ACOD_SHEEP
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 03-AUG-2022, entry version 108.
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}.
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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 GeneID; 443185; -.
DR KEGG; oas:443185; -.
DR CTD; 6319; -.
DR eggNOG; KOG1600; Eukaryota.
DR OrthoDB; 971318at2759; -.
DR Proteomes; UP000002356; 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; 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; PTHR11351; 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
