ID ACOD_CYPCA Reviewed; 327 AA. AC Q92038; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 2. DT 27-MAR-2024, entry version 97. 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 {ECO:0000303|PubMed:8629000}; DE AltName: Full=Fatty acid desaturase; DE AltName: Full=Stearoyl-CoA desaturase; OS Cyprinus carpio (Common carp). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Cyprininae; Cyprinus. OX NCBI_TaxID=7962; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION. RC TISSUE=Liver; RX PubMed=8629000; DOI=10.1126/science.271.5250.815; RA Tiku P.E., Gracey A.Y., Macartney A.I., Beynon R.J., Cossins A.R.; RT "Cold-induced expression of delta 9-desaturase in carp by transcriptional RT and posttranslational mechanisms."; RL Science 271:815-818(1996). RN [2] RP SEQUENCE REVISION TO 11-25 AND C-TERMINUS. RA Tiku P.E.; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. 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. Has high specificity and catalyzes the CC insertion of a cis double bond at the delta-9 position into fatty acyl- CC CoA substrates including palmitoyl-CoA and stearoyl-CoA. Contributes to CC the biosynthesis of membrane phospholipids, cholesterol esters and CC triglycerides. {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:O00767}; Multi-pass membrane protein CC {ECO:0000305}. CC -!- INDUCTION: By cold. A 10-fold increase in transcript levels is observed CC 48-60 hours after cooling. {ECO:0000269|PubMed:8629000}. 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; U31864; AAB03857.2; -; mRNA. DR AlphaFoldDB; Q92038; -. DR SMR; Q92038; -. DR Proteomes; UP000694384; Unplaced. DR Proteomes; UP000694427; Unplaced. DR Proteomes; UP000694700; Unplaced. DR Proteomes; UP000694701; Unplaced. DR Proteomes; UP001155660; Genome assembly. 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; ISS:UniProtKB. 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; IPR005804; FA_desaturase_dom. DR InterPro; IPR001522; FADS-1_CS. DR PANTHER; PTHR11351; ACYL-COA DESATURASE; 1. DR PANTHER; PTHR11351:SF102; STEAROYL-COA DESATURASE; 1. DR Pfam; PF00487; FA_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; Reference proteome; Stress response; Transmembrane; KW Transmembrane helix. FT CHAIN 1..327 FT /note="Acyl-CoA desaturase" FT /id="PRO_0000185403" FT TOPO_DOM 1..39 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TRANSMEM 40..60 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TOPO_DOM 61..64 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TRANSMEM 65..85 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TOPO_DOM 86..184 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TRANSMEM 185..204 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TOPO_DOM 205..208 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TRANSMEM 209..230 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O00767" FT TOPO_DOM 231..327 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O00767" FT MOTIF 87..92 FT /note="Histidine box-1" FT /evidence="ECO:0000305" FT MOTIF 124..128 FT /note="Histidine box-2" FT /evidence="ECO:0000305" FT MOTIF 265..269 FT /note="Histidine box-3" FT /evidence="ECO:0000305" FT BINDING 42 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 87 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 92 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 115 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 122 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 123 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 124 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 127 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 128 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P13516" 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 229 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O00767" FT BINDING 236 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 265 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 268 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P13516" FT BINDING 269 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P13516" SQ SEQUENCE 327 AA; 37820 MW; 3E794CB408D33089 CRC64; MPDREIKSPI WHPEPGTVED VFDHTYKEKE GPKPPTVIVW RNVILMSLLH LGALYGLFLF PSARALTWIW FFGCLLFSAL GITAGAHRLW SHRSYKASLP LQIFLALGNS MAFQNDIYEW SRDHRVHHKY SETDADPHNA VRGFFFSHVG WLLVRKHPDV IEKGRKLELS DLKADKVVMF QRRFYKPSVL LMCFFVPTFV PWYVWGESLW VAYFVPALLR YALVLNATWL VNSAAHMWGN RPYDSSINPR ENRFVTFSAI GEGFHNYHHT FPFDYATSEF GCKLNLTTCC FIDLMCFLGL AREPKRVSRE AVLARAQRTG DGSHWSG //