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Protein

Acyl-CoA desaturase 1

Gene

Scd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Stearyl-CoA desaturase that utilizes O2 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).By similarity2 Publications

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.2 Publications

Cofactori

Fe2+2 PublicationsNote: Expected to bind 2 Fe2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741SubstrateBy similarity
Metal bindingi119 – 1191Iron 1By similarity
Metal bindingi124 – 1241Iron 1By similarity
Binding sitei147 – 1471SubstrateBy similarity
Binding sitei154 – 1541SubstrateBy similarity
Binding sitei155 – 1551SubstrateBy similarity
Metal bindingi156 – 1561Iron 1By similarity
Metal bindingi159 – 1591Iron 2By similarity
Metal bindingi160 – 1601Iron 1By similarity
Binding sitei187 – 1871SubstrateBy similarity
Binding sitei188 – 1881SubstrateBy similarity
Binding sitei261 – 2611SubstrateBy similarity
Metal bindingi268 – 2681Iron 2By similarity
Metal bindingi297 – 2971Iron 2By similarity
Metal bindingi300 – 3001Iron 1By similarity
Metal bindingi301 – 3011Iron 2By similarity

GO - Molecular functioni

  • iron ion binding Source: UniProtKB
  • oxidoreductase activity Source: UniProtKB
  • palmitoyl-CoA 9-desaturase activity Source: Ensembl
  • stearoyl-CoA 9-desaturase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14123.
BRENDAi1.14.19.1. 5301.
ReactomeiR-RNO-2426168. Activation of gene expression by SREBF (SREBP).
R-RNO-75105. Fatty Acyl-CoA Biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase 1 (EC:1.14.19.12 Publications)
Alternative name(s):
Delta(9)-desaturase 1Curated
Short name:
Delta-9 desaturase 1Curated
Fatty acid desaturase 1
Stearoyl-CoA desaturase 11 Publication
Gene namesi
Name:Scd1
Synonyms:Scd
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi621176. Scd1.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Curated
  • Membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7171CytoplasmicBy similarityAdd
BLAST
Transmembranei72 – 9221HelicalBy similarityAdd
BLAST
Topological domaini93 – 964LumenalBy similarity
Transmembranei97 – 11721HelicalBy similarityAdd
BLAST
Topological domaini118 – 21699CytoplasmicBy similarityAdd
BLAST
Transmembranei217 – 23620HelicalBy similarityAdd
BLAST
Topological domaini237 – 2404LumenalBy similarity
Transmembranei241 – 26222HelicalBy similarityAdd
BLAST
Topological domaini263 – 35896CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of endoplasmic reticulum membrane Source: RGD
  • integral component of membrane Source: UniProtKB
  • intracellular membrane-bounded organelle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi119 – 1191H → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi124 – 1241H → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi156 – 1561H → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi157 – 1571R → N: No effect on enzyme activity. 1 Publication
Mutagenesisi159 – 1591H → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi160 – 1601H → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi166 – 1661H → A: No effect on enzyme activity. 1 Publication
Mutagenesisi170 – 1701H → A: No effect on enzyme activity; when associated with H-173. 1 Publication
Mutagenesisi173 – 1731R → H: No effect on enzyme activity; when associated with A-170. 1 Publication
Mutagenesisi297 – 2971H → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi300 – 3001H → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi301 – 3011H → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi315 – 3151H → A: No effect on enzyme activity. 1 Publication

Chemistry

ChEMBLiCHEMBL5424.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Acyl-CoA desaturase 1PRO_0000185400Add
BLAST

Proteomic databases

PaxDbiP07308.
PeptideAtlasiP07308.
PRIDEiP07308.

PTM databases

iPTMnetiP07308.
PhosphoSiteiP07308.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

Up-regulated in liver in the absence of dietary unsaturated fatty acids(PubMed:1982442). Expression in adipose tissue seems to be constitutive (PubMed:1982442).1 Publication

Gene expression databases

GenevisibleiP07308. RN.

Interactioni

Protein-protein interaction databases

BioGridi251497. 1 interaction.
STRINGi10116.ENSRNOP00000018447.

