Reviewed,
UniProtKB/Swiss-Prot Q6P7B9 (ACOD2_RAT)
Last modified
June 16, 2009.
Version 43.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Acyl-CoA desaturase 2 EC=1.14.19.1 Alternative name(s): Stearoyl-CoA desaturase 2 Fatty acid desaturase 2 Delta(9)-desaturase 2 | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 358 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 By similarity. |
| 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 | fatty acid biosynthetic process Traceable author statement. Source: RGD myelinationInferred from expression pattern. Source: RGD oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW microsomeTraceable author statement. Source: RGD |
| Molecular function | iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW stearoyl-CoA 9-desaturase activityInferred from direct assay. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 358 | 358 | Acyl-CoA desaturase 2 | PRO_0000185401 | |||||
Regions | |||||||||
| Transmembrane | 75 – 95 | 21 | Potential | ||||||
| Transmembrane | 97 – 117 | 21 | Potential | ||||||
| Transmembrane | 222 – 242 | 21 | Potential | ||||||
| Transmembrane | 314 – 334 | 21 | Potential | ||||||
| Motif | 119 – 124 | 6 | Histidine box-1 | ||||||
| Motif | 156 – 160 | 5 | Histidine box-2 | ||||||
| Motif | 297 – 301 | 5 | Histidine box-3 | ||||||
Experimental info | |||||||||
| Sequence conflict | 76 | 1 | V → I in BAA92436. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning and tissue expression of rat stearoyl-CoA desaturase 2." Hoshino T., Ishiguro K., Ohtsu K. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [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: Prostate. |
| [3] | "Identification of novel mRNAs expressed in oligodendrocytes." Baba H., Fuss B., Watson J.B., Zane L.T., Macklin W.B. Neurochem. Res. 19:1091-1099(1994) [PubMed: 7800118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-60. |
Cross-references
Sequence databases | |
|---|---|
| AB032243 mRNA. Translation: BAA92436.1. BC061737 mRNA. Translation: AAH61737.1. S75730 mRNA. Translation: AAB32826.1. | |
| IPI | IPI00464460. |
| RefSeq | NP_114029.1. |
| UniGene | Rn.83595 |
3D structure databases | |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q6P7B9. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000013279. Rattus norvegicus. [Contig view] |
| GeneID | 83792. |
| KEGG | rno:83792. |
Organism-specific databases | |
| RGD | 621177. Scd2. |
Phylogenomic databases | |
| HOVERGEN | Q6P7B9. |
Enzyme and pathway databases | |
| BRENDA | 1.14.19.1. 248. |
Gene expression databases | |
| ArrayExpress | Q6P7B9. |
| GermOnline | ENSRNOG00000013279. Rattus norvegicus. |
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 | 616377. |
Entry information
| Entry name | ACOD2_RAT | ||||||||
| Accession | Primary (citable) accession number: Q6P7B9 Secondary accession number(s): Q64066, Q9JMC9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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