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Acyl-CoA desaturase 1 (EC 1.14.19.1) (Delta(9)-desaturase 1) (Delta-9 desaturase 1) (Fatty acid desaturase 1) (Stearoyl-CoA desaturase 1)

 ACOD1_MOUSE             Reviewed;         355 AA.
P13516; Q922I6;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 2.
07-JUN-2017, entry version 164.
RecName: Full=Acyl-CoA desaturase 1 {ECO:0000305};
EC=1.14.19.1 {ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11500518, ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:16275639, ECO:0000269|PubMed:16443825, ECO:0000269|PubMed:26098370};
AltName: Full=Delta(9)-desaturase 1 {ECO:0000303|PubMed:16443825};
Short=Delta-9 desaturase 1 {ECO:0000303|PubMed:16443825};
AltName: Full=Fatty acid desaturase 1;
AltName: Full=Stearoyl-CoA desaturase 1 {ECO:0000303|PubMed:10899171, ECO:0000303|PubMed:16275639};
Name=Scd1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Adipocyte;
PubMed=2903162;
Ntambi J.M., Buhrow S.A., Kaestner K.H., Christy R.J., Sibley E.,
Kelly T.J. Jr., Lane M.D.;
"Differentiation-induced gene expression in 3T3-L1 preadipocytes.
Characterization of a differentially expressed gene encoding stearoyl-
CoA desaturase.";
J. Biol. Chem. 263:17291-17300(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
INVOLVEMENT IN AB.
PubMed=17738154; DOI=10.1126/science.148.3676.1471;
Gates A.H., Karasek M.;
"Hereditary absence of sebaceous glands in the mouse.";
Science 148:1471-1473(1965).
[4]
DISEASE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND FUNCTION.
PubMed=10545940; DOI=10.1038/15446;
Zheng Y., Eilertsen K.J., Ge L., Zhang L., Sundberg J.P., Prouty S.M.,
Stenn K.S., Parimoo S.;
"Scd1 is expressed in sebaceous glands and is disrupted in the asebia
mouse.";
Nat. Genet. 23:268-270(1999).
[5]
DISEASE.
PubMed=10854228; DOI=10.1016/S0002-9440(10)65078-X;
Sundberg J.P., Boggess D., Sundberg B.A., Eilertsen K., Parimoo S.,
Filippi M., Stenn K.;
"Asebia-2J (Scd1(ab2J)): a new allele and a model for scarring
alopecia.";
Am. J. Pathol. 156:2067-2075(2000).
[6]
FUNCTION, CATALYTIC ACTIVITY, DISEASE, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=10899171; DOI=10.1074/jbc.M005488200;
Miyazaki M., Kim Y.C., Gray-Keller M.P., Attie A.D., Ntambi J.M.;
"The biosynthesis of hepatic cholesterol esters and triglycerides is
impaired in mice with a disruption of the gene for stearoyl-CoA
desaturase 1.";
J. Biol. Chem. 275:30132-30138(2000).
[7]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=11161812; DOI=10.1006/geno.2000.6429;
Zheng Y., Prouty S.M., Harmon A., Sundberg J.P., Stenn K.S.,
Parimoo S.;
"Scd3--a novel gene of the stearoyl-CoA desaturase family with
restricted expression in skin.";
Genomics 71:182-191(2001).
[8]
FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=11500518; DOI=10.1074/jbc.M106442200;
Miyazaki M., Kim H.J., Man W.C., Ntambi J.M.;
"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.";
J. Biol. Chem. 276:39455-39461(2001).
[9]
DISEASE, FUNCTION, INDUCTION BY HIGH-CARBOHYDRATE DIET, AND TISSUE
SPECIFICITY.
PubMed=11441127;
Miyazaki M., Kim Y.C., Ntambi J.M.;
"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.";
J. Lipid Res. 42:1018-1024(2001).
[10]
FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=11533264;
Miyazaki M., Man W.C., Ntambi J.M.;
"Targeted disruption of stearoyl-CoA desaturase1 gene in mice causes
atrophy of sebaceous and meibomian glands and depletion of wax esters
in the eyelid.";
J. Nutr. 131:2260-2268(2001).
[11]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=12177411; DOI=10.1073/pnas.132384699;
Ntambi J.M., Miyazaki M., Stoehr J.P., Lan H., Kendziorski C.M.,
Yandell B.S., Song Y., Cohen P., Friedman J.M., Attie A.D.;
"Loss of stearoyl-CoA desaturase-1 function protects mice against
adiposity.";
Proc. Natl. Acad. Sci. U.S.A. 99:11482-11486(2002).
[12]
INDUCTION BY HIGH CARBOHYDRATE; UNSATURATED FATTY ACIDS AND NR1H3
AGONISTS, AND TISSUE SPECIFICITY.
PubMed=12815040; DOI=10.1074/jbc.M304724200;
Miyazaki M., Jacobson M.J., Man W.C., Cohen P., Asilmaz E.,
Friedman J.M., Ntambi J.M.;
"Identification and characterization of murine SCD4, a novel heart-
specific stearoyl-CoA desaturase isoform regulated by leptin and
dietary factors.";
J. Biol. Chem. 278:33904-33911(2003).
[13]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=15210843; DOI=10.1194/jlr.M400039-JLR200;
Lee S.H., Dobrzyn A., Dobrzyn P., Rahman S.M., Miyazaki M.,
Ntambi J.M.;
"Lack of stearoyl-CoA desaturase 1 upregulates basal thermogenesis but
causes hypothermia in a cold environment.";
J. Lipid Res. 45:1674-1682(2004).
[14]
DISEASE, AND VARIANT AB PRO-278 INS.
PubMed=15278437; DOI=10.1007/s00438-004-1043-3;
Lu Y., Bu L., Zhou S., Jin M., Sundberg J.P., Jiang H., Qian M.,
Shi Y., Zhao G., Kong X., Hu L.;
"Scd1ab-Xyk: a new asebia allele characterized by a CCC trinucleotide
insertion in exon 5 of the stearoyl-CoA desaturase 1 gene in mouse.";
Mol. Genet. Genomics 272:129-137(2004).
[15]
SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
PubMed=16275639; DOI=10.1074/jbc.M508733200;
Man W.C., Miyazaki M., Chu K., Ntambi J.M.;
"Membrane topology of mouse stearoyl-CoA desaturase 1.";
J. Biol. Chem. 281:1251-1260(2006).
[16]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=16443825; DOI=10.1194/jlr.C500025-JLR200;
Miyazaki M., Bruggink S.M., Ntambi J.M.;
"Identification of mouse palmitoyl-coenzyme A Delta9-desaturase.";
J. Lipid Res. 47:700-704(2006).
[17]
DISRUPTION PHENOTYPE, FUNCTION, AND INDUCTION BY DIETARY STEARATE.
PubMed=17127673; DOI=10.1074/jbc.M610158200;
Sampath H., Miyazaki M., Dobrzyn A., Ntambi J.M.;
"Stearoyl-CoA desaturase-1 mediates the pro-lipogenic effects of
dietary saturated fat.";
J. Biol. Chem. 282:2483-2493(2007).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Liver, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
REVIEW.
PubMed=24356954; DOI=10.1074/jbc.R113.516716;
Sampath H., Ntambi J.M.;
"Role of stearoyl-CoA desaturase-1 in skin integrity and whole body
energy balance.";
J. Biol. Chem. 289:2482-2488(2014).
[20]
REVIEW.
PubMed=24295027; DOI=10.1021/jm401516c;
Zhang Z., Dales N.A., Winther M.D.;
"Opportunities and challenges in developing stearoyl-coenzyme A
desaturase-1 inhibitors as novel therapeutics for human disease.";
J. Med. Chem. 57:5039-5056(2014).
[21]
X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 24-355 IN COMPLEX WITH
STEAROYL-COENZYME A AND ZINC IONS, FUNCTION, TOPOLOGY, CATALYTIC
ACTIVITY, AND COFACTOR.
PubMed=26098370; DOI=10.1038/nature14549;
Bai Y., McCoy J.G., Levin E.J., Sobrado P., Rajashankar K.R.,
Fox B.G., Zhou M.;
"X-ray structure of a mammalian stearoyl-CoA desaturase.";
Nature 524:252-256(2015).
-!- FUNCTION: Stearyl-CoA desaturase that utilizes O(2) 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). {ECO:0000269|PubMed:10899171,
ECO:0000269|PubMed:11441127, ECO:0000269|PubMed:11500518,
ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:12177411,
ECO:0000269|PubMed:15210843, ECO:0000269|PubMed:16275639,
ECO:0000269|PubMed:16443825, ECO:0000269|PubMed:17127673,
ECO:0000269|PubMed:26098370, ECO:0000305|PubMed:24295027,
ECO:0000305|PubMed:24356954}.
-!- CATALYTIC ACTIVITY: Stearoyl-CoA + 2 ferrocytochrome b5 + O(2) + 2
H(+) = oleoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O.
{ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11500518,
ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:16275639,
ECO:0000269|PubMed:16443825, ECO:0000269|PubMed:26098370}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000305|PubMed:26098370};
Note=Expected to bind 2 Fe(2+) ions per subunit, instead of the
Zn(2+) ions seen in the 3D-structure.
{ECO:0000305|PubMed:26098370};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:16275639, ECO:0000305|PubMed:16443825}; Multi-
pass membrane protein {ECO:0000269|PubMed:16275639}. Microsome
membrane {ECO:0000269|PubMed:10899171,
ECO:0000269|PubMed:11500518, ECO:0000269|PubMed:11533264,
ECO:0000269|PubMed:16443825}.
-!- TISSUE SPECIFICITY: 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). {ECO:0000269|PubMed:10545940,
ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11441127,
ECO:0000269|PubMed:11500518, ECO:0000269|PubMed:11533264,
ECO:0000269|PubMed:12815040}.
-!- DEVELOPMENTAL STAGE: Up-regulated during the early anagen phase of
the hair cycle. Thereafter, levels decrease and are very low at
telogen phase. {ECO:0000269|PubMed:10545940,
ECO:0000269|PubMed:11161812}.
-!- INDUCTION: 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). {ECO:0000269|PubMed:11441127,
ECO:0000269|PubMed:12815040, ECO:0000269|PubMed:17127673}.
-!- DOMAIN: The histidine box domains are involved in binding the
catalytic metal ions. {ECO:0000269|PubMed:26098370}.
-!- DISEASE: Note=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). {ECO:0000269|PubMed:10545940,
ECO:0000269|PubMed:10854228, ECO:0000269|PubMed:10899171,
ECO:0000269|PubMed:11441127, ECO:0000269|PubMed:11533264,
ECO:0000269|PubMed:15278437, ECO:0000269|PubMed:17738154}.
-!- DISRUPTION PHENOTYPE: 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). {ECO:0000269|PubMed:11500518,
ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:12177411,
ECO:0000269|PubMed:15210843, ECO:0000269|PubMed:17127673}.
-!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
{ECO:0000305}.
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EMBL; M21285; AAA40103.1; -; Genomic_DNA.
EMBL; M21280; AAA40103.1; JOINED; Genomic_DNA.
EMBL; M21281; AAA40103.1; JOINED; Genomic_DNA.
EMBL; M21282; AAA40103.1; JOINED; Genomic_DNA.
EMBL; M21283; AAA40103.1; JOINED; Genomic_DNA.
EMBL; M21284; AAA40103.1; JOINED; Genomic_DNA.
EMBL; BC007474; AAH07474.1; -; mRNA.
EMBL; BC055453; AAH55453.1; -; mRNA.
CCDS; CCDS29850.1; -.
PIR; A32115; A32115.
RefSeq; NP_033153.2; NM_009127.4.
UniGene; Mm.267377; -.
PDB; 4YMK; X-ray; 2.60 A; A/D=24-355.
PDBsum; 4YMK; -.
ProteinModelPortal; P13516; -.
SMR; P13516; -.
MINT; MINT-4996454; -.
STRING; 10090.ENSMUSP00000036936; -.
BindingDB; P13516; -.
ChEMBL; CHEMBL5353; -.
iPTMnet; P13516; -.
PhosphoSitePlus; P13516; -.
PaxDb; P13516; -.
PeptideAtlas; P13516; -.
PRIDE; P13516; -.
Ensembl; ENSMUST00000041331; ENSMUSP00000036936; ENSMUSG00000037071.
GeneID; 20249; -.
KEGG; mmu:20249; -.
UCSC; uc008hpr.2; mouse.
CTD; 20249; -.
MGI; MGI:98239; Scd1.
eggNOG; KOG1600; Eukaryota.
eggNOG; COG1398; LUCA.
GeneTree; ENSGT00530000063158; -.
HOGENOM; HOG000270352; -.
HOVERGEN; HBG003367; -.
InParanoid; P13516; -.
KO; K00507; -.
OMA; HATWGWG; -.
OrthoDB; EOG091G0B5S; -.
PhylomeDB; P13516; -.
TreeFam; TF313251; -.
BRENDA; 1.14.19.1; 3474.
Reactome; R-MMU-75105; Fatty acyl-CoA biosynthesis.
ChiTaRS; Scd1; mouse.
PRO; PR:P13516; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000037071; -.
CleanEx; MM_SCD1; -.
ExpressionAtlas; P13516; baseline and differential.
Genevisible; P13516; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:WormBase.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
GO; GO:0032896; F:palmitoyl-CoA 9-desaturase activity; IDA:UniProtKB.
GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:UniProtKB.
GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
GO; GO:0034435; P:cholesterol esterification; IMP:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
GO; GO:0006633; P:fatty acid biosynthetic process; IMP:MGI.
GO; GO:1903966; P:monounsaturated fatty acid biosynthetic process; IDA:MGI.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IMP:MGI.
GO; GO:0010873; P:positive regulation of cholesterol esterification; TAS:BHF-UCL.
GO; GO:0033561; P:regulation of water loss via skin; IMP:UniProtKB.
GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
GO; GO:0048733; P:sebaceous gland development; IMP:UniProtKB.
GO; GO:0034434; P:sterol esterification; IMP:UniProtKB.
GO; GO:1903699; P:tarsal gland development; IMP:UniProtKB.
GO; GO:0006641; P:triglyceride metabolic process; IMP:UniProtKB.
GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; ISO:MGI.
GO; GO:0050872; P:white fat cell differentiation; IDA:MGI.
CDD; cd03505; Delta9-FADS-like; 1.
InterPro; IPR015876; Acyl-CoA_DS.
InterPro; IPR005804; FA_desaturase_dom.
InterPro; IPR001522; FADS-1_CS.
PANTHER; PTHR11351; PTHR11351; 1.
Pfam; PF00487; FA_desaturase; 1.
PRINTS; PR00075; FACDDSATRASE.
PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disease mutation;
Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
Microsome; Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 355 Acyl-CoA desaturase 1.
/FTId=PRO_0000185397.
TOPO_DOM 1 68 Cytoplasmic.
{ECO:0000305|PubMed:16275639}.
TRANSMEM 69 89 Helical. {ECO:0000269|PubMed:26098370}.
TOPO_DOM 90 93 Lumenal. {ECO:0000305|PubMed:26098370}.
TRANSMEM 94 114 Helical. {ECO:0000269|PubMed:26098370}.
TOPO_DOM 115 213 Cytoplasmic.
{ECO:0000305|PubMed:26098370}.
TRANSMEM 214 233 Helical. {ECO:0000269|PubMed:26098370}.
TOPO_DOM 234 237 Lumenal. {ECO:0000305|PubMed:26098370}.
TRANSMEM 238 259 Helical. {ECO:0000269|PubMed:26098370}.
TOPO_DOM 260 355 Cytoplasmic.
{ECO:0000305|PubMed:16275639}.
MOTIF 116 121 Histidine box-1. {ECO:0000305}.
MOTIF 153 157 Histidine box-2. {ECO:0000305}.
MOTIF 294 298 Histidine box-3. {ECO:0000305}.
METAL 116 116 Iron 1. {ECO:0000305|PubMed:26098370}.
METAL 121 121 Iron 1. {ECO:0000305|PubMed:26098370}.
METAL 153 153 Iron 1. {ECO:0000305|PubMed:26098370}.
METAL 156 156 Iron 2. {ECO:0000305|PubMed:26098370}.
METAL 157 157 Iron 1. {ECO:0000305|PubMed:26098370}.
METAL 265 265 Iron 2. {ECO:0000305|PubMed:26098370}.
METAL 294 294 Iron 2. {ECO:0000305|PubMed:26098370}.
METAL 297 297 Iron 1. {ECO:0000305|PubMed:26098370}.
METAL 298 298 Iron 2. {ECO:0000305|PubMed:26098370}.
BINDING 71 71 Substrate. {ECO:0000269|PubMed:26098370}.
BINDING 144 144 Substrate. {ECO:0000269|PubMed:26098370}.
BINDING 151 151 Substrate. {ECO:0000269|PubMed:26098370}.
BINDING 152 152 Substrate. {ECO:0000269|PubMed:26098370}.
BINDING 184 184 Substrate. {ECO:0000269|PubMed:26098370}.
BINDING 185 185 Substrate. {ECO:0000269|PubMed:26098370}.
BINDING 258 258 Substrate. {ECO:0000269|PubMed:26098370}.
VARIANT 278 278 S -> SP (in ab).
{ECO:0000269|PubMed:15278437}.
CONFLICT 97 97 C -> A (in Ref. 1; AAA40103).
{ECO:0000305}.
CONFLICT 148 148 E -> D (in Ref. 1; AAA40103).
{ECO:0000305}.
STRAND 59 61 {ECO:0000244|PDB:4YMK}.
HELIX 69 86 {ECO:0000244|PDB:4YMK}.
HELIX 87 91 {ECO:0000244|PDB:4YMK}.
HELIX 94 112 {ECO:0000244|PDB:4YMK}.
HELIX 113 120 {ECO:0000244|PDB:4YMK}.
STRAND 124 126 {ECO:0000244|PDB:4YMK}.
HELIX 128 141 {ECO:0000244|PDB:4YMK}.
HELIX 146 158 {ECO:0000244|PDB:4YMK}.
TURN 159 161 {ECO:0000244|PDB:4YMK}.
HELIX 169 171 {ECO:0000244|PDB:4YMK}.
HELIX 173 177 {ECO:0000244|PDB:4YMK}.
HELIX 179 181 {ECO:0000244|PDB:4YMK}.
HELIX 187 193 {ECO:0000244|PDB:4YMK}.
HELIX 199 202 {ECO:0000244|PDB:4YMK}.
HELIX 205 212 {ECO:0000244|PDB:4YMK}.
HELIX 214 222 {ECO:0000244|PDB:4YMK}.
HELIX 225 233 {ECO:0000244|PDB:4YMK}.
HELIX 238 243 {ECO:0000244|PDB:4YMK}.
TURN 244 246 {ECO:0000244|PDB:4YMK}.
HELIX 247 258 {ECO:0000244|PDB:4YMK}.
TURN 259 262 {ECO:0000244|PDB:4YMK}.
HELIX 263 265 {ECO:0000244|PDB:4YMK}.
STRAND 267 269 {ECO:0000244|PDB:4YMK}.
HELIX 282 287 {ECO:0000244|PDB:4YMK}.
TURN 288 292 {ECO:0000244|PDB:4YMK}.
HELIX 294 299 {ECO:0000244|PDB:4YMK}.
STRAND 306 311 {ECO:0000244|PDB:4YMK}.
HELIX 315 325 {ECO:0000244|PDB:4YMK}.
STRAND 328 330 {ECO:0000244|PDB:4YMK}.
HELIX 337 347 {ECO:0000244|PDB:4YMK}.
HELIX 352 354 {ECO:0000244|PDB:4YMK}.
SEQUENCE 355 AA; 41046 MW; 00E2348C1898FE75 CRC64;
MPAHMLQEIS SSYTTTTTIT APPSGNEREK VKTVPLHLEE DIRPEMKEDI HDPTYQDEEG
PPPKLEYVWR NIILMVLLHL GGLYGIILVP SCKLYTCLFG IFYYMTSALG ITAGAHRLWS
HRTYKARLPL RIFLIIANTM AFQNDVYEWA RDHRAHHKFS ETHADPHNSR RGFFFSHVGW
LLVRKHPAVK EKGGKLDMSD LKAEKLVMFQ RRYYKPGLLL MCFILPTLVP WYCWGETFVN
SLFVSTFLRY TLVLNATWLV NSAAHLYGYR PYDKNIQSRE NILVSLGAVG EGFHNYHHTF
PFDYSASEYR WHINFTTFFI DCMAALGLAY DRKKVSKATV LARIKRTGDG SHKSS


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