| IED ID | IndEnz0002001327 |
| Enzyme Type ID | protease001327 |
| Protein Name |
Stearoyl-CoA desaturase hSCD1 EC 1.14.19.1 Acyl-CoA desaturase Delta 9 -desaturase Delta-9 desaturase Fatty acid desaturase |
| Gene Name | SCD FADS5 SCD1 SCDOS |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MPAHLLQDDISSSYTTTTTITAPPSRVLQNGGDKLETMPLYLEDDIRPDIKDDIYDPTYKDKEGPSPKVEYVWRNIILMSLLHLGALYGITLIPTCKFYTWLWGVFYYFVSALGITAGAHRLWSHRSYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGSTLDLSDLEAEKLVMFQRRYYKPGLLMMCFILPTLVPWYFWGETFQNSVFVATFLRYAVVLNATWLVNSAAHLFGYRPYDKNISPRENILVSLGAVGEGFHNYHHSFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAILARIKRTGDGNYKSG |
| Enzyme Length | 359 |
| Uniprot Accession Number | O00767 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 75; /note=Substrate; /evidence=ECO:0000269|PubMed:26098317; BINDING 148; /note=Substrate; /evidence=ECO:0000269|PubMed:26098317; BINDING 155; /note=Substrate; /evidence=ECO:0000269|PubMed:26098317; BINDING 156; /note=Substrate; /evidence=ECO:0000269|PubMed:26098317; BINDING 188; /note=Substrate; /evidence=ECO:0000269|PubMed:26098317; BINDING 189; /note=Substrate; /evidence=ECO:0000269|PubMed:26098317; BINDING 262; /note=Substrate; /evidence=ECO:0000269|PubMed:26098317 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387, ChEBI:CHEBI:57394; EC=1.14.19.1; Evidence={ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797, ECO:0000269|PubMed:18765284}; CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 = (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:36931, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57379, ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:15610069}; |
| DNA Binding | |
| EC Number | 1.14.19.1 |
| Enzyme Function | FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:15907797, PubMed:18765284). 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:15907797, PubMed:18765284). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:15610069). Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity). {ECO:0000250|UniProtKB:P13516, ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797, ECO:0000269|PubMed:18765284}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (5); Binding site (7); Chain (1); Helix (21); Metal binding (9); Modified residue (2); Motif (3); Natural variant (1); Sequence conflict (10); Topological domain (5); Transmembrane (4); Turn (4) |
| Keywords | 3D-structure;Direct protein sequencing;Endoplasmic reticulum;Fatty acid biosynthesis;Fatty acid metabolism;Iron;Lipid biosynthesis;Lipid metabolism;Membrane;Metal-binding;Oxidoreductase;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | Q13520; Q9UJ71; P20138; Q9HA82; Q2HXU8-2; Q96BA8; P49447; Q9BQA9; Q9Y282; P08034; Q8TDT2; O15529; Q8TED1; Q7Z5P4; Q8N5M9; P48051; Q9NX47; Q8NI22; Q5SR56; O14880; Q9H2K0; P15151; Q9BRK0; Q86VR2; Q99942; Q9NY72; Q9BY50; Q3KNW5; Q8TBB6; Q9NPE6; P27105; Q9NPL8; Q96MV1; Q3MIR4; O15393-2; Q9Y320; Q3ZAQ7; A0A142I5B9 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15907797}; Multi-pass membrane protein {ECO:0000269|PubMed:18765284, ECO:0000305}. |
| Modified Residue | MOD_RES 198; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 203; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4ZYO; |
| Mapped Pubmed ID | 10400691; 11414710; 12061775; 12401889; 14683458; 14967817; 14967823; 15609334; 15662557; 15708362; 15851470; 15855323; 16213227; 16385451; 16723740; 17614770; 17636091; 17684114; 17852835; 18030445; 18286258; 18340007; 18499418; 18660489; 18697866; 18832746; 18952834; 19130493; 19154947; 19478146; 19710915; 19913121; 20032470; 20195357; 20395685; 20565855; 20579763; 20599700; 20628086; 20713121; 21045174; 21060977; 21179554; 21331774; 21544602; 21658928; 21674150; 21775116; 21831035; 22026420; 22046234; 22049297; 22157815; 22209225; 22457791; 22819528; 22946088; 23013158; 23015656; 23019225; 23139775; 23208590; 23221600; 23331615; 23613812; 23633458; 23934750; 24135379; 24309934; 24356954; 24357007; 24368438; 24375980; 24780075; 24827925; 24864084; 25122791; 25264165; 25528629; 25880005; 26022099; 26224474; 26391970; 26638075; 27223066; 27306423; 27467133; 27562731; 27838812; 27846372; 27861513; 28345489; 28368399; 28397284; 28647567; 28724430; 28765876; 28797843; 28801090; 29396722; 29530061; 30190473; 30517862; 30592142; 30754064; 30884788; 30927246; 31119852; 31235426; 31623522; 31642233; 31708235; 31903889; 31915810; 31993937; 32350414; 32392704; 32438926; 32670392; 33430034; 33511729; 33612070; 33904180; 34030117; 34171462; 34621052; 34680068; |
| Motif | MOTIF 120..125; /note=Histidine box-1; /evidence=ECO:0000305; MOTIF 157..161; /note=Histidine box-2; /evidence=ECO:0000305; MOTIF 298..302; /note=Histidine box-3; /evidence=ECO:0000305 |
| Gene Encoded By | |
| Mass | 41,523 |
| Kinetics | |
| Metal Binding | METAL 120; /note=Iron 1; /evidence=ECO:0000305|PubMed:26098317; METAL 125; /note=Iron 1; /evidence=ECO:0000305|PubMed:26098317; METAL 157; /note=Iron 1; /evidence=ECO:0000305|PubMed:26098317; METAL 160; /note=Iron 2; /evidence=ECO:0000305|PubMed:26098317; METAL 161; /note=Iron 1; /evidence=ECO:0000305|PubMed:26098317; METAL 269; /note=Iron 2; /evidence=ECO:0000305|PubMed:26098317; METAL 298; /note=Iron 2; /evidence=ECO:0000305|PubMed:26098317; METAL 301; /note=Iron 1; /evidence=ECO:0000305|PubMed:26098317; METAL 302; /note=Iron 2; /evidence=ECO:0000305|PubMed:26098317 |
| Rhea ID | RHEA:19721; RHEA:36931 |
| Cross Reference Brenda | 1.14.19.1; |