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Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Stearyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (By similarity). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity).By similarity

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.By similarity

Cofactori

Fe2+By similarityNote: Expected to bind 2 Fe2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei75 – 751SubstrateBy