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Protein

Acyl-CoA desaturase 1

Gene

Scd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Stearyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. 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:11500518, PubMed:11533264, PubMed:16275639, PubMed:16443825, PubMed:26098370). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:11500518, PubMed:11533264, PubMed:16443825, PubMed:26098370). Plays an important role in lipid biosynthesis (PubMed:17127673, PubMed:10899171, PubMed:11500518, PubMed:11441127, PubMed:11533264, PubMed:12177411, PubMed:26098370). Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (PubMed:12177411, PubMed:17127673, PubMed:24356954, PubMed:24295027). Plays an important role in body energy homeostasis (PubMed:17127673, PubMed:15210843, PubMed:24295027, PubMed:24356954). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (PubMed:10899171, PubMed:11500518, PubMed:11441127, PubMed:11533264, PubMed:12177411, PubMed:15210843, PubMed:26098370). Required for normal development of sebaceous glands (PubMed:17738154, PubMed:11533264). Required for the biosynthesis of normal levels of delta-9 unsaturated fatty acids and 1-alkyl-2,3-diacylglycerol in the Harderian gland (PubMed:11500518). Required for normal production of meibum, an oily material that prevents drying of the cornea (PubMed:11533264).2 Publications10 Publications

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.6 Publications

Cofactori

Fe2+1 PublicationNote: Expected to bind 2 Fe2+ ions per subunit, instead of the Zn2+ ions seen in the 3D-structure.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711Substrate1 Publication
Metal bindingi116 – 1161Iron 11 Publication
Metal bindingi121 – 1211Iron 11 Publication
Binding sitei144 – 1441Substrate1 Publication
Binding sitei151 – 1511Substrate1 Publication
Binding sitei152 – 1521Substrate1 Publication
Metal bindingi153 – 1531Iron 11 Publication
Metal bindingi156 – 1561Iron 21 Publication
Metal bindingi157 – 1571Iron 11 Publication
Binding sitei184 – 1841Substrate1 Publication
Binding sitei185 – 1851Substrate1 Publication
Binding sitei258 – 2581Substrate1 Publication
Metal bindingi265 – 2651Iron 21 Publication
Metal bindingi294 – 2941Iron 21 Publication
Metal bindingi297 – 2971Iron 11 Publication
Metal bindingi298 – 2981Iron 21 Publication

GO - Molecular functioni

  • iron ion binding Source: UniProtKB
  • metal ion binding Source: UniProtKB
  • oxidoreductase activity Source: MGI
  • palmitoyl-CoA 9-desaturase activity Source: UniProtKB
  • stearoyl-CoA 9-desaturase activity Source: UniProtKB

GO - Biological processi

  • brown fat cell differentiation Source: MGI
  • cholesterol esterification Source: UniProtKB
  • defense response to Gram-positive bacterium Source: MGI
  • fatty acid biosynthetic process Source: MGI
  • monounsaturated fatty acid biosynthetic process Source: UniProtKB
  • negative regulation of growth of symbiont in host Source: MGI
  • positive regulation of cholesterol esterification Source: BHF-UCL
  • regulation of water loss via skin Source: UniProtKB
  • response to fatty acid Source: Ensembl
  • sebaceous gland development Source: UniProtKB
  • sterol esterification Source: UniProtKB
  • tarsal gland development Source: UniProtKB
  • triglyceride metabolic process Source: UniProtKB
  • unsaturated fatty acid biosynthetic process Source: MGI
  • white fat cell differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.19.1. 3474.
ReactomeiR-MMU-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase 1Curated (EC:1.14.19.16 Publications)
Alternative name(s):
Delta(9)-desaturase 11 Publication
Short name:
Delta-9 desaturase 11 Publication
Fatty acid desaturase 1
Stearoyl-CoA desaturase 12 Publications
Gene namesi
Name:Scd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:98239. Scd1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6868Cytoplasmic1 PublicationAdd
BLAST
Transmembranei69 – 8921Helical1 PublicationAdd
BLAST
Topological domaini90 – 934Lumenal1 Publication
Transmembranei94 – 11421Helical1 PublicationAdd
BLAST
Topological domaini115 – 21399Cytoplasmic1 PublicationAdd
BLAST
Transmembranei214 – 23320Helical1 PublicationAdd
BLAST
Topological domaini234 – 2374Lumenal1 Publication
Transmembranei238 – 25922Helical1 PublicationAdd
BLAST
Topological domaini260 – 35596Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Involvement in diseasei

Defects is Scd1 are the cause of asebia (ab) (PubMed:17738154, PubMed:10545940, PubMed:10854228, PubMed:10899171, PubMed:15278437). The trait is due to spontaneous autosomal recessive mutations that give rise to deletions or point mutations in Scd1. The ab trait has complete penetrance (PubMed:17738154). Ab mice are characterized by reduced body weight, extreme sebaceous gland hypoplasia leading to nearly complete absence of sebaceous glands, and thickened, scaly skin with hyperkeratosis and alopecia (PubMed:17738154, PubMed:10854228, PubMed:15278437). The hair follicles are abnormally long and extend at a sharp angle into the subcutis, probably due to abnormal persistence of inner root sheath. Frequently the hair shaft ruptures through the base of the hair follicle, giving rise to inflammation that results in scarring alopecia (PubMed:10854228, PubMed:15278437). Besides, ab mice display increased transepithelial water loss (PubMed:10854228). Ab mice present a narrow eye fissure and their eyes are nearly closed (PubMed:10854228, PubMed:15278437). Older mice develop blindness (PubMed:17738154). Scd1 activity is almost absent in liver, and is not compensated by expression of another family member (PubMed:10899171). Liver levels of total cholesterol esters are decreased by 87%, while plasma cholesterol levels are increased by 35% (PubMed:10899171). Likewise, skin sterol esters and diol diesters are strongly reduced (PubMed:10854228). Liver triglyceride levels are decreased by 62%, while plasma triglyceride levels are decreased by 67% (PubMed:10899171). The fatty acid composition of liver triglycerides is altered, with a decrease of about 85% in palmitoleate (C16:1) and oleate (C18:1) levels (PubMed:10899171). These defects cannot be compensated by a diet enriched in unsaturated fatty acids (PubMed:10899171, PubMed:11441127).

Disruption phenotypei

Mice are viable and fertile (PubMed:11533264). Compared to wild-type, they consume about 25% more food, but are leaner and acumulate less white adipose tissue (PubMed:12177411, PubMed:17127673). Their liver glycogen levels are lower than wild-type, except when their diet is supplemented with high levels of triolein (PubMed:17127673). They gain weight and accumulate white adipose tissue when their diet contains high levels of triolein (PubMed:17127673). They loose weight on a diet rich in tristearin, contrary to wild-type (PubMed:17127673). Mutant mice cannot maintain their body temperature when exposed to cold; they display hypoglycemia, depleted liver glycogen levels, and die of hypothermia (PubMed:15210843). Mutant mice display increased levels of mitochondrial fatty acid oxidation and decreased expression of genes that are important for de novo lipogenesis, especially when their diet is enriched in saturated fatty acids (PubMed:12177411, PubMed:17127673). Their brown adipose tissues shows increased lipolysis and fatty acid oxidation (PubMed:15210843). They display increased metabolic rates during the day and the night (PubMed:12177411). Liver, skin and white adipose tissue from mutant mice show strongly decreased levels of palmitoleate and reduced levels of oleate, with increased levels of saturated fatty acids (PubMed:11533264). Likewise, skin and eyelids are deficient in cholesterol esters, wax esters and triglycerides (PubMed:11533264). These defects cannot be compensated by a diet enriched in unsaturated fatty acids (PubMed:11533264). Mutant mice have decreased levels of liver and plasma triglycerides (PubMed:17127673). Likewise, the levels of triglycerides, 1,2-diacylglycerol and free fatty acids are decreased in the brown adipose tissue (PubMed:15210843). Besides, brown adipose tissue, liver and plasma triglycerides are depleted in unsaturated fatty acids and are enriched in saturated fatty acids (PubMed:15210843, PubMed:17127673). A diet enriched in triolein increases liver and plasma levels of triglycerides (PubMed:17127673). Mutant mice display lower fasting insulin levels, normal fasting glucose levels, increased glucose tolerance and increased insulin sensitivity (PubMed:12177411). Mutant mice display alopecia and atrophy of sebaceous glands and Meibomian glands (PubMed:11533264). Besides, they present a narrow eye fissure and their eyes are nearly closed (PubMed:11533264). This eye phenotype is probably due to a defect in the production of meibum, the oily material that prevents drying of the cornea. Scd1 activity is almost absent in liver, and is not compensated by expression of another family member (PubMed:11533264). Strongly reduced levels of lipids containing delta-9 unsaturated fatty acids in the Harderian gland, leading to strongly reduced levels of 1-alkyl-2,3-diacylglycerol in the Harderian gland (PubMed:11500518).5 Publications

Keywords - Diseasei

Disease mutation

Chemistry

ChEMBLiCHEMBL5353.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355Acyl-CoA desaturase 1PRO_0000185397Add
BLAST

Proteomic databases

EPDiP13516.
PaxDbiP13516.
PRIDEiP13516.

PTM databases

iPTMnetiP13516.
PhosphoSiteiP13516.

Expressioni

Tissue specificityi

Detected in liver (at protein level) (PubMed:10899171, PubMed:11533264). Detected in skin and liver (PubMed:10545940, PubMed:11161812, PubMed:11441127, PubMed:11533264). Detected in sebaceous gland, but not in hair follicle (PubMed:10545940). Detected in white and brown adipose tissue, eyelid, Harderian gland, and at lower levels in Meibomian gland, eyeball and adrenal gland (PubMed:11500518, PubMed:11533264). Highly expressed in liver, and detected at low levels in brain, heart, lung, stomach, skeletal muscle and kidney (PubMed:11161812, PubMed:12815040).6 Publications

Developmental stagei

Up-regulated during the early anagen phase of the hair cycle. Thereafter, levels decrease and are very low at telogen phase.2 Publications

Inductioni

Up-regulated by agonists that activate NR1H3 (PubMed:12815040). Up-regulated by a high-carbohydrate diet (PubMed:11441127). Up-regulated by a fat-free, high-carbohydrate diet (PubMed:12815040). Down-regulated by a high-carbohydrate diet enriched in unsaturated fatty acids (PubMed:12815040). Up-regulated by a diet containing high levels of stearate (PubMed:17127673).3 Publications

Gene expression databases

BgeeiP13516.
CleanExiMM_SCD1.
ExpressionAtlasiP13516. baseline and differential.
GenevisibleiP13516. MM.

Interactioni

Protein-protein interaction databases

MINTiMINT-4996454.
STRINGi10090.ENSMUSP00000036936.

Chemistry

BindingDBiP13516.

Structurei

Secondary structure

1
355
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi59 – 613Combined sources
Helixi69 – 8618Combined sources
Helixi87 – 915Combined sources
Helixi94 – 11219Combined sources
Helixi113 – 1208Combined sources
Beta strandi124 – 1263Combined sources
Helixi128 – 14114Combined sources
Helixi146 – 15813Combined sources
Turni159 – 1613Combined sources
Helixi169 – 1713Combined sources
Helixi173 – 1775Combined sources
Helixi179 – 1813Combined sources
Helixi187 – 1937Combined sources
Helixi199 – 2024Combined sources
Helixi205 – 2128Combined sources
Helixi214 – 2229Combined sources
Helixi225 – 2339Combined sources
Helixi238 – 2436Combined sources
Turni244 – 2463Combined sources
Helixi247 – 25812Combined sources
Turni259 – 2624Combined sources
Helixi263 – 2653Combined sources
Beta strandi267 – 2693Combined sources
Helixi282 – 2876Combined sources
Turni288 – 2925Combined sources
Helixi294 – 2996Combined sources
Beta strandi306 – 3116Combined sources
Helixi315 – 32511Combined sources
Beta strandi328 – 3303Combined sources
Helixi337 – 34711Combined sources
Helixi352 – 3543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YMKX-ray2.60A/D24-355[»]
ProteinModelPortaliP13516.
SMRiP13516. Positions 40-355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi116 – 1216Histidine box-1Curated
Motifi153 – 1575Histidine box-2Curated
Motifi294 – 2985Histidine box-3Curated

Domaini

The histidine box domains are involved in binding the catalytic metal ions.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiP13516.
KOiK00507.
OMAiWICDTRY.
OrthoDBiEOG7ZPNKS.
PhylomeDBiP13516.
TreeFamiTF313251.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13516-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAHMLQEIS SSYTTTTTIT APPSGNEREK VKTVPLHLEE DIRPEMKEDI
60 70 80 90 100
HDPTYQDEEG PPPKLEYVWR NIILMVLLHL GGLYGIILVP SCKLYTCLFG
110 120 130 140 150
IFYYMTSALG ITAGAHRLWS HRTYKARLPL RIFLIIANTM AFQNDVYEWA
160 170 180 190 200
RDHRAHHKFS ETHADPHNSR RGFFFSHVGW LLVRKHPAVK EKGGKLDMSD
210 220 230 240 250
LKAEKLVMFQ RRYYKPGLLL MCFILPTLVP WYCWGETFVN SLFVSTFLRY
260 270 280 290 300
TLVLNATWLV NSAAHLYGYR PYDKNIQSRE NILVSLGAVG EGFHNYHHTF
310 320 330 340 350
PFDYSASEYR WHINFTTFFI DCMAALGLAY DRKKVSKATV LARIKRTGDG

SHKSS
Length:355
Mass (Da):41,046
Last modified:June 6, 2002 - v2
Checksum:i00E2348C1898FE75
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971C → A in AAA40103 (PubMed:2903162).Curated
Sequence conflicti148 – 1481E → D in AAA40103 (PubMed:2903162).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti278 – 2781S → SP in ab. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21285
, M21280, M21281, M21282, M21283, M21284 Genomic DNA. Translation: AAA40103.1.
BC007474 mRNA. Translation: AAH07474.1.
BC055453 mRNA. Translation: AAH55453.1.
CCDSiCCDS29850.1.
PIRiA32115.
RefSeqiNP_033153.2. NM_009127.4.
UniGeneiMm.267377.

Genome annotation databases

EnsembliENSMUST00000041331; ENSMUSP00000036936; ENSMUSG00000037071.
GeneIDi20249.
KEGGimmu:20249.
UCSCiuc008hpr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21285
, M21280, M21281, M21282, M21283, M21284 Genomic DNA. Translation: AAA40103.1.
BC007474 mRNA. Translation: AAH07474.1.
BC055453 mRNA. Translation: AAH55453.1.
CCDSiCCDS29850.1.
PIRiA32115.
RefSeqiNP_033153.2. NM_009127.4.
UniGeneiMm.267377.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YMKX-ray2.60A/D24-355[»]
ProteinModelPortaliP13516.
SMRiP13516. Positions 40-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4996454.
STRINGi10090.ENSMUSP00000036936.

Chemistry

BindingDBiP13516.
ChEMBLiCHEMBL5353.

PTM databases

iPTMnetiP13516.
PhosphoSiteiP13516.

Proteomic databases

EPDiP13516.
PaxDbiP13516.
PRIDEiP13516.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041331; ENSMUSP00000036936; ENSMUSG00000037071.
GeneIDi20249.
KEGGimmu:20249.
UCSCiuc008hpr.2. mouse.

Organism-specific databases

CTDi20249.
MGIiMGI:98239. Scd1.

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiP13516.
KOiK00507.
OMAiWICDTRY.
OrthoDBiEOG7ZPNKS.
PhylomeDBiP13516.
TreeFamiTF313251.

Enzyme and pathway databases

BRENDAi1.14.19.1. 3474.
ReactomeiR-MMU-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

ChiTaRSiScd1. mouse.
PROiP13516.
SOURCEiSearch...

Gene expression databases

BgeeiP13516.
CleanExiMM_SCD1.
ExpressionAtlasiP13516. baseline and differential.
GenevisibleiP13516. MM.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  3. "Hereditary absence of sebaceous glands in the mouse."
    Gates A.H., Karasek M.
    Science 148:1471-1473(1965) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN AB.
  4. "Scd1 is expressed in sebaceous glands and is disrupted in the asebia mouse."
    Zheng Y., Eilertsen K.J., Ge L., Zhang L., Sundberg J.P., Prouty S.M., Stenn K.S., Parimoo S.
    Nat. Genet. 23:268-270(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION.
  5. "Asebia-2J (Scd1(ab2J)): a new allele and a model for scarring alopecia."
    Sundberg J.P., Boggess D., Sundberg B.A., Eilertsen K., Parimoo S., Filippi M., Stenn K.
    Am. J. Pathol. 156:2067-2075(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE.
  6. "The biosynthesis of hepatic cholesterol esters and triglycerides is impaired in mice with a disruption of the gene for stearoyl-CoA desaturase 1."
    Miyazaki M., Kim Y.C., Gray-Keller M.P., Attie A.D., Ntambi J.M.
    J. Biol. Chem. 275:30132-30138(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISEASE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. "Scd3--a novel gene of the stearoyl-CoA desaturase family with restricted expression in skin."
    Zheng Y., Prouty S.M., Harmon A., Sundberg J.P., Stenn K.S., Parimoo S.
    Genomics 71:182-191(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. "Oleoyl-CoA is the major de novo product of stearoyl-CoA desaturase 1 gene isoform and substrate for the biosynthesis of the Harderian gland 1-alkyl-2,3-diacylglycerol."
    Miyazaki M., Kim H.J., Man W.C., Ntambi J.M.
    J. Biol. Chem. 276:39455-39461(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  9. "A lipogenic diet in mice with a disruption of the stearoyl-CoA desaturase 1 gene reveals a stringent requirement of endogenous monounsaturated fatty acids for triglyceride synthesis."
    Miyazaki M., Kim Y.C., Ntambi J.M.
    J. Lipid Res. 42:1018-1024(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, FUNCTION, INDUCTION BY HIGH-CARBOHYDRATE DIET, TISSUE SPECIFICITY.
  10. "Targeted disruption of stearoyl-CoA desaturase1 gene in mice causes atrophy of sebaceous and meibomian glands and depletion of wax esters in the eyelid."
    Miyazaki M., Man W.C., Ntambi J.M.
    J. Nutr. 131:2260-2268(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  11. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  12. "Identification and characterization of murine SCD4, a novel heart-specific stearoyl-CoA desaturase isoform regulated by leptin and dietary factors."
    Miyazaki M., Jacobson M.J., Man W.C., Cohen P., Asilmaz E., Friedman J.M., Ntambi J.M.
    J. Biol. Chem. 278:33904-33911(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HIGH CARBOHYDRATE; UNSATURATED FATTY ACIDS AND NR1H3 AGONISTS, TISSUE SPECIFICITY.
  13. "Lack of stearoyl-CoA desaturase 1 upregulates basal thermogenesis but causes hypothermia in a cold environment."
    Lee S.H., Dobrzyn A., Dobrzyn P., Rahman S.M., Miyazaki M., Ntambi J.M.
    J. Lipid Res. 45:1674-1682(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  14. "Scd1ab-Xyk: a new asebia allele characterized by a CCC trinucleotide insertion in exon 5 of the stearoyl-CoA desaturase 1 gene in mouse."
    Lu Y., Bu L., Zhou S., Jin M., Sundberg J.P., Jiang H., Qian M., Shi Y., Zhao G., Kong X., Hu L.
    Mol. Genet. Genomics 272:129-137(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, VARIANT AB PRO-278 INS.
  15. "Membrane topology of mouse stearoyl-CoA desaturase 1."
    Man W.C., Miyazaki M., Chu K., Ntambi J.M.
    J. Biol. Chem. 281:1251-1260(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
  16. "Identification of mouse palmitoyl-coenzyme A Delta9-desaturase."
    Miyazaki M., Bruggink S.M., Ntambi J.M.
    J. Lipid Res. 47:700-704(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  17. "Stearoyl-CoA desaturase-1 mediates the pro-lipogenic effects of dietary saturated fat."
    Sampath H., Miyazaki M., Dobrzyn A., Ntambi J.M.
    J. Biol. Chem. 282:2483-2493(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, INDUCTION BY DIETARY STEARATE.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Liver and Lung.
  19. "Role of stearoyl-CoA desaturase-1 in skin integrity and whole body energy balance."
    Sampath H., Ntambi J.M.
    J. Biol. Chem. 289:2482-2488(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  20. "Opportunities and challenges in developing stearoyl-coenzyme A desaturase-1 inhibitors as novel therapeutics for human disease."
    Zhang Z., Dales N.A., Winther M.D.
    J. Med. Chem. 57:5039-5056(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  21. "X-ray structure of a mammalian stearoyl-CoA desaturase."
    Bai Y., McCoy J.G., Levin E.J., Sobrado P., Rajashankar K.R., Fox B.G., Zhou M.
    Nature 524:252-256(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 24-355 IN COMPLEX WITH STEAROYL-COENZYME A AND ZINC IONS, FUNCTION, TOPOLOGY, CATALYTIC ACTIVITY, COFACTOR.

Entry informationi

Entry nameiACOD1_MOUSE
AccessioniPrimary (citable) accession number: P13516
Secondary accession number(s): Q922I6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 6, 2002
Last modified: June 8, 2016
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.