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 24-JAN-2024, entry version 199. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 BioGRID; 203088; 1. DR STRING; 10090.ENSMUSP00000036936; -. DR BindingDB; P13516; -. DR ChEMBL; CHEMBL5353; -. DR iPTMnet; P13516; -. DR PhosphoSitePlus; P13516; -. DR SwissPalm; P13516; -. DR jPOST; P13516; -. DR PaxDb; 10090-ENSMUSP00000036936; -. DR PeptideAtlas; P13516; -. DR ProteomicsDB; 285595; -. DR Pumba; P13516; -. DR DNASU; 20249; -. DR Ensembl; ENSMUST00000041331.4; ENSMUSP00000036936.3; ENSMUSG00000037071.4. DR GeneID; 20249; -. DR KEGG; mmu:20249; -. DR UCSC; uc008hpr.2; mouse. DR AGR; MGI:98239; -. 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; DYATSEW; -. DR OrthoDB; 637961at2759; -. DR PhylomeDB; P13516; -. DR TreeFam; TF313251; -. DR BRENDA; 1.14.19.1; 3474. DR Reactome; R-MMU-75105; Fatty acyl-CoA biosynthesis. DR BioGRID-ORCS; 20249; 6 hits in 79 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 251 other cell types or tissues. DR ExpressionAtlas; P13516; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:WormBase. DR GO; GO:0016020; C:membrane; 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:0042632; P:cholesterol homeostasis; TAS:BHF-UCL. 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:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab. DR GO; GO:0009617; P:response to bacterium; IEP:MGI. DR GO; GO:0070542; P:response to fatty acid; ISO:MGI. DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl. DR GO; GO:0048733; P:sebaceous gland development; IMP:UniProtKB. DR GO; GO:0055092; P:sterol homeostasis; IMP:GO_Central. 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; ACYL-COA DESATURASE; 1. DR PANTHER; PTHR11351:SF69; ACYL-COA DESATURASE 1; 1. DR Pfam; PF00487; FA_desaturase; 1. DR PRINTS; PR00075; FACDDSATRASE. DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1. DR Genevisible; P13516; MM. 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 //