Chemistry

BindingDBiP07308.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi119 – 1246Histidine box-1Curated
Motifi156 – 1605Histidine box-2Curated
Motifi297 – 3015Histidine box-3Curated

Domaini

The histidine box domains are involved in binding the catalytic metal ions.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiP07308.
KOiK00507.
OMAiLIPTCKF.
OrthoDBiEOG7ZPNKS.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07308-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAHMLQEIS SSYTTTTTIT EPPSGNLQNG REKMKKVPLY LEEDIRPEMR
60 70 80 90 100
EDIHDPSYQD EEGPPPKLEY VWRNIILMAL LHVGALYGIT LIPSSKVYTL
110 120 130 140 150
LWGIFYYLIS ALGITAGAHR LWSHRTYKAR LPLRIFLIIA NTMAFQNDVY
160 170 180 190 200
EWARDHRAHH KFSETHADPH NSRRGFFFSH VGWLLVRKHP AVKEKGGKLD
210 220 230 240 250
MSDLKAEKLV MFQRRYYKPG LLLMCFILPT LVPWYCWGET FLHSLFVSTF
260 270 280 290 300
LRYTLVLNAT WLVNSAAHLY GYRPYDKNIQ SRENILVSLG AVGEGFHNYH
310 320 330 340 350
HAFPYDYSAS EYRWHINFTT FFIDCMAALG LAYDRKKVSK AAVLARIKRT

GDGSHKSS
Length:358
Mass (Da):41,467
Last modified:November 23, 2004 - v2
Checksum:iB4C960A969B63774
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti291 – 2911A → S in AAA42116 (PubMed:2428815).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02585 mRNA. Translation: AAA42116.1.
AF509568 mRNA. Translation: AAM34745.1.
AF509569 mRNA. Translation: AAM34746.1.
PIRiA24699.
RefSeqiNP_631931.2. NM_139192.2.
XP_006231495.1. XM_006231433.2.
UniGeneiRn.1023.

Genome annotation databases

EnsembliENSRNOT00000018447; ENSRNOP00000018447; ENSRNOG00000013552.
GeneIDi246074.
KEGGirno:246074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02585 mRNA. Translation: AAA42116.1.
AF509568 mRNA. Translation: AAM34745.1.
AF509569 mRNA. Translation: AAM34746.1.
PIRiA24699.
RefSeqiNP_631931.2. NM_139192.2.
XP_006231495.1. XM_006231433.2.
UniGeneiRn.1023.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251497. 1 interaction.
STRINGi10116.ENSRNOP00000018447.

Chemistry

BindingDBiP07308.
ChEMBLiCHEMBL5424.

PTM databases

iPTMnetiP07308.
PhosphoSiteiP07308.

Proteomic databases

PaxDbiP07308.
PeptideAtlasiP07308.
PRIDEiP07308.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018447; ENSRNOP00000018447; ENSRNOG00000013552.
GeneIDi246074.
KEGGirno:246074.

Organism-specific databases

CTDi6319.
RGDi621176. Scd1.

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiP07308.
KOiK00507.
OMAiLIPTCKF.
OrthoDBiEOG7ZPNKS.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14123.
BRENDAi1.14.19.1. 5301.
ReactomeiR-RNO-2426168. Activation of gene expression by SREBF (SREBP).
R-RNO-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

PROiP07308.

Gene expression databases

GenevisibleiP07308. RN.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Construction and sequence of cDNA for rat liver stearyl coenzyme A desaturase."
    Thiede M.A., Ozols J., Strittmatter P.
    J. Biol. Chem. 261:13230-13235(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Structure and regulation of rat liver microsomal stearoyl-CoA desaturase gene."
    Mihara K.
    J. Biochem. 108:1022-1029(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY FAT-FREE DIET.
  3. "Stearoyl-CoA desaturase 1 (Scd1) gene overexpression is associated with genetic predisposition to hepatocarcinogenesis in mice and rats."
    Falvella F.S., Pascale R.M., Gariboldi M., Manenti G., De Miglio M.R., Simile M.M., Dragani T.A., Feo F.
    Carcinogenesis 23:1933-1936(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Brown Norway and Fischer 344.
  4. "Bacterial synthesis of active rat stearyl-CoA desaturase lacking the 26-residue amino-terminal amino acid sequence."
    Strittmatter P., Thiede M.A., Hackett C.S., Ozols J.
    J. Biol. Chem. 263:2532-2535(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase."
    Shanklin J., Whittle E., Fox B.G.
    Biochemistry 33:12787-12794(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, 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.

Entry informationi

Entry nameiACOD1_RAT
AccessioniPrimary (citable) accession number: P07308
Secondary accession number(s): Q8JZL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 23, 2004
Last modified: July 6, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Desaturase has a half-life of only 4 hours.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.