Q92038 (ACOD_CYPCA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 72.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Acyl-CoA desaturase EC=1.14.19.1 Alternative name(s): Delta(9)-desaturase Short name=Delta-9 desaturase Fatty acid desaturase Stearoyl-CoA desaturase |
| Organism | Cyprinus carpio (Common carp) |
| Taxonomic identifier | 7962 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Cyprinus![]() |
Protein attributes
| Sequence length | 327 AA. |
| Sequence status | Complete. |
| 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 By similarity. |
| Subcellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein Probable. |
| Induction | By cold. A 10-fold increase in transcript levels is observed 48-60 hours after cooling. Ref.1 |
| 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 Fatty acid metabolism Lipid biosynthesis Lipid metabolism Stress response |
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | Iron |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological_process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to stressInferred 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 |
| Molecular_function | iron ion binding Inferred from electronic annotation. Source: InterPro 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 – 327 | 327 | Acyl-CoA desaturase | PRO_0000185403 | |||||
Regions | |||||||||
| Topological domain | 2 – 38 | 37 | Cytoplasmic Potential | ||||||
| Transmembrane | 39 – 60 | 22 | Helical; Potential | ||||||
| Topological domain | 61 – 69 | 9 | Lumenal Potential | ||||||
| Transmembrane | 70 – 86 | 17 | Helical; Potential | ||||||
| Topological domain | 87 – 183 | 97 | Cytoplasmic Potential | ||||||
| Transmembrane | 184 – 202 | 19 | Helical; Potential | ||||||
| Topological domain | 203 – 217 | 15 | Lumenal Potential | ||||||
| Transmembrane | 218 – 240 | 23 | Helical; Potential | ||||||
| Topological domain | 241 – 327 | 87 | Cytoplasmic Potential | ||||||
| Motif | 87 – 92 | 6 | Histidine box-1 | ||||||
| Motif | 124 – 128 | 5 | Histidine box-2 | ||||||
| Motif | 265 – 269 | 5 | Histidine box-3 | ||||||
Sequences
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References
| [1] | "Cold-induced expression of delta 9-desaturase in carp by transcriptional and posttranslational mechanisms." Tiku P.E., Gracey A.Y., Macartney A.I., Beynon R.J., Cossins A.R. Science 271:815-818(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. Tissue: Liver. |
| [2] | Tiku P.E. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 11-25 AND C-TERMINUS. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U31864 mRNA. Translation: AAB03857.2. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG003367. |
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. |
| PROSITE | PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACOD_CYPCA | ||||||||
| Accession | Primary (citable) accession number: Q92038 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
