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Reviewed, UniProtKB/Swiss-Prot Q9TT94 (ACOD_BOVIN)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Acyl-CoA desaturase
    EC=1.14.19.1
Alternative name(s):
    Stearoyl-CoA desaturase
    Fatty acid desaturase
    Delta(9)-desaturase
Gene names
Name: SCD
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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.

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Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   LigandIron
   Molecular functionOxidoreductase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

stearoyl-CoA 9-desaturase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Acyl-CoA desaturase
PRO_0000185394

Regions

Transmembrane76 – 9621 Potential
Transmembrane98 – 11821 Potential
Transmembrane223 – 24321 Potential
Transmembrane315 – 33521 Potential
Motif120 – 1256Histidine box-1
Motif157 – 1615Histidine box-2
Motif298 – 3025Histidine box-3

Amino acid modifications

Modified residue1981Phosphoserine By similarity
Modified residue1991Phosphothreonine By similarity
Modified residue2031Phosphoserine By similarity

Experimental info

Sequence conflict51L → M in AAF22305. Ref.1
Sequence conflict2931A → V in AAF22305. Ref.1
Sequence conflict2931A → V in AAL99940. Ref.2
Sequence conflict3561Y → H in AAF22305. Ref.1
Sequence conflict3591G → S in AAF22305. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q9TT94-1 [UniParc].

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

FASTA35941,705
        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

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References

« Hide '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: 10945276] [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.

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Cross-references

Sequence databases

AF188710 mRNA. Translation: AAF22305.1.
AF481919 expand/collapse EMBL AC list , 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.
IPIIPI00711960.
PIRPC7092.
RefSeqNP_776384.3.
UniGeneBt.89685
Bt.97115

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID280924.
KEGGbta:280924.

Phylogenomic databases

HOVERGENQ9TT94.

Enzyme and pathway databases

BRENDA1.14.19.1. 251.

Family and domain databases

InterProIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSPR00075. FACDDSATRASE.
ProDomPD002221. Desaturase. 1 hit.
PD001081. FA_desat_sub. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameACOD_BOVIN
AccessionPrimary (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: June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents