Acyl-CoA desaturase - Bos taurus (Bovine)

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Q9TT94 (ACOD_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 92. 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
EC=1.14.19.1

Alternative name(s):
Delta(9)-desaturase
Short name=Delta-9 desaturase
Fatty acid desaturase
Stearoyl-CoA desaturase

Gene names

Name:

SCD

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
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 By similarity.
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.
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
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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

Chain

1 – 359

359

Acyl-CoA desaturase

PRO_0000185394

Regions

Topological domain

1 – 71

Cytoplasmic Potential

Transmembrane

72 – 93

Helical; Potential

Topological domain

94 – 102

Lumenal Potential

Transmembrane

103 – 119

Helical; Potential

Topological domain

120 – 216

Cytoplasmic Potential

Transmembrane

217 – 235

Helical; Potential

Topological domain

236 – 250

Lumenal Potential

Transmembrane

251 – 273

Helical; Potential

Topological domain

274 – 359

Cytoplasmic Potential

Motif

120 – 125

Histidine box-1

Motif

157 – 161

Histidine box-2

Motif

298 – 302

Histidine box-3

Amino acid modifications

Modified residue

203

Phosphoserine By similarity

Experimental info

Sequence conflict

L → M in AAF22305. Ref.1

Sequence conflict

293

A → V in AAF22305. Ref.1

Sequence conflict

293

A → V in AAL99940. Ref.2

Sequence conflict

356

Y → H in AAF22305. Ref.1

Sequence conflict

359

G → S in AAF22305. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9TT94 [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: C7C9E9FA3A8FD205
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FASTA

359

41,705

        10         20         30         40         50         60 
MPAHLLQEEI SSSYTTTTTI TAPPSRVLQN GGGKLEKTPL YLEEDIRPEM RDDIYDPTYQ 

        70         80         90        100        110        120 
DKEGPKPKLE YVWRNIILMS LLHLGALYGI TLIPTCKIYT YIWVLFYYLM GALGITAGAH 

       130        140        150        160        170        180 
RLWSHRTYKA RLPLRVFLII GNTMAFQNDV FEWSRDHRAH HKFSETDADP HNSRRGFFFS 

       190        200        210        220        230        240 
HVGWLLVRKH PAVKEKGSTL NLSDLRAEKL VMFQRRYYKP GVLLLCFILP TLVPWYLWDE 

       250        260        270        280        290        300 
TFQNSLFFAT LFRYALGLNV TWLVNSAAHM YGYRPYDKTI NPRENILVSL GAAGEGFHNY 

       310        320        330        340        350 
HHTFPYDYSA SEYRWHINFT TFFIDCMAAI GLAYDRKKVS KAAILARIKR TGEESYKSG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of bovine stearoyl CoA desaturasel cDNA from adipose tissues." Chung M.I., Ha S.H., Jeong S., Bok J., Cho K., Baik M.G., Choi Y.J. Biosci. Biotechnol. Biochem. 64:1526-1530(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adipose tissue.
[2]	"Bovine stearoyl-CoA desaturase gene structure and large scale SNP analysis." Glimm D., Dong F., Kennelly J. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Genomic structure and expression of the bovine stearoyl-CoA desaturase gene." Medrano J.F., Islas-Trejo A.D., Johnson A.M., DePeters E.J. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]	NIH - Mammalian Gene Collection (MGC) project Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Hypothalamus.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF188710 mRNA. Translation: AAF22305.1. AF481919 , AF481915, AF481916, AF481917, AF481918 Genomic DNA. Translation: AAL99940.1. AY241932 Genomic DNA. Translation: AAO63569.1. AY241933 mRNA. Translation: AAO63570.1. BC112700 mRNA. Translation: AAI12701.1.
IPI	IPI00711960.
PIR	PC7092.
RefSeq	NP_776384.3. NM_173959.4.
UniGene	Bt.65021.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	280924.
KEGG	bta:280924.
Organism-specific databases
CTD	6319.
Phylogenomic databases
HOVERGEN	HBG003367.
KO	K00507.
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
NextBio	20805045.

Entry information

Entry name

ACOD_BOVIN

Accession

Primary (citable) accession number: Q9TT94
Secondary accession number(s): Q861R6, Q8SQ76

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	June 27, 2006
Last modified:	April 3, 2013
This is version 92 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

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents