SCD_MESAU
ID SCD_MESAU Reviewed; 354 AA.
AC Q64420;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Stearoyl-CoA desaturase;
DE EC=1.14.19.1 {ECO:0000250|UniProtKB:P13516};
DE AltName: Full=Acyl-CoA desaturase;
DE AltName: Full=Delta(9)-desaturase;
DE Short=Delta-9 desaturase;
DE AltName: Full=Fatty acid desaturase;
GN Name=SCD; Synonyms=FAR-17c {ECO:0000303|PubMed:7772580};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7772580; DOI=10.1016/0923-1811(94)00357-k;
RA Ideta R., Seki T., Adachi K.;
RT "Sequence analysis and characterization of FAR-17c, an androgen-dependent
RT gene in the flank organs of hamsters.";
RL J. Dermatol. Sci. 9:94-102(1995).
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: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 -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 =
CC (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36931, 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:57379,
CC ChEBI:CHEBI:61540; Evidence={ECO:0000250|UniProtKB:O00767};
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; L26956; AAC42058.1; -; mRNA.
DR AlphaFoldDB; Q64420; -.
DR SMR; Q64420; -.
DR eggNOG; KOG1600; Eukaryota.
DR BRENDA; 1.14.19.1; 3239.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of 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; PTHR11351; 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; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..354
FT /note="Stearoyl-CoA desaturase"
FT /id="PRO_0000185396"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 89..92
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 114..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 213..232
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 233..236
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 237..258
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 259..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 115..120
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 152..156
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 293..297
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT COMPBIAS 8..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
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 143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 152
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="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 293
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 297
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00767"
SQ SEQUENCE 354 AA; 40968 MW; B41A0831845EB874 CRC64;
MPGHLLQEEM TSSYTTTTTT ITEPPSESLQ KTVPLYLEED IRPEMKEDIY DPSYQDEEGP
PPKLEYVWRN IILMALLHLG ALYGLVLVPS SKVYTLLWAF VYYVISIEGI GAGVHRLWSH
RTYKARLPLR IFLIIANTMA FQNDVYEWAR DHRAHHKFSE TYADPHDSRR GFFFSHVGWL
LVRKHPAVKE KGGKLDMSDL KAEKLVMFQR RYYKPAILLM CFILPTFVPW YFWGEAFVNS
LCVSTFLRYT LVLNATWLVN SAAHLYGYRP YDKNIDPREN ALVSLGCLGE GFHNYHHAFP
YDYSASEYRW HINFTTFFID CMAALGLAYD RKKVSKAAVL ARIKRTGDGS CKSG
