Acyl-CoA desaturase 1 - Rattus norvegicus (Rat)

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P07308 (ACOD1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 110. History...

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

Documents (1) |

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
Synonyms:	Scd

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 Probable.
Induction	This protein is the only inducible component of this fatty acyl-CoA desaturase system.
Domain	The histidine box domains may contain the active site and/or be involved in metal ion binding.
Miscellaneous	Desaturase has a half-life of only 4 hours.
Sequence similarities	Belongs to the fatty acid desaturase family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
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	fatty acid biosynthetic process Traceable author statement. Source: RGD
Cellular component	integral to endoplasmic reticulum membrane Traceable author statement. Source: RGD microsome Inferred from direct assay. Source: RGD
Molecular function	iron ion binding Inferred from electronic annotation. Source: InterPro stearoyl-CoA 9-desaturase activity Inferred from direct assay. Source: RGD
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 – 358

357

Acyl-CoA desaturase 1

PRO_0000185400

Regions

Topological domain

2 – 70

Cytoplasmic Potential

Transmembrane

71 – 92

Helical; Potential

Topological domain

93 – 101

Lumenal Potential

Transmembrane

102 – 118

Helical; Potential

Topological domain

119 – 215

Cytoplasmic Potential

Transmembrane

216 – 234

Helical; Potential

Topological domain

235 – 249

Lumenal Potential

Transmembrane

250 – 272

Helical; Potential

Topological domain

273 – 358

Cytoplasmic Potential

Motif

119 – 124

Histidine box-1

Motif

156 – 160

Histidine box-2

Motif

297 – 301

Histidine box-3

Experimental info

Sequence conflict

291

A → S in AAA42116. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P07308 [UniParc].

Last modified November 23, 2004. Version 2.
Checksum: B4C960A969B63774
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FASTA

358

41,467

        10         20         30         40         50         60 
MPAHMLQEIS SSYTTTTTIT EPPSGNLQNG REKMKKVPLY LEEDIRPEMR EDIHDPSYQD 

        70         80         90        100        110        120 
EEGPPPKLEY VWRNIILMAL LHVGALYGIT LIPSSKVYTL LWGIFYYLIS ALGITAGAHR 

       130        140        150        160        170        180 
LWSHRTYKAR LPLRIFLIIA NTMAFQNDVY EWARDHRAHH KFSETHADPH NSRRGFFFSH 

       190        200        210        220        230        240 
VGWLLVRKHP AVKEKGGKLD MSDLKAEKLV MFQRRYYKPG LLLMCFILPT LVPWYCWGET 

       250        260        270        280        290        300 
FLHSLFVSTF LRYTLVLNAT WLVNSAAHLY GYRPYDKNIQ SRENILVSLG AVGEGFHNYH 

       310        320        330        340        350 
HAFPYDYSAS EYRWHINFTT FFIDCMAALG LAYDRKKVSK AAVLARIKRT GDGSHKSS

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References

[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: 2428815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure and regulation of rat liver microsomal stearoyl-CoA desaturase gene." Mihara K. J. Biochem. 108:1022-1029(1990) [PubMed: 1982442] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 12419843] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Brown Norway and Fischer 344.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J02585 mRNA. Translation: AAA42116.1. AF509568 mRNA. Translation: AAM34745.1. AF509569 mRNA. Translation: AAM34746.1.
IPI	IPI00206235.
PIR	A24699.
RefSeq	NP_631931.2. NM_139192.2.
UniGene	Rn.1023.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P07308.
PTM databases
PhosphoSite	P07308.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	246074.
KEGG	rno:246074.
NMPDR	fig\|10116.3.peg.4150.
UCSC	NM_139192. rat.
Organism-specific databases
CTD	20249.
RGD	621176. Scd1.
Phylogenomic databases
eggNOG	roNOG11035.
GeneTree	ENSGT00530000063158.
HOVERGEN	HBG003367.
InParanoid	P07308.
OMA	PTCKLYT.
PhylomeDB	P07308.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14123.
BRENDA	1.14.19.1. 5301.
Gene expression databases
ArrayExpress	P07308.
Genevestigator	P07308.
GermOnline	ENSRNOG00000013552. Rattus norvegicus.
Family and domain databases
InterPro	IPR005804. Fatty_acid_desaturase-1. IPR001522. Fatty_acid_desaturase-1_C. IPR015876. Fatty_acid_desaturase-1_core. [Graphical view]
KO	K00507.
Pfam	PF00487. FA_desaturase. 1 hit. [Graphical view]
PRINTS	PR00075. FACDDSATRASE.
PROSITE	PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	623356.

Entry information

Entry name

ACOD1_RAT

Accession

Primary (citable) accession number: P07308
Secondary accession number(s): Q8JZL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	November 23, 2004
Last modified:	November 16, 2011
This is version 110 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

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

Protein-protein interaction databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents