ACOD1_MOUSE
ID ACOD1_MOUSE Reviewed; 355 AA.
AC P13516; Q922I6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Acyl-CoA desaturase 1 {ECO:0000305};
DE 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};
DE AltName: Full=Delta(9)-desaturase 1 {ECO:0000303|PubMed:16443825};
DE Short=Delta-9 desaturase 1 {ECO:0000303|PubMed:16443825};
DE AltName: Full=Fatty acid desaturase 1;
DE AltName: Full=Stearoyl-CoA desaturase 1 {ECO:0000303|PubMed:10899171, ECO:0000303|PubMed:16275639};
GN Name=Scd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Adipocyte;
RX PubMed=2903162; DOI=10.1016/s0021-9258(19)77834-x;
RA Ntambi J.M., Buhrow S.A., Kaestner K.H., Christy R.J., Sibley E.,
RA Kelly T.J. Jr., Lane M.D.;
RT "Differentiation-induced gene expression in 3T3-L1 preadipocytes.
RT Characterization of a differentially expressed gene encoding stearoyl-CoA
RT desaturase.";
RL J. Biol. Chem. 263:17291-17300(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INVOLVEMENT IN AB.
RX PubMed=17738154; DOI=10.1126/science.148.3676.1471;
RA Gates A.H., Karasek M.;
RT "Hereditary absence of sebaceous glands in the mouse.";
RL Science 148:1471-1473(1965).
RN [4]
RP DISEASE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=10545940; DOI=10.1038/15446;
RA Zheng Y., Eilertsen K.J., Ge L., Zhang L., Sundberg J.P., Prouty S.M.,
RA Stenn K.S., Parimoo S.;
RT "Scd1 is expressed in sebaceous glands and is disrupted in the asebia
RT mouse.";
RL Nat. Genet. 23:268-270(1999).
RN [5]
RP DISEASE.
RX PubMed=10854228; DOI=10.1016/s0002-9440(10)65078-x;
RA Sundberg J.P., Boggess D., Sundberg B.A., Eilertsen K., Parimoo S.,
RA Filippi M., Stenn K.;
RT "Asebia-2J (Scd1(ab2J)): a new allele and a model for scarring alopecia.";
RL Am. J. Pathol. 156:2067-2075(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DISEASE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10899171; DOI=10.1074/jbc.m005488200;
RA Miyazaki M., Kim Y.C., Gray-Keller M.P., Attie A.D., Ntambi J.M.;
RT "The biosynthesis of hepatic cholesterol esters and triglycerides is
RT impaired in mice with a disruption of the gene for stearoyl-CoA desaturase
RT 1.";
RL J. Biol. Chem. 275:30132-30138(2000).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11161812; DOI=10.1006/geno.2000.6429;
RA Zheng Y., Prouty S.M., Harmon A., Sundberg J.P., Stenn K.S., Parimoo S.;
RT "Scd3--a novel gene of the stearoyl-CoA desaturase family with restricted
RT expression in skin.";
RL Genomics 71:182-191(2001).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11500518; DOI=10.1074/jbc.m106442200;
RA Miyazaki M., Kim H.J., Man W.C., Ntambi J.M.;
RT "Oleoyl-CoA is the major de novo product of stearoyl-CoA desaturase 1 gene
RT isoform and substrate for the biosynthesis of the Harderian gland 1-alkyl-
RT 2,3-diacylglycerol.";
RL J. Biol. Chem. 276:39455-39461(2001).
RN [9]
RP DISEASE, FUNCTION, INDUCTION BY HIGH-CARBOHYDRATE DIET, AND TISSUE
RP SPECIFICITY.
