Reviewed, UniProtKB/Swiss-Prot P07308 (ACOD1_RAT)

Names and origin

Protein names

Recommended name:
    Acyl-CoA desaturase 1
    EC=1.14.19.1
Alternative name(s):
    Stearoyl-CoA desaturase 1
    Fatty acid desaturase 1
    Delta(9)-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 not processed.
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
Ligand	Iron
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Traceable author statement. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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: UniProtKB-KW stearoyl-CoA 9-desaturase activity Ref.3 Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 358	358	Acyl-CoA desaturase 1		PRO_0000185400
Regions
	Transmembrane	75 – 95	21	Potential
	Transmembrane	97 – 117	21	Potential
	Transmembrane	221 – 241	21	Potential
	Transmembrane	314 – 334	21	Potential
	Motif	119 – 124	6	Histidine box-1
	Motif	156 – 160	5	Histidine box-2
	Motif	297 – 301	5	Histidine box-3
Experimental info
	Sequence conflict	291	1	A → S in AAA42116. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P07308-1 [UniParc]. Last modified November 23, 2004. Version 2. Checksum: B4C960A969B63774	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

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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J02585 mRNA. Translation: AAA42116.1. AF509568 mRNA. Translation: AAM34745.1. AF509569 mRNA. Translation: AAM34746.1.
IPI	IPI00206235.
PIR	A24699.
RefSeq	NP_631931.2.
UniGene	Rn.1023
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P07308.
Genome annotation databases
Ensembl	ENSRNOG00000013552. Rattus norvegicus. [Contig view]
GeneID	246074.
KEGG	rno:246074.
NMPDR	fig|10116.3.peg.4150.
Organism-specific databases
RGD	621176. Scd1.
Phylogenomic databases
HOVERGEN	P07308.
OMA	P07308. VFYYFVS.
Enzyme and pathway databases
BRENDA	1.14.19.1. 248.
Gene expression databases
ArrayExpress	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]
Pfam	PF00487. FA_desaturase. 1 hit. [Graphical view]
PRINTS	PR00075. FACDDSATRASE.
ProDom	PD002221. Desaturase. 1 hit. PD001081. FA_desat_sub. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)