conflict | 148 | 1 | E → D in AAA40103. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Differentiation-induced gene expression in 3T3-L1 preadipocytes. Characterization of a differentially expressed gene encoding stearoyl-CoA desaturase." Ntambi J.M., Buhrow S.A., Kaestner K.H., Christy R.J., Sibley E., Kelly T.J. Jr., Lane M.D. J. Biol. Chem. 263:17291-17300(1988) [PubMed: 2903162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Adipocyte. |
| [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
M21285 M21284 Genomic DNA. Translation: AAA40103.1. BC007474 mRNA. Translation: AAH07474.1. BC055453 mRNA. Translation: AAH55453.1. | |
| IPI | IPI00322530. |
| PIR | A32115. |
| RefSeq | NP_033153.2. |
| UniGene | Mm.267377 |
3D structure databases | |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P13516. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000037071. Mus musculus. [Contig view] |
| GeneID | 20249. |
| KEGG | mmu:20249. |
Organism-specific databases | |
| MGI | MGI:98239. Scd1. |
Phylogenomic databases | |
| HOGENOM | P13516. |
| HOVERGEN | P13516. |
| OMA | P13516. EEMSSSY. |
Enzyme and pathway databases | |
| BRENDA | 1.14.19.1. 244. |
Gene expression databases | |
| ArrayExpress | P13516. |
| Bgee | P13516. |
| CleanEx | MM_SCD1. |
| GermOnline | ENSMUSG00000037071. Mus musculus. |
Family and domain databases | |
| InterPro | IPR005804. Fatty_acid_desaturase-1. IPR001522. Fatty_acid_desaturase-1_C. IPR015876. Fatty_acid_desaturase-1_core. [Graphical view] |
| Pfam | PF00487. FA_desaturase. 1 hit. [Graphical view] |
| PRINTS | PR00075. FACDDSATRASE. |
| ProDom | PD002221. Desaturase. 1 hit. PD001081. FA_desat_sub. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 297897. |
| SOURCE | Search... |
Entry information
| Entry name | ACOD1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P13516 Secondary accession number(s): Q922I6 | ||||||||
| Entry history |
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| 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


