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Acyl-CoA desaturase 1 (EC 1.14.19.1) (Delta(9)-desaturase 1) (Delta-9 desaturase 1) (Fatty acid desaturase 1) (Stearoyl-CoA desaturase 1)

 ACOD1_RAT               Reviewed;         358 AA.
P07308; Q8JZL5;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 2.
23-MAY-2018, entry version 154.
RecName: Full=Acyl-CoA desaturase 1;
EC=1.14.19.1 {ECO:0000269|PubMed:2892838, ECO:0000269|PubMed:7947684};
AltName: Full=Delta(9)-desaturase 1 {ECO:0000305};
Short=Delta-9 desaturase 1 {ECO:0000305};
AltName: Full=Fatty acid desaturase 1;
AltName: Full=Stearoyl-CoA desaturase 1 {ECO:0000303|PubMed:12419843};
Name=Scd1; Synonyms=Scd;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2428815;
Thiede M.A., Ozols J., Strittmatter P.;
"Construction and sequence of cDNA for rat liver stearyl coenzyme A
desaturase.";
J. Biol. Chem. 261:13230-13235(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY
FAT-FREE DIET.
PubMed=1982442; DOI=10.1093/oxfordjournals.jbchem.a123301;
Mihara K.;
"Structure and regulation of rat liver microsomal stearoyl-CoA
desaturase gene.";
J. Biochem. 108:1022-1029(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Brown Norway, and Fischer 344;
PubMed=12419843; DOI=10.1093/carcin/23.11.1933;
Falvella F.S., Pascale R.M., Gariboldi M., Manenti G., De Miglio M.R.,
Simile M.M., Dragani T.A., Feo F.;
"Stearoyl-CoA desaturase 1 (Scd1) gene overexpression is associated
with genetic predisposition to hepatocarcinogenesis in mice and
rats.";
Carcinogenesis 23:1933-1936(2002).
[4]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=2892838;
Strittmatter P., Thiede M.A., Hackett C.S., Ozols J.;
"Bacterial synthesis of active rat stearyl-CoA desaturase lacking the
26-residue amino-terminal amino acid sequence.";
J. Biol. Chem. 263:2532-2535(1988).
[5]
CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF HIS-119; HIS-124;
HIS-156; ARG-157; HIS-159; HIS-160; HIS-166; HIS-170; ARG-173;
HIS-297; HIS-300 AND HIS-301.
PubMed=7947684; DOI=10.1021/bi00209a009;
Shanklin J., Whittle E., Fox B.G.;
"Eight histidine residues are catalytically essential in a membrane-
associated iron enzyme, stearoyl-CoA desaturase, and are conserved in
alkane hydroxylase and xylene monooxygenase.";
Biochemistry 33:12787-12794(1994).
-!- FUNCTION: Stearyl-CoA desaturase that utilizes O(2) and electrons
from reduced cytochrome b5 to introduce the first double bond into
saturated fatty acyl-CoA substrates (PubMed:2892838,
PubMed:7947684). Catalyzes the insertion of a cis double bond at
the Delta-9 position into fatty acyl-CoA substrates including
palmitoyl-CoA and stearoyl-CoA (PubMed:2892838, PubMed:7947684).
Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids.
Plays an important role in lipid biosynthesis. Plays an important
role in regulating the expression of genes that are involved in
lipogenesis and in regulating mitochondrial fatty acid oxidation
(By similarity). Plays an important role in body energy
homeostasis (By similarity). Contributes to the biosynthesis of
membrane phospholipids, cholesterol esters and triglycerides
(PubMed:7947684). Required for normal development of sebaceous
glands. Required for the biosynthesis of normal levels of Delta-9
unsaturated fatty acids and 1-alkyl-2,3-diacylglycerol in the
Harderian gland. Required for normal production of meibum, an oily
material that prevents drying of the cornea (By similarity).
{ECO:0000250|UniProtKB:P13516, ECO:0000269|PubMed:2892838,
ECO:0000269|PubMed:7947684}.
-!- CATALYTIC ACTIVITY: Stearoyl-CoA + 2 ferrocytochrome b5 + O(2) + 2
H(+) = oleoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O.
{ECO:0000269|PubMed:2892838, ECO:0000269|PubMed:7947684}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000305|PubMed:2892838,
ECO:0000305|PubMed:7947684};
Note=Expected to bind 2 Fe(2+) ions per subunit.
{ECO:0000250|UniProtKB:P13516};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:O00767}; Multi-pass membrane protein
{ECO:0000305}. Membrane {ECO:0000269|PubMed:2892838}; Multi-pass
membrane protein {ECO:0000269|PubMed:2892838}.
-!- TISSUE SPECIFICITY: Detected in liver (at protein level)
(PubMed:2892838). Detected in adipose tissue. Detected in liver
when rats are kept on a fat-free diet, but not when their food
contains unsaturated fatty acids. {ECO:0000269|PubMed:1982442}.
-!- INDUCTION: Up-regulated in liver in the absence of dietary
unsaturated fatty acids(PubMed:1982442). Expression in adipose
tissue seems to be constitutive (PubMed:1982442).
{ECO:0000269|PubMed:1982442}.
-!- DOMAIN: The histidine box domains are involved in binding the
catalytic metal ions. {ECO:0000305|PubMed:7947684}.
-!- MISCELLANEOUS: Desaturase has a half-life of only 4 hours.
-!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; J02585; AAA42116.1; -; mRNA.
EMBL; AF509568; AAM34745.1; -; mRNA.
EMBL; AF509569; AAM34746.1; -; mRNA.
PIR; A24699; A24699.
RefSeq; NP_631931.2; NM_139192.2.
RefSeq; XP_006231495.1; XM_006231433.2.
UniGene; Rn.1023; -.
SMR; P07308; -.
BioGrid; 251497; 1.
STRING; 10116.ENSRNOP00000018447; -.
BindingDB; P07308; -.
ChEMBL; CHEMBL5424; -.
iPTMnet; P07308; -.
PhosphoSitePlus; P07308; -.
PaxDb; P07308; -.
PeptideAtlas; P07308; -.
PRIDE; P07308; -.
Ensembl; ENSRNOT00000018447; ENSRNOP00000018447; ENSRNOG00000013552.
GeneID; 246074; -.
KEGG; rno:246074; -.
CTD; 6319; -.
RGD; 621176; Scd1.
eggNOG; KOG1600; Eukaryota.
eggNOG; COG1398; LUCA.
GeneTree; ENSGT00530000063158; -.
HOGENOM; HOG000270352; -.
HOVERGEN; HBG003367; -.
InParanoid; P07308; -.
KO; K00507; -.
OMA; HATWGWG; -.
OrthoDB; EOG091G0B5S; -.
BioCyc; MetaCyc:MONOMER-14123; -.
BRENDA; 1.14.19.1; 5301.
Reactome; R-RNO-75105; Fatty acyl-CoA biosynthesis.
PRO; PR:P07308; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000013552; -.
Genevisible; P07308; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; TAS:RGD.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
GO; GO:0016491; F:oxidoreductase activity; IMP:UniProtKB.
GO; GO:0032896; F:palmitoyl-CoA 9-desaturase activity; IEA:Ensembl.
GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:UniProtKB.
GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
GO; GO:0034435; P:cholesterol esterification; IEA:Ensembl.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
GO; GO:0006633; P:fatty acid biosynthetic process; TAS:RGD.
GO; GO:0008610; P:lipid biosynthetic process; IEP:RGD.
GO; GO:1903966; P:monounsaturated fatty acid biosynthetic process; IBA:GO_Central.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0033561; P:regulation of water loss via skin; IEA:Ensembl.
GO; GO:0070542; P:response to fatty acid; IDA:UniProtKB.
GO; GO:1903699; P:tarsal gland development; IEA:Ensembl.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB.
GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl.
CDD; cd03505; Delta9-FADS-like; 1.
InterPro; IPR015876; Acyl-CoA_DS.
InterPro; IPR005804; FA_desaturase_dom.
InterPro; IPR001522; FADS-1_CS.
PANTHER; PTHR11351; PTHR11351; 1.
Pfam; PF00487; FA_desaturase; 1.
PRINTS; PR00075; FACDDSATRASE.
PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
Fatty acid biosynthesis; Fatty acid metabolism; Iron;
Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 358 Acyl-CoA desaturase 1.
/FTId=PRO_0000185400.
TOPO_DOM 1 71 Cytoplasmic.
{ECO:0000250|UniProtKB:P13516}.
TRANSMEM 72 92 Helical. {ECO:0000250|UniProtKB:P13516}.
TOPO_DOM 93 96 Lumenal. {ECO:0000250|UniProtKB:P13516}.
TRANSMEM 97 117 Helical. {ECO:0000250|UniProtKB:P13516}.
TOPO_DOM 118 216 Cytoplasmic.
{ECO:0000250|UniProtKB:P13516}.
TRANSMEM 217 236 Helical. {ECO:0000250|UniProtKB:P13516}.
TOPO_DOM 237 240 Lumenal. {ECO:0000250|UniProtKB:P13516}.
TRANSMEM 241 262 Helical. {ECO:0000250|UniProtKB:P13516}.
TOPO_DOM 263 358 Cytoplasmic.
{ECO:0000250|UniProtKB:P13516}.
MOTIF 119 124 Histidine box-1. {ECO:0000305}.
MOTIF 156 160 Histidine box-2. {ECO:0000305}.
MOTIF 297 301 Histidine box-3. {ECO:0000305}.
METAL 119 119 Iron 1. {ECO:0000250|UniProtKB:P13516}.
METAL 124 124 Iron 1. {ECO:0000250|UniProtKB:P13516}.
METAL 156 156 Iron 1. {ECO:0000250|UniProtKB:P13516}.
METAL 159 159 Iron 2. {ECO:0000250|UniProtKB:P13516}.
METAL 160 160 Iron 1. {ECO:0000250|UniProtKB:P13516}.
METAL 268 268 Iron 2. {ECO:0000250|UniProtKB:P13516}.
METAL 297 297 Iron 2. {ECO:0000250|UniProtKB:P13516}.
METAL 300 300 Iron 1. {ECO:0000250|UniProtKB:P13516}.
METAL 301 301 Iron 2. {ECO:0000250|UniProtKB:P13516}.
BINDING 74 74 Substrate.
{ECO:0000250|UniProtKB:O00767}.
BINDING 147 147 Substrate.
{ECO:0000250|UniProtKB:O00767}.
BINDING 154 154 Substrate.
{ECO:0000250|UniProtKB:O00767}.
BINDING 155 155 Substrate.
{ECO:0000250|UniProtKB:O00767}.
BINDING 187 187 Substrate.
{ECO:0000250|UniProtKB:O00767}.
BINDING 188 188 Substrate.
{ECO:0000250|UniProtKB:O00767}.
BINDING 261 261 Substrate.
{ECO:0000250|UniProtKB:O00767}.
MUTAGEN 119 119 H->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 124 124 H->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 156 156 H->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 157 157 R->N: No effect on enzyme activity.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 159 159 H->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 160 160 H->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 166 166 H->A: No effect on enzyme activity.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 170 170 H->A: No effect on enzyme activity; when
associated with H-173.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 173 173 R->H: No effect on enzyme activity; when
associated with A-170.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 297 297 H->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 300 300 H->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 301 301 H->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:7947684}.
MUTAGEN 315 315 H->A: No effect on enzyme activity.
{ECO:0000269|PubMed:7947684}.
CONFLICT 291 291 A -> S (in Ref. 1; AAA42116).
{ECO:0000305}.
SEQUENCE 358 AA; 41467 MW; B4C960A969B63774 CRC64;
MPAHMLQEIS SSYTTTTTIT EPPSGNLQNG REKMKKVPLY LEEDIRPEMR EDIHDPSYQD
EEGPPPKLEY VWRNIILMAL LHVGALYGIT LIPSSKVYTL LWGIFYYLIS ALGITAGAHR
LWSHRTYKAR LPLRIFLIIA NTMAFQNDVY EWARDHRAHH KFSETHADPH NSRRGFFFSH
VGWLLVRKHP AVKEKGGKLD MSDLKAEKLV MFQRRYYKPG LLLMCFILPT LVPWYCWGET
FLHSLFVSTF LRYTLVLNAT WLVNSAAHLY GYRPYDKNIQ SRENILVSLG AVGEGFHNYH
HAFPYDYSAS EYRWHINFTT FFIDCMAALG LAYDRKKVSK AAVLARIKRT GDGSHKSS


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