Acyl-CoA desaturase 1 - Mus musculus (Mouse)

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P13516 (ACOD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 128. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

Scd1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Stearoyl-CoA + 2 ferrocytochrome b5 + O₂ + 2 H⁺ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H₂O.
Cofactor	Iron.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.3.
Domain	The histidine box domains may contain the active site and/or be involved in metal ion binding.
Sequence similarities	Belongs to the fatty acid desaturase family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Iron
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brown fat cell differentiation Inferred from direct assay PubMed 18492766. Source: MGI cholesterol esterification Inferred from mutant phenotype PubMed 16040962. Source: MGI defense response to Gram-positive bacterium Inferred from mutant phenotype PubMed 16040962. Source: MGI fatty acid biosynthetic process Inferred from mutant phenotype PubMed 12815040. Source: MGI negative regulation of growth of symbiont in host Inferred from mutant phenotype PubMed 16040962. Source: MGI positive regulation of cholesterol esterification Traceable author statement PubMed 11090130. Source: BHF-UCL white fat cell differentiation Inferred from direct assay PubMed 18492766. Source: MGI
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	iron ion binding Inferred from electronic annotation. Source: InterPro stearoyl-CoA 9-desaturase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 355

354

Acyl-CoA desaturase 1

PRO_0000185397

Regions

Topological domain

2 – 67

Cytoplasmic Potential

Transmembrane

68 – 89

Helical; Potential

Topological domain

90 – 98

Lumenal Potential

Transmembrane

99 – 115

Helical; Potential

Topological domain

116 – 212

Cytoplasmic Potential

Transmembrane

213 – 231

Helical; Potential

Topological domain

232 – 246

Lumenal Potential

Transmembrane

247 – 269

Helical; Potential

Topological domain

270 – 355

Cytoplasmic Potential

Motif

116 – 121

Histidine box-1

Motif

153 – 157

Histidine box-2

Motif

294 – 298

Histidine box-3

Experimental info

Sequence conflict

C → A in AAA40103. Ref.1

Sequence conflict

148

E → D in AAA40103. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P13516 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: 00E2348C1898FE75
Show »

FASTA

355

41,046

        10         20         30         40         50         60 
MPAHMLQEIS SSYTTTTTIT APPSGNEREK VKTVPLHLEE DIRPEMKEDI HDPTYQDEEG 

        70         80         90        100        110        120 
PPPKLEYVWR NIILMVLLHL GGLYGIILVP SCKLYTCLFG IFYYMTSALG ITAGAHRLWS 

       130        140        150        160        170        180 
HRTYKARLPL RIFLIIANTM AFQNDVYEWA RDHRAHHKFS ETHADPHNSR RGFFFSHVGW 

       190        200        210        220        230        240 
LLVRKHPAVK EKGGKLDMSD LKAEKLVMFQ RRYYKPGLLL MCFILPTLVP WYCWGETFVN 

       250        260        270        280        290        300 
SLFVSTFLRY TLVLNATWLV NSAAHLYGYR PYDKNIQSRE NILVSLGAVG EGFHNYHHTF 

       310        320        330        340        350 
PFDYSASEYR WHINFTTFFI DCMAALGLAY DRKKVSKATV LARIKRTGDG SHKSS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M21285 , M21280, M21281, M21282, M21283, M21284 Genomic DNA. Translation: AAA40103.1. BC007474 mRNA. Translation: AAH07474.1. BC055453 mRNA. Translation: AAH55453.1.
IPI	IPI00322530.
PIR	A32115.
RefSeq	NP_033153.2. NM_009127.4.
UniGene	Mm.267377.
3D structure databases
ProteinModelPortal	P13516.
ModBase	Search...
PTM databases
PhosphoSite	P13516.
Proteomic databases
PaxDb	P13516.
PRIDE	P13516.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000041331; ENSMUSP00000036936; ENSMUSG00000037071.
GeneID	20249.
KEGG	mmu:20249.
Organism-specific databases
CTD	20249.
MGI	MGI:98239. Scd1.
Phylogenomic databases
eggNOG	COG1398.
HOGENOM	HOG000270352.
HOVERGEN	HBG003367.
InParanoid	P13516.
KO	K00507.
OMA	LEYPLAY.
OrthoDB	EOG4GQQ59.
Gene expression databases
ArrayExpress	P13516.
Bgee	P13516.
CleanEx	MM_SCD1.
Genevestigator	P13516.
GermOnline	ENSMUSG00000037071. Mus musculus.
Family and domain databases
InterPro	IPR005804. Fatty_acid_desaturase-1. IPR001522. Fatty_acid_desaturase-1_C. IPR015876. Fatty_acid_desaturase-1_core. [Graphical view]
Pfam	PF00487. FA_desaturase. 1 hit. [Graphical view]
PRINTS	PR00075. FACDDSATRASE.
PROSITE	PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P13516.
ChEMBL	CHEMBL5353.
ChiTaRS	Scd1. mouse.
NextBio	297897.
SOURCE	Search...

Entry information

Entry name

ACOD1_MOUSE

Accession

Primary (citable) accession number: P13516
Secondary accession number(s): Q922I6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	June 6, 2002
Last modified:	April 3, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents