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Protein

Acyl-CoA desaturase 1

Gene

Scd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O2 and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA.

Catalytic activityi

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

Cofactori

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. stearoyl-CoA 9-desaturase activity Source: UniProtKB-EC

GO - Biological processi

  1. brown fat cell differentiation Source: MGI
  2. cholesterol esterification Source: MGI
  3. defense response to Gram-positive bacterium Source: MGI
  4. fatty acid biosynthetic process Source: MGI
  5. negative regulation of growth of symbiont in host Source: MGI
  6. positive regulation of cholesterol esterification Source: BHF-UCL
  7. white fat cell differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

Iron

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase 1 (EC:1.14.19.1)
Alternative name(s):
Delta(9)-desaturase 1
Short name:
Delta-9 desaturase 1
Fatty acid desaturase 1
Stearoyl-CoA desaturase 1
Gene namesi
Name:Scd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:98239. Scd1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6767CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei68 – 8922HelicalSequence AnalysisAdd
BLAST
Topological domaini90 – 989LumenalSequence Analysis
Transmembranei99 – 11517HelicalSequence AnalysisAdd
BLAST
Topological domaini116 – 21297CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei213 – 23119HelicalSequence AnalysisAdd
BLAST
Topological domaini232 – 24615LumenalSequence AnalysisAdd
BLAST
Transmembranei247 – 26923HelicalSequence AnalysisAdd
BLAST
Topological domaini270 – 35586CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. integral component of endoplasmic reticulum membrane Source: WormBase
  3. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355Acyl-CoA desaturase 1PRO_0000185397Add
BLAST

Proteomic databases

MaxQBiP13516.
PaxDbiP13516.
PRIDEiP13516.

PTM databases

PhosphoSiteiP13516.

Expressioni

Gene expression databases

BgeeiP13516.
CleanExiMM_SCD1.
ExpressionAtlasiP13516. baseline and differential.
GenevestigatoriP13516.

Interactioni

Protein-protein interaction databases

MINTiMINT-4996454.

Structurei

3D structure databases

ProteinModelPortaliP13516.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi116 – 1216Histidine box-1
Motifi153 – 1575Histidine box-2
Motifi294 – 2985Histidine box-3

Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similaritiesi

Belongs to the fatty acid desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1398.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiP13516.
KOiK00507.
OMAiWNESLLC.
OrthoDBiEOG7ZPNKS.
PhylomeDBiP13516.
TreeFamiTF313251.

Family and domain databases

InterProiIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13516-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPAHMLQEIS SSYTTTTTIT APPSGNEREK VKTVPLHLEE DIRPEMKEDI
60 70 80 90 100
HDPTYQDEEG PPPKLEYVWR NIILMVLLHL GGLYGIILVP SCKLYTCLFG
110 120 130 140 150
IFYYMTSALG ITAGAHRLWS HRTYKARLPL RIFLIIANTM AFQNDVYEWA
160 170 180 190 200
RDHRAHHKFS ETHADPHNSR RGFFFSHVGW LLVRKHPAVK EKGGKLDMSD
210 220 230 240 250
LKAEKLVMFQ RRYYKPGLLL MCFILPTLVP WYCWGETFVN SLFVSTFLRY
260 270 280 290 300
TLVLNATWLV NSAAHLYGYR PYDKNIQSRE NILVSLGAVG EGFHNYHHTF
310 320 330 340 350
PFDYSASEYR WHINFTTFFI DCMAALGLAY DRKKVSKATV LARIKRTGDG

SHKSS
Length:355
Mass (Da):41,046
Last modified:June 6, 2002 - v2
Checksum:i00E2348C1898FE75
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971C → A in AAA40103. (PubMed:2903162)Curated
Sequence conflicti148 – 1481E → D in AAA40103. (PubMed:2903162)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21285
, M21280, M21281, M21282, M21283, M21284 Genomic DNA. Translation: AAA40103.1.
BC007474 mRNA. Translation: AAH07474.1.
BC055453 mRNA. Translation: AAH55453.1.
CCDSiCCDS29850.1.
PIRiA32115.
RefSeqiNP_033153.2. NM_009127.4.
UniGeneiMm.267377.

Genome annotation databases

EnsembliENSMUST00000041331; ENSMUSP00000036936; ENSMUSG00000037071.
GeneIDi20249.
KEGGimmu:20249.
UCSCiuc008hpr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21285
, M21280, M21281, M21282, M21283, M21284 Genomic DNA. Translation: AAA40103.1.
BC007474 mRNA. Translation: AAH07474.1.
BC055453 mRNA. Translation: AAH55453.1.
CCDSiCCDS29850.1.
PIRiA32115.
RefSeqiNP_033153.2. NM_009127.4.
UniGeneiMm.267377.

3D structure databases

ProteinModelPortaliP13516.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4996454.

Chemistry

BindingDBiP13516.
ChEMBLiCHEMBL5353.

PTM databases

PhosphoSiteiP13516.

Proteomic databases

MaxQBiP13516.
PaxDbiP13516.
PRIDEiP13516.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041331; ENSMUSP00000036936; ENSMUSG00000037071.
GeneIDi20249.
KEGGimmu:20249.
UCSCiuc008hpr.2. mouse.

Organism-specific databases

CTDi20249.
MGIiMGI:98239. Scd1.

Phylogenomic databases

eggNOGiCOG1398.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiP13516.
KOiK00507.
OMAiWNESLLC.
OrthoDBiEOG7ZPNKS.
PhylomeDBiP13516.
TreeFamiTF313251.

Miscellaneous databases

ChiTaRSiScd1. mouse.
NextBioi297897.
PROiP13516.
SOURCEiSearch...

Gene expression databases

BgeeiP13516.
CleanExiMM_SCD1.
ExpressionAtlasiP13516. baseline and differential.
GenevestigatoriP13516.

Family and domain databases

InterProiIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Differentiation-induced gene expression in 3T3-L1 preadipocytes. Characterization of a differentially expressed gene encoding stearoyl-CoA desaturase."
    Ntambi J.M., Buhrow S.A., Kaestner K.H., Christy R.J., Sibley E., Kelly T.J. Jr., Lane M.D.
    J. Biol. Chem. 263:17291-17300(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Adipocyte.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  3. "Membrane topology of mouse stearoyl-CoA desaturase 1."
    Man W.C., Miyazaki M., Chu K., Ntambi J.M.
    J. Biol. Chem. 281:1251-1260(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.

Entry informationi

Entry nameiACOD1_MOUSE
AccessioniPrimary (citable) accession number: P13516
Secondary accession number(s): Q922I6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 6, 2002
Last modified: February 4, 2015
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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.