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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)DescriptionActionsGraphical viewLength
Binding sitei74SubstrateBy similarity1
Metal bindingi119Iron 1By similarity1
Metal bindingi124Iron 1By similarity1
Binding sitei147SubstrateBy similarity1
Binding sitei154SubstrateBy similarity1
Binding sitei155SubstrateBy similarity1
Metal bindingi156Iron 1By similarity1
Metal bindingi159Iron 2By similarity1
Metal bindingi160Iron 1By similarity1
Binding sitei187SubstrateBy similarity1
Binding sitei188SubstrateBy similarity1
Binding sitei261SubstrateBy similarity1
Metal bindingi268Iron 2By similarity1
Metal bindingi297Iron 2By similarity1
Metal bindingi300Iron 1By similarity1
Metal bindingi301Iron 2By similarity1

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)DescriptionActionsGraphical viewLength
Topological domaini1 – 71CytoplasmicBy similarityAdd BLAST71
Transmembranei72 – 92HelicalBy similarityAdd BLAST21
Topological domaini93 – 96LumenalBy similarity4
Transmembranei97 – 117HelicalBy similarityAdd BLAST21
Topological domaini118 – 216CytoplasmicBy similarityAdd BLAST99
Transmembranei217 – 236HelicalBy similarityAdd BLAST20
Topological domaini237 – 240LumenalBy similarity4
Transmembranei241 – 262HelicalBy similarityAdd BLAST22
Topological domaini263 – 358CytoplasmicBy similarityAdd BLAST96

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)DescriptionActionsGraphical viewLength
Mutagenesisi119H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi124H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi156H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi157R → N: No effect on enzyme activity. 1 Publication1
Mutagenesisi159H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi160H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi166H → A: No effect on enzyme activity. 1 Publication1
Mutagenesisi170H → A: No effect on enzyme activity; when associated with H-173. 1 Publication1
Mutagenesisi173R → H: No effect on enzyme activity; when associated with A-170. 1 Publication1
Mutagenesisi297H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi300H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi301H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi315H → A: No effect on enzyme activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5424.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001854001 – 358Acyl-CoA desaturase 1Add BLAST358

Proteomic databases

PaxDbiP07308.
PeptideAtlasiP07308.
PRIDEiP07308.

PTM databases

iPTMnetiP07308.
PhosphoSitePlusiP07308.

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

BgeeiENSRNOG00000013552.
GenevisibleiP07308. RN.

Interactioni

Protein-protein interaction databases

BioGridi251497. 1 interactor.
STRINGi10116.ENSRNOP00000018447.

Chemistry databases

BindingDBiP07308.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi119 – 124Histidine box-1Curated6
Motifi156 – 160Histidine box-2Curated5
Motifi297 – 301Histidine box-3Curated5

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.
OrthoDBiEOG091G0B5S.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiIPR015876. Acyl-CoA_DS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti291A → S in AAA42116 (PubMed:2428815).Curated1

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 interactor.
STRINGi10116.ENSRNOP00000018447.

Chemistry databases

BindingDBiP07308.
ChEMBLiCHEMBL5424.

PTM databases

iPTMnetiP07308.
PhosphoSitePlusiP07308.

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.
OrthoDBiEOG091G0B5S.

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

BgeeiENSRNOG00000013552.
GenevisibleiP07308. RN.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiIPR015876. Acyl-CoA_DS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 146 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.