RX PubMed=11441127;
RA Miyazaki M., Kim Y.C., Ntambi J.M.;
RT "A lipogenic diet in mice with a disruption of the stearoyl-CoA desaturase
RT 1 gene reveals a stringent requirement of endogenous monounsaturated fatty
RT acids for triglyceride synthesis.";
RL J. Lipid Res. 42:1018-1024(2001).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11533264; DOI=10.1093/jn/131.9.2260;
RA Miyazaki M., Man W.C., Ntambi J.M.;
RT "Targeted disruption of stearoyl-CoA desaturase1 gene in mice causes
RT atrophy of sebaceous and meibomian glands and depletion of wax esters in
RT the eyelid.";
RL J. Nutr. 131:2260-2268(2001).
RN [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12177411; DOI=10.1073/pnas.132384699;
RA Ntambi J.M., Miyazaki M., Stoehr J.P., Lan H., Kendziorski C.M.,
RA Yandell B.S., Song Y., Cohen P., Friedman J.M., Attie A.D.;
RT "Loss of stearoyl-CoA desaturase-1 function protects mice against
RT adiposity.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11482-11486(2002).
RN [12]
RP INDUCTION BY HIGH CARBOHYDRATE; UNSATURATED FATTY ACIDS AND NR1H3 AGONISTS,
RP AND TISSUE SPECIFICITY.
RX PubMed=12815040; DOI=10.1074/jbc.m304724200;
RA Miyazaki M., Jacobson M.J., Man W.C., Cohen P., Asilmaz E., Friedman J.M.,
RA Ntambi J.M.;
RT "Identification and characterization of murine SCD4, a novel heart-specific
RT stearoyl-CoA desaturase isoform regulated by leptin and dietary factors.";
RL J. Biol. Chem. 278:33904-33911(2003).
RN [13]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15210843; DOI=10.1194/jlr.m400039-jlr200;
RA Lee S.H., Dobrzyn A., Dobrzyn P., Rahman S.M., Miyazaki M., Ntambi J.M.;
RT "Lack of stearoyl-CoA desaturase 1 upregulates basal thermogenesis but
RT causes hypothermia in a cold environment.";
RL J. Lipid Res. 45:1674-1682(2004).
RN [14]
RP DISEASE, AND VARIANT AB PRO-278 INS.
RX PubMed=15278437; DOI=10.1007/s00438-004-1043-3;
RA Lu Y., Bu L., Zhou S., Jin M., Sundberg J.P., Jiang H., Qian M., Shi Y.,
RA Zhao G., Kong X., Hu L.;
RT "Scd1ab-Xyk: a new asebia allele characterized by a CCC trinucleotide
RT insertion in exon 5 of the stearoyl-CoA desaturase 1 gene in mouse.";
RL Mol. Genet. Genomics 272:129-137(2004).
RN [15]
RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX PubMed=16275639; DOI=10.1074/jbc.m508733200;
RA Man W.C., Miyazaki M., Chu K., Ntambi J.M.;
RT "Membrane topology of mouse stearoyl-CoA desaturase 1.";
RL J. Biol. Chem. 281:1251-1260(2006).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=16443825; DOI=10.1194/jlr.c500025-jlr200;
RA Miyazaki M., Bruggink S.M., Ntambi J.M.;
RT "Identification of mouse palmitoyl-coenzyme A Delta9-desaturase.";
RL J. Lipid Res. 47:700-704(2006).
RN [17]
RP DISRUPTION PHENOTYPE, FUNCTION, AND INDUCTION BY DIETARY STEARATE.
RX PubMed=17127673; DOI=10.1074/jbc.m610158200;
RA Sampath H., Miyazaki M., Dobrzyn A., Ntambi J.M.;
RT "Stearoyl-CoA desaturase-1 mediates the pro-lipogenic effects of dietary
RT saturated fat.";
RL J. Biol. Chem. 282:2483-2493(2007).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [19]
RP REVIEW.
RX PubMed=24356954; DOI=10.1074/jbc.r113.516716;
RA Sampath H., Ntambi J.M.;
RT "Role of stearoyl-CoA desaturase-1 in skin integrity and whole body energy
RT balance.";
RL J. Biol. Chem. 289:2482-2488(2014).
RN [20]
RP REVIEW.
RX PubMed=24295027; DOI=10.1021/jm401516c;
RA Zhang Z., Dales N.A., Winther M.D.;
RT "Opportunities and challenges in developing stearoyl-coenzyme A desaturase-
RT 1 inhibitors as novel therapeutics for human disease.";
RL J. Med. Chem. 57:5039-5056(2014).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 24-355 IN COMPLEX WITH
RP STEAROYL-COENZYME A AND ZINC IONS, FUNCTION, TOPOLOGY, CATALYTIC ACTIVITY,
RP AND COFACTOR.
RX PubMed=26098370; DOI=10.1038/nature14549;
RA Bai Y., McCoy J.G., Levin E.J., Sobrado P., Rajashankar K.R., Fox B.G.,
RA Zhou M.;
RT "X-ray structure of a mammalian stearoyl-CoA desaturase.";
RL Nature 524:252-256(2015).
CC -!- FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from
CC reduced cytochrome b5 to introduce the first double bond into saturated
CC fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond
CC at the Delta-9 position into fatty acyl-CoA substrates including
CC palmitoyl-CoA and stearoyl-CoA (PubMed:11500518, PubMed:11533264,
CC PubMed:16275639, PubMed:16443825, PubMed:26098370). Gives rise to a
CC mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:11500518,
CC PubMed:11533264, PubMed:16443825, PubMed:26098370). Plays an important
CC role in lipid biosynthesis (PubMed:17127673, PubMed:10899171,
CC PubMed:11500518, PubMed:11441127, PubMed:11533264, PubMed:12177411,
CC PubMed:26098370). Plays an important role in regulating the expression
CC of genes that are involved in lipogenesis and in regulating
CC mitochondrial fatty acid oxidation (PubMed:12177411, PubMed:17127673,
CC PubMed:24356954, PubMed:24295027). Plays an important role in body
CC energy homeostasis (PubMed:17127673, PubMed:15210843, PubMed:24295027,
CC PubMed:24356954). Contributes to the biosynthesis of membrane
CC phospholipids, cholesterol esters and triglycerides (PubMed:10899171,
CC PubMed:11500518, PubMed:11441127, PubMed:11533264, PubMed:12177411,
CC PubMed:15210843, PubMed:26098370). Required for normal development of
CC sebaceous glands (PubMed:17738154, PubMed:11533264). Required for the
CC biosynthesis of normal levels of Delta-9 unsaturated fatty acids and 1-
CC alkyl-2,3-diacylglycerol in the Harderian gland (PubMed:11500518).
CC Required for normal production of meibum, an oily material that
CC prevents drying of the cornea (PubMed:11533264).
CC {ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11441127,
CC ECO:0000269|PubMed:11500518, ECO:0000269|PubMed:11533264,
CC ECO:0000269|PubMed:12177411, ECO:0000269|PubMed:15210843,
CC ECO:0000269|PubMed:16275639, ECO:0000269|PubMed:16443825,
CC ECO:0000269|PubMed:17127673, ECO:0000269|PubMed:26098370,
CC ECO:0000305|PubMed:24295027, ECO:0000305|PubMed:24356954}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA =
CC (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57394; EC=1.14.19.1;
CC Evidence={ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11500518,
CC ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:16275639,
CC ECO:0000269|PubMed:16443825, ECO:0000269|PubMed:26098370};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000305|PubMed:26098370};
CC Note=Expected to bind 2 Fe(2+) ions per subunit, instead of the Zn(2+)
CC ions seen in the 3D-structure. {ECO:0000305|PubMed:26098370};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16275639, ECO:0000305|PubMed:16443825}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16275639}. Microsome membrane
CC {ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11500518,
CC ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:16443825}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level)
CC (PubMed:10899171, PubMed:11533264). Detected in skin and liver
CC (PubMed:10545940, PubMed:11161812, PubMed:11441127, PubMed:11533264).
