ID ACOD_SHEEP Reviewed; 359 AA. AC O62849; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Acyl-CoA desaturase; DE EC=1.14.19.1 {ECO:0000250|UniProtKB:P13516}; DE AltName: Full=Delta(9)-desaturase; DE Short=Delta-9 desaturase; DE AltName: Full=Fatty acid desaturase; DE AltName: Full=Stearoyl-CoA desaturase {ECO:0000303|PubMed:9554990}; GN Name=SCD; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Y1089; TISSUE=Adipose tissue; RX PubMed=9554990; DOI=10.1016/s0005-2760(97)00210-5; RA Ward R.J., Travers M.T., Richards S.E., Vernon R.G., Salter A.M., RA Buttery P.J., Barber M.C.; RT "Stearoyl-CoA desaturase mRNA is transcribed from a single gene in the RT ovine genome."; RL Biochim. Biophys. Acta 1391:145-156(1998). 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 (By similarity). Gives rise to a mixture CC of 16:1 and 18:1 unsaturated fatty acids. Plays an important role in CC lipid biosynthesis. Plays an important role in regulating the CC expression of genes that are involved in lipogenesis and in regulating CC mitochondrial fatty acid oxidation (By similarity). Plays an important CC role in body energy homeostasis (By similarity). Contributes to the CC biosynthesis of membrane phospholipids, cholesterol esters and CC triglycerides (By similarity). {ECO:0000250|UniProtKB:O00767, CC ECO:0000250|UniProtKB:P13516}. 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:0000250|UniProtKB:P13516}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000250|UniProtKB:P13516}; CC Note=Expected to bind 2 Fe(2+) ions per subunit. CC {ECO:0000250|UniProtKB:P13516}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:P13516}; Multi-pass membrane protein CC {ECO:0000305}. CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic CC metal ions. {ECO:0000250|UniProtKB:O00767}. 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; AJ001048; CAA04502.1; -; mRNA. DR RefSeq; NP_001009254.1; NM_001009254.1. DR AlphaFoldDB; O62849; -. DR SMR; O62849; -. DR STRING; 9940.ENSOARP00000015742; -. DR PaxDb; 9940-ENSOARP00000015742; -. DR GeneID; 443185; -. DR KEGG; oas:443185; -. DR CTD; 6319; -. DR eggNOG; KOG1600; Eukaryota. DR OrthoDB; 637961at2759; -. DR Proteomes; UP000002356; Unplaced. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB. DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB. DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:AgBase. DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; ISS:UniProtKB. DR CDD; cd03505; Delta9-FADS-like; 1. DR InterPro; IPR015876; Acyl-CoA_DS. DR InterPro; IPR001522; FADS-1_CS. DR PANTHER; PTHR11351; ACYL-COA DESATURASE; 1. DR PANTHER; PTHR11351:SF102; STEAROYL-COA DESATURASE; 1. DR PRINTS; PR00075; FACDDSATRASE. DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1. PE 2: Evidence at transcript level; KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism; KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding; KW Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..359 FT /note="Acyl-CoA desaturase" FT /id="PRO_0000185402" FT TOPO_DOM 1..72 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TRANSMEM 73..93 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TOPO_DOM 94..97 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TRANSMEM 98..118 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TOPO_DOM 119..217 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TRANSMEM 218..237 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TOPO_DOM 238..241 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TRANSMEM 242..263 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TOPO_DOM 264..359 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O00767" FT MOTIF 120..125 FT /note="Histidine box-1" FT /evidence="ECO:0000305" FT MOTIF 157..161 FT /note="Histidine box-2" FT /evidence="ECO:0000305" FT MOTIF 298..302 FT /note="Histidine box-3" FT /evidence="ECO:0000305" FT BINDING 75 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 120 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 125 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 148 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 155 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 156 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 157 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 160 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 161 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 188 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 189 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 262 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 269 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 298 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 301 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 302 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P13516" FT MOD_RES 203 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O00767" SQ SEQUENCE 359 AA; 41671 MW; 219CFEBB1E353418 CRC64; MPAHLLQEEI SSSYTTTTTI TAPPSRVLQN GGGKLEKTPL YLEEDIRPEM RDDIYDPNYQ DKEGPKPKLE YVWRNIILMG LLHLGALYGI TLIPTCKIYT FLWVLFYYVI SALGITAGVH RLWSHRTYKA RLPLRVFLII ANTMAFQNDV FEWSRDHRAH HKFSETDADP HNSRRGFFFS HVGWLLVRKH PAVREKGATL DLSDLRAEKL VMFQRRYYKP GVLLLCFILP TLVPWYLWGE SFQNSLFFAT FLRYAVVLNA TWLVNSAAHM YGYRPYDKTI NPRENILVSL GAVGEGFHNY HHTFPYDYSA SEYRWHINFT TFFIDCMAAI GLAYDRKKVS KAAVLGRMKR TGEESYKSG //