SCD_PIG
ID SCD_PIG Reviewed; 359 AA.
AC O02858; A0A4X1U207; Q6RWA7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 116.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=15147407; DOI=10.1111/j.1365-2052.2004.01129.x;
RA Ren J., Knorr C., Guo Y.M., Ding N.S., Ai H.S., Brenig B., Huang L.S.;
RT "Characterization of five single nucleotide polymorphisms in the porcine
RT stearoyl-CoA desaturase (SCD) gene.";
RL Anim. Genet. 35:255-257(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15556291; DOI=10.1016/j.gene.2004.06.017;
RA Ren J., Knorr C., Huang L., Brenig B.;
RT "Isolation and molecular characterization of the porcine stearoyl-CoA
RT desaturase gene.";
RL Gene 340:19-30(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hannum G.I., Koren S., Schroeder S.G., Chin S.C., Nonneman D.J.,
RA Becker S.A., Rosen B.D., Bickhart D.M., Putnam N.H., Green R.E.,
RA Tuggle C.K., Liu H., Rohrer G.A., Warr A., Hall R., Kim K., Hume D.A.,
RA Talbot R., Chow W., Howe K., Schwartz A.S., Watson M., Archibald A.L.,
RA Phillippy A.M., Smith T.P.L.;
RT "USMARCv1.0.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-334.
RA Fumiere O.;
RL Submitted (JUN-1997) 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. 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}.
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DR EMBL; Z97186; CAB10004.1; -; mRNA.
DR EMBL; AY487829; AAR87713.1; -; mRNA.
DR EMBL; AY487830; AAR87714.1; -; Genomic_DNA.
DR EMBL; JN613287; AEY68756.1; -; mRNA.
DR EMBL; DQIR01249731; HDC05209.1; -; Transcribed_RNA.
DR RefSeq; NP_998946.1; NM_213781.1.
DR AlphaFoldDB; O02858; -.
DR SMR; O02858; -.
DR STRING; 9823.ENSSSCP00000011244; -.
DR PaxDb; O02858; -.
DR PRIDE; O02858; -.
DR Ensembl; ENSSSCT00015091855; ENSSSCP00015037586; ENSSSCG00015068485.
DR Ensembl; ENSSSCT00070027417; ENSSSCP00070022809; ENSSSCG00070014006.
DR GeneID; 396670; -.
DR KEGG; ssc:396670; -.
DR CTD; 6319; -.
DR eggNOG; KOG1600; Eukaryota.
DR HOGENOM; CLU_027359_0_0_1; -.
DR InParanoid; O02858; -.
DR OMA; SCGESWH; -.
DR OrthoDB; 971318at2759; -.
DR TreeFam; TF313251; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 14.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
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..359
FT /note="Stearoyl-CoA desaturase"
FT /id="PRO_0000185399"
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"
FT CONFLICT 35
FT /note="L -> S (in Ref. 4; CAB10004)"
FT CONFLICT 66..67
FT /note="RP -> QG (in Ref. 4; CAB10004)"
SQ SEQUENCE 359 AA; 41376 MW; 5AC07C9534ADAA0B CRC64;
MPAHLLQEEI SSSYTTTTTI TAPSSRVLQN GGGKLEKTPQ YVEEDIRPEM KDDIYDPTYQ
DKEGPRPKLE YVWRNIILMS LLHLGALYGI ILIPTCKIYT LLWAFAYYLL SAVGVTAGAH
RLWSHRTYKA RLPLRVFLII ANTMAFQNDV YEWARDHRAH HKFSETDADP HNSRRGFFFS
HVGWLLVRKH PAVKEKGGLL NMSDLKAEKL VMFQRRYYKP GILLMCFILP TIVPWYCWGE
AFPQSLFVAT FLRYAIVLNA TWLVNSAAHL YGYRPYDKTI SPRENILVSL GAVGEGFHNY
HHTFPYDYSA SEYRWHINLT TFFIDCMAAL GLAYDRKKVS KAAILARIKR TGDESYKSG