CC Detected in sebaceous gland, but not in hair follicle
CC (PubMed:10545940). Detected in white and brown adipose tissue, eyelid,
CC Harderian gland, and at lower levels in Meibomian gland, eyeball and
CC adrenal gland (PubMed:11500518, PubMed:11533264). Highly expressed in
CC liver, and detected at low levels in brain, heart, lung, stomach,
CC skeletal muscle and kidney (PubMed:11161812, PubMed:12815040).
CC {ECO:0000269|PubMed:10545940, ECO:0000269|PubMed:10899171,
CC ECO:0000269|PubMed:11441127, ECO:0000269|PubMed:11500518,
CC ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:12815040}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during the early anagen phase of the
CC hair cycle. Thereafter, levels decrease and are very low at telogen
CC phase. {ECO:0000269|PubMed:10545940, ECO:0000269|PubMed:11161812}.
CC -!- INDUCTION: Up-regulated by agonists that activate NR1H3
CC (PubMed:12815040). Up-regulated by a high-carbohydrate diet
CC (PubMed:11441127). Up-regulated by a fat-free, high-carbohydrate diet
CC (PubMed:12815040). Down-regulated by a high-carbohydrate diet enriched
CC in unsaturated fatty acids (PubMed:12815040). Up-regulated by a diet
CC containing high levels of stearate (PubMed:17127673).
CC {ECO:0000269|PubMed:11441127, ECO:0000269|PubMed:12815040,
CC ECO:0000269|PubMed:17127673}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000269|PubMed:26098370}.
CC -!- DISEASE: Note=Defects is Scd1 are the cause of asebia (ab)
CC (PubMed:17738154, PubMed:10545940, PubMed:10854228, PubMed:10899171,
CC PubMed:15278437). The trait is due to spontaneous autosomal recessive
CC mutations that give rise to deletions or point mutations in Scd1. The
CC ab trait has complete penetrance (PubMed:17738154). Ab mice are
CC characterized by reduced body weight, extreme sebaceous gland
CC hypoplasia leading to nearly complete absence of sebaceous glands, and
CC thickened, scaly skin with hyperkeratosis and alopecia
CC (PubMed:17738154, PubMed:10854228, PubMed:15278437). The hair follicles
CC are abnormally long and extend at a sharp angle into the subcutis,
CC probably due to abnormal persistence of inner root sheath. Frequently
CC the hair shaft ruptures through the base of the hair follicle, giving
CC rise to inflammation that results in scarring alopecia
CC (PubMed:10854228, PubMed:15278437). Besides, ab mice display increased
CC transepithelial water loss (PubMed:10854228). Ab mice present a narrow
CC eye fissure and their eyes are nearly closed (PubMed:10854228,
CC PubMed:15278437). Older mice develop blindness (PubMed:17738154). Scd1
CC activity is almost absent in liver, and is not compensated by
CC expression of another family member (PubMed:10899171). Liver levels of
CC total cholesterol esters are decreased by 87%, while plasma cholesterol
CC levels are increased by 35% (PubMed:10899171). Likewise, skin sterol
CC esters and diol diesters are strongly reduced (PubMed:10854228). Liver
CC triglyceride levels are decreased by 62%, while plasma triglyceride
CC levels are decreased by 67% (PubMed:10899171). The fatty acid
CC composition of liver triglycerides is altered, with a decrease of about
CC 85% in palmitoleate (C16:1) and oleate (C18:1) levels
CC (PubMed:10899171). These defects cannot be compensated by a diet
CC enriched in unsaturated fatty acids (PubMed:10899171, PubMed:11441127).
CC {ECO:0000269|PubMed:10545940, ECO:0000269|PubMed:10854228,
CC ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11441127,
CC ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:15278437,
CC ECO:0000269|PubMed:17738154}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile (PubMed:11533264).
CC Compared to wild-type, they consume about 25% more food, but are leaner
CC and acumulate less white adipose tissue (PubMed:12177411,
CC PubMed:17127673). Their liver glycogen levels are lower than wild-type,
CC except when their diet is supplemented with high levels of triolein
CC (PubMed:17127673). They gain weight and accumulate white adipose tissue
CC when their diet contains high levels of triolein (PubMed:17127673).
CC They loose weight on a diet rich in tristearin, contrary to wild-type
CC (PubMed:17127673). Mutant mice cannot maintain their body temperature
CC when exposed to cold; they display hypoglycemia, depleted liver
CC glycogen levels, and die of hypothermia (PubMed:15210843). Mutant mice
CC display increased levels of mitochondrial fatty acid oxidation and
CC decreased expression of genes that are important for de novo
CC lipogenesis, especially when their diet is enriched in saturated fatty
CC acids (PubMed:12177411, PubMed:17127673). Their brown adipose tissues
CC shows increased lipolysis and fatty acid oxidation (PubMed:15210843).
CC They display increased metabolic rates during the day and the night
CC (PubMed:12177411). Liver, skin and white adipose tissue from mutant
CC mice show strongly decreased levels of palmitoleate and reduced levels
CC of oleate, with increased levels of saturated fatty acids
CC (PubMed:11533264). Likewise, skin and eyelids are deficient in
CC cholesterol esters, wax esters and triglycerides (PubMed:11533264).
CC These defects cannot be compensated by a diet enriched in unsaturated
CC fatty acids (PubMed:11533264). Mutant mice have decreased levels of
CC liver and plasma triglycerides (PubMed:17127673). Likewise, the levels
CC of triglycerides, 1,2-diacylglycerol and free fatty acids are decreased
CC in the brown adipose tissue (PubMed:15210843). Besides, brown adipose
CC tissue, liver and plasma triglycerides are depleted in unsaturated
CC fatty acids and are enriched in saturated fatty acids (PubMed:15210843,
CC PubMed:17127673). A diet enriched in triolein increases liver and
CC plasma levels of triglycerides (PubMed:17127673). Mutant mice display
CC lower fasting insulin levels, normal fasting glucose levels, increased
CC glucose tolerance and increased insulin sensitivity (PubMed:12177411).
CC Mutant mice display alopecia and atrophy of sebaceous glands and
CC Meibomian glands (PubMed:11533264). Besides, they present a narrow eye
CC fissure and their eyes are nearly closed (PubMed:11533264). This eye
CC phenotype is probably due to a defect in the production of meibum, the
CC oily material that prevents drying of the cornea. Scd1 activity is
CC almost absent in liver, and is not compensated by expression of another
CC family member (PubMed:11533264). Strongly reduced levels of lipids
CC containing Delta-9 unsaturated fatty acids in the Harderian gland,
CC leading to strongly reduced levels of 1-alkyl-2,3-diacylglycerol in the
CC Harderian gland (PubMed:11500518). {ECO:0000269|PubMed:11500518,
CC ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:12177411,
CC ECO:0000269|PubMed:15210843, ECO:0000269|PubMed:17127673}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; M21285; AAA40103.1; -; Genomic_DNA.
DR EMBL; M21280; AAA40103.1; JOINED; Genomic_DNA.
DR EMBL; M21281; AAA40103.1; JOINED; Genomic_DNA.
DR EMBL; M21282; AAA40103.1; JOINED; Genomic_DNA.
DR EMBL; M21283; AAA40103.1; JOINED; Genomic_DNA.
DR EMBL; M21284; AAA40103.1; JOINED; Genomic_DNA.
DR EMBL; BC007474; AAH07474.1; -; mRNA.
DR EMBL; BC055453; AAH55453.1; -; mRNA.
DR CCDS; CCDS29850.1; -.
DR PIR; A32115; A32115.
DR RefSeq; NP_033153.2; NM_009127.4.
DR PDB; 4YMK; X-ray; 2.60 A; A/D=24-355.
DR PDB; 6WF2; X-ray; 3.51 A; A/B=24-355.
DR PDBsum; 4YMK; -.
DR PDBsum; 6WF2; -.
DR AlphaFoldDB; P13516; -.
DR SMR; P13516; -.
DR STRING; 10090.ENSMUSP00000036936; -.
DR BindingDB; P13516; -.
DR ChEMBL; CHEMBL5353; -.
DR iPTMnet; P13516; -.
DR PhosphoSitePlus; P13516; -.
DR SwissPalm; P13516; -.
DR jPOST; P13516; -.
DR PaxDb; P13516; -.
DR PeptideAtlas; P13516; -.
DR PRIDE; P13516; -.
DR ProteomicsDB; 285595; -.
DR DNASU; 20249; -.
DR Ensembl; ENSMUST00000041331; ENSMUSP00000036936; ENSMUSG00000037071.
DR GeneID; 20249; -.
DR KEGG; mmu:20249; -.
DR UCSC; uc008hpr.2; mouse.
DR CTD; 20249; -.
DR MGI; MGI:98239; Scd1.
DR VEuPathDB; HostDB:ENSMUSG00000037071; -.
DR eggNOG; KOG1600; Eukaryota.
DR GeneTree; ENSGT00940000162971; -.
DR HOGENOM; CLU_027359_0_0_1; -.
DR InParanoid; P13516; -.
DR OMA; IGYHRLY; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; P13516; -.
DR TreeFam; TF313251; -.
DR BRENDA; 1.14.19.1; 3474.
DR BioGRID-ORCS; 20249; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Scd1; mouse.
DR PRO; PR:P13516; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P13516; protein.
DR Bgee; ENSMUSG00000037071; Expressed in thoracic mammary gland and 247 other tissues.
DR ExpressionAtlas; P13516; baseline and differential.
DR Genevisible; P13516; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
DR GO; GO:0032896; F:palmitoyl-CoA 9-desaturase activity; IDA:UniProtKB.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:UniProtKB.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0034435; P:cholesterol esterification; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:MGI.
DR GO; GO:0008610; P:lipid biosynthetic process; TAS:MGI.
DR GO; GO:0055088; P:lipid homeostasis; IMP:MGI.
DR GO; GO:1903966; P:monounsaturated fatty acid biosynthetic process; IDA:MGI.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; TAS:BHF-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0033561; P:regulation of water loss via skin; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0070542; P:response to fatty acid; ISO:MGI.
DR GO; GO:0048733; P:sebaceous gland development; IMP:UniProtKB.
DR GO; GO:0034434; P:sterol esterification; IMP:UniProtKB.
DR GO; GO:1903699; P:tarsal gland development; IMP:UniProtKB.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:UniProtKB.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0050872; P:white fat cell differentiation; IDA:MGI.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Metal-binding; Microsome; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..355
FT /note="Acyl-CoA desaturase 1"
FT /id="PRO_0000185397"
FT TOPO_DOM 1..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16275639"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26098370"
FT TOPO_DOM 90..93
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:26098370"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26098370"
FT TOPO_DOM 115..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26098370"
FT TRANSMEM 214..233
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26098370"
FT TOPO_DOM 234..237
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:26098370"
FT TRANSMEM 238..259
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26098370"
FT TOPO_DOM 260..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16275639"
FT REGION 9..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 116..121
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 153..157
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 294..298
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098370"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:26098370"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:26098370"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098370"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098370"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098370"
FT BINDING 153
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:26098370"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:26098370"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:26098370"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098370"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098370"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26098370"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:26098370"
FT BINDING 294
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:26098370"
FT BINDING 297
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:26098370"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:26098370"
FT VARIANT 278
FT /note="S -> SP (in ab)"
FT /evidence="ECO:0000269|PubMed:15278437"
FT CONFLICT 97
FT /note="C -> A (in Ref. 1; AAA40103)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="E -> D (in Ref. 1; AAA40103)"
FT /evidence="ECO:0000305"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 69..86
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 94..112
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:4YMK"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:4YMK"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:4YMK"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:4YMK"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:4YMK"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:4YMK"
FT TURN 288..292
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:4YMK"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:4YMK"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 337..347
FT /evidence="ECO:0007829|PDB:4YMK"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:4YMK"
SQ 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
