UniProtKB - P07308 (ACOD1_RAT)
Acyl-CoA desaturase 1
Scd1
Functioni
Stearoyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:2892838, PubMed:7947684).
Catalyzes the insertion of a cis double bond at the Delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:2892838, PubMed:7947684).
Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity).
Plays an important role in body energy homeostasis (By similarity).
Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (PubMed:7947684).
Required for normal development of sebaceous glands. Required for the biosynthesis of normal levels of Delta-9 unsaturated fatty acids and 1-alkyl-2,3-diacylglycerol in the Harderian gland. Required for normal production of meibum, an oily material that prevents drying of the cornea (By similarity).
By similarity2 PublicationsMiscellaneous
Catalytic activityi
- 2 Fe(II)-[cytochrome b5] + 2 H+ + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O2 PublicationsEC:1.14.19.12 Publications
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 74 | SubstrateBy similarity | 1 | |
Metal bindingi | 119 | Iron 1By similarity | 1 | |
Metal bindingi | 124 | Iron 1By similarity | 1 | |
Binding sitei | 147 | SubstrateBy similarity | 1 | |
Binding sitei | 154 | SubstrateBy similarity | 1 | |
Binding sitei | 155 | SubstrateBy similarity | 1 | |
Metal bindingi | 156 | Iron 1By similarity | 1 | |
Metal bindingi | 159 | Iron 2By similarity | 1 | |
Metal bindingi | 160 | Iron 1By similarity | 1 | |
Binding sitei | 187 | SubstrateBy similarity | 1 | |
Binding sitei | 188 | SubstrateBy similarity | 1 | |
Binding sitei | 261 | SubstrateBy similarity | 1 | |
Metal bindingi | 268 | Iron 2By similarity | 1 | |
Metal bindingi | 297 | Iron 2By similarity | 1 | |
Metal bindingi | 300 | Iron 1By similarity | 1 | |
Metal bindingi | 301 | Iron 2By similarity | 1 |
GO - Molecular functioni
- iron ion binding Source: UniProtKB
- metal ion binding Source: RGD
- oxidoreductase activity Source: UniProtKB
- palmitoyl-CoA 9-desaturase activity Source: RGD
- stearoyl-CoA 9-desaturase activity Source: UniProtKB
GO - Biological processi
- brown fat cell differentiation Source: RGD
- cholesterol esterification Source: RGD
- defense response to Gram-positive bacterium Source: RGD
- fatty acid biosynthetic process Source: RGD
- lipid biosynthetic process Source: RGD
- lipid homeostasis Source: RGD
- monounsaturated fatty acid biosynthetic process Source: RGD
- positive regulation of cold-induced thermogenesis Source: YuBioLab
- regulation of water loss via skin Source: RGD
- response to bacterium Source: RGD
- response to fatty acid Source: UniProtKB
- sebaceous gland development Source: RGD
- sterol esterification Source: RGD
- tarsal gland development Source: RGD
- triglyceride metabolic process Source: RGD
- unsaturated fatty acid biosynthetic process Source: UniProtKB
- white fat cell differentiation Source: RGD
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Ligand | Iron, Metal-binding |
Enzyme and pathway databases
BRENDAi | 1.14.19.1, 5301 |
Names & Taxonomyi
Protein namesi | Recommended name: Acyl-CoA desaturase 1 (EC:1.14.19.12 Publications)Alternative name(s): Delta(9)-desaturase 1Curated Short name: Delta-9 desaturase 1Curated Fatty acid desaturase 1 Stearoyl-CoA desaturase 11 Publication |
Gene namesi | Name:Scd1 Synonyms:Scd |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 621176, Scd1 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Curated
Other locations
- Membrane 1 Publication; Multi-pass membrane protein 1 Publication
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: UniProtKB
- integral component of endoplasmic reticulum membrane Source: RGD
Other locations
- integral component of membrane Source: UniProtKB
- intracellular membrane-bounded organelle Source: RGD
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 71 | CytoplasmicBy similarityAdd BLAST | 71 | |
Transmembranei | 72 – 92 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 93 – 96 | LumenalBy similarity | 4 | |
Transmembranei | 97 – 117 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 118 – 216 | CytoplasmicBy similarityAdd BLAST | 99 | |
Transmembranei | 217 – 236 | HelicalBy similarityAdd BLAST | 20 | |
Topological domaini | 237 – 240 | LumenalBy similarity | 4 | |
Transmembranei | 241 – 262 | HelicalBy similarityAdd BLAST | 22 | |
Topological domaini | 263 – 358 | CytoplasmicBy similarityAdd BLAST | 96 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 119 | H → A: Abolishes enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 124 | H → A: Abolishes enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 156 | H → A: Abolishes enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 157 | R → N: No effect on enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 159 | H → A: Abolishes enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 160 | H → A: Abolishes enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 166 | H → A: No effect on enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 170 | H → A: No effect on enzyme activity; when associated with H-173. 1 Publication | 1 | |
Mutagenesisi | 173 | R → H: No effect on enzyme activity; when associated with A-170. 1 Publication | 1 | |
Mutagenesisi | 297 | H → A: Abolishes enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 300 | H → A: Abolishes enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 301 | H → A: Abolishes enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 315 | H → A: No effect on enzyme activity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL5424 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000185400 | 1 – 358 | Acyl-CoA desaturase 1Add BLAST | 358 |
Proteomic databases
jPOSTi | P07308 |
PaxDbi | P07308 |
PeptideAtlasi | P07308 |
PTM databases
iPTMneti | P07308 |
PhosphoSitePlusi | P07308 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSRNOG00000013552, Expressed in liver and 22 other tissues |
Genevisiblei | P07308, RN |
Interactioni
Protein-protein interaction databases
BioGRIDi | 251497, 1 interactor |
STRINGi | 10116.ENSRNOP00000018447 |
Chemistry databases
BindingDBi | P07308 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 8 – 33 | DisorderedSequence analysisAdd BLAST | 26 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 119 – 124 | Histidine box-1Curated | 6 | |
Motifi | 156 – 160 | Histidine box-2Curated | 5 | |
Motifi | 297 – 301 | Histidine box-3Curated | 5 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 8 – 27 | Polar residuesSequence analysisAdd BLAST | 20 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1600, Eukaryota |
GeneTreei | ENSGT00940000162971 |
HOGENOMi | CLU_027359_0_0_1 |
InParanoidi | P07308 |
OMAi | QGFRWWE |
OrthoDBi | 971318at2759 |
Family and domain databases
CDDi | cd03505, Delta9-FADS-like, 1 hit |
InterProi | View protein in InterPro IPR015876, Acyl-CoA_DS IPR005804, FA_desaturase_dom IPR001522, FADS-1_CS |
PANTHERi | PTHR11351, PTHR11351, 1 hit |
Pfami | View protein in Pfam PF00487, FA_desaturase, 1 hit |
PRINTSi | PR00075, FACDDSATRASE |
PROSITEi | View protein in PROSITE PS00476, FATTY_ACID_DESATUR_1, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MPAHMLQEIS SSYTTTTTIT EPPSGNLQNG REKMKKVPLY LEEDIRPEMR
60 70 80 90 100
EDIHDPSYQD EEGPPPKLEY VWRNIILMAL LHVGALYGIT LIPSSKVYTL
110 120 130 140 150
LWGIFYYLIS ALGITAGAHR LWSHRTYKAR LPLRIFLIIA NTMAFQNDVY
160 170 180 190 200
EWARDHRAHH KFSETHADPH NSRRGFFFSH VGWLLVRKHP AVKEKGGKLD
210 220 230 240 250
MSDLKAEKLV MFQRRYYKPG LLLMCFILPT LVPWYCWGET FLHSLFVSTF
260 270 280 290 300
LRYTLVLNAT WLVNSAAHLY GYRPYDKNIQ SRENILVSLG AVGEGFHNYH
310 320 330 340 350
HAFPYDYSAS EYRWHINFTT FFIDCMAALG LAYDRKKVSK AAVLARIKRT
GDGSHKSS
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 291 | A → S in AAA42116 (PubMed:2428815).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J02585 mRNA Translation: AAA42116.1 AF509568 mRNA Translation: AAM34745.1 AF509569 mRNA Translation: AAM34746.1 |
PIRi | A24699 |
RefSeqi | NP_631931.2, NM_139192.2 XP_006231495.1, XM_006231433.2 |
Genome annotation databases
Ensembli | ENSRNOT00000018447; ENSRNOP00000018447; ENSRNOG00000013552 |
GeneIDi | 246074 |
KEGGi | rno:246074 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J02585 mRNA Translation: AAA42116.1 AF509568 mRNA Translation: AAM34745.1 AF509569 mRNA Translation: AAM34746.1 |
PIRi | A24699 |
RefSeqi | NP_631931.2, NM_139192.2 XP_006231495.1, XM_006231433.2 |
3D structure databases
SMRi | P07308 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 251497, 1 interactor |
STRINGi | 10116.ENSRNOP00000018447 |
Chemistry databases
BindingDBi | P07308 |
ChEMBLi | CHEMBL5424 |
PTM databases
iPTMneti | P07308 |
PhosphoSitePlusi | P07308 |
Proteomic databases
jPOSTi | P07308 |
PaxDbi | P07308 |
PeptideAtlasi | P07308 |
Genome annotation databases
Ensembli | ENSRNOT00000018447; ENSRNOP00000018447; ENSRNOG00000013552 |
GeneIDi | 246074 |
KEGGi | rno:246074 |
Organism-specific databases
CTDi | 6319 |
RGDi | 621176, Scd1 |
Phylogenomic databases
eggNOGi | KOG1600, Eukaryota |
GeneTreei | ENSGT00940000162971 |
HOGENOMi | CLU_027359_0_0_1 |
InParanoidi | P07308 |
OMAi | QGFRWWE |
OrthoDBi | 971318at2759 |
Enzyme and pathway databases
BRENDAi | 1.14.19.1, 5301 |
Miscellaneous databases
PROi | PR:P07308 |
Gene expression databases
Bgeei | ENSRNOG00000013552, Expressed in liver and 22 other tissues |
Genevisiblei | P07308, RN |
Family and domain databases
CDDi | cd03505, Delta9-FADS-like, 1 hit |
InterProi | View protein in InterPro IPR015876, Acyl-CoA_DS IPR005804, FA_desaturase_dom IPR001522, FADS-1_CS |
PANTHERi | PTHR11351, PTHR11351, 1 hit |
Pfami | View protein in Pfam PF00487, FA_desaturase, 1 hit |
PRINTSi | PR00075, FACDDSATRASE |
PROSITEi | View protein in PROSITE PS00476, FATTY_ACID_DESATUR_1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ACOD1_RAT | |
Accessioni | P07308Primary (citable) accession number: P07308 Secondary accession number(s): Q8JZL5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1988 |
Last sequence update: | November 23, 2004 | |
Last modified: | February 23, 2022 | |
This is version 170 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families