SCD1_TACFU
ID SCD1_TACFU Reviewed; 331 AA.
AC A0A0C5Q309;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Acyl-CoA desaturase 1 {ECO:0000305};
DE EC=1.14.19.1 {ECO:0000250|UniProtKB:P13516};
DE AltName: Full=Delta(9)-desaturase 1 {ECO:0000305};
DE Short=Delta-9 desaturase 1 {ECO:0000305};
DE AltName: Full=Fatty acid desaturase 1 {ECO:0000305};
DE AltName: Full=Stearoyl-CoA desaturase 1 {ECO:0000303|PubMed:25497832, ECO:0000312|EMBL:AJQ20791.1};
GN Name=SCD1 {ECO:0000303|PubMed:25497832, ECO:0000312|EMBL:AJQ20791.1};
OS Tachysurus fulvidraco (Yellow catfish) (Pimelodus fulvidraco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Bagridae; Tachysurus.
OX NCBI_TaxID=1234273 {ECO:0000312|EMBL:AJQ20791.1};
RN [1] {ECO:0000312|EMBL:AJQ20791.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, AND PHYLOGENETIC
RP ANALYSIS.
RC TISSUE=Liver {ECO:0000303|PubMed:25497832};
RX PubMed=25497832; DOI=10.1016/j.gene.2014.12.014;
RA Song Y.F., Luo Z., Pan Y.X., Zhang L.H., Chen Q.L., Zheng J.L.;
RT "Three unsaturated fatty acid biosynthesis-related genes in yellow catfish
RT Pelteobagrus fulvidraco: Molecular characterization, tissue expression and
RT transcriptional regulation by leptin.";
RL Gene 563:1-9(2015).
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. Contributes to the biosynthesis of
CC membrane phospholipids, cholesterol esters and triglycerides.
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:0000255|RuleBase:RU000581};
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:0000250|UniProtKB:P13516}.
CC -!- TISSUE SPECIFICITY: Expression is highest in liver, followed by brain
CC and intestine, and lowest in spleen. Also expressed in heart, gill and
CC muscle. {ECO:0000269|PubMed:25497832}.
CC -!- INDUCTION: Expression is transcriptionally down-regulated by
CC intraperitoneal injection of human leptin at 24 hours and 48 hours
CC post-injection. {ECO:0000269|PubMed:25497832}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000255|RuleBase:RU000581}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000255|RuleBase:RU000581, ECO:0000305}.
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DR EMBL; KJ818303; AJQ20791.1; -; mRNA.
DR AlphaFoldDB; A0A0C5Q309; -.
DR SMR; A0A0C5Q309; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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; Transmembrane; Transmembrane helix.
FT CHAIN 1..331
FT /note="Acyl-CoA desaturase 1"
FT /id="PRO_0000441396"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TOPO_DOM 68..71
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TRANSMEM 72..90
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TOPO_DOM 91..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TOPO_DOM 210..213
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TRANSMEM 214..235
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT TOPO_DOM 236..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT MOTIF 92..97
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT MOTIF 129..133
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT MOTIF 270..274
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 49
FT /ligand="substrate"
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 97
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="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 129
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 132
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 241
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 270
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 273
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 274
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
SQ SEQUENCE 331 AA; 37621 MW; 8F3242F9EE5D01F1 CRC64;
MTEVDDGCGG RLRGSVLLED ECDLKQECET PTHSLVQGRD PPVVVVWRNV VLMSVLHTAA
VYGLVLLPSA SAYTLLAFCF VSSALGITAG AHRLWSHRSY KASLPLRIFL AVANSMGFQN
DIYEWARDHR VHHKYSETDA DPHNASRGFF FAHIGWLLVK KHPKVIENGQ KLELSDLKND
RVVMFQRRFY KHSVVVMCFL IPAMLPWFLW AESLWVGYFV PVLLRYALVL NATWLVNSAA
HMWGNQPYDV NINPRENRFV TFSAIGEGFH NYHHTFPYDY ATSEFGCRLN LTTCFINLMC
VLGLAKDCRR VPTELVMARV KRTGDGSHRS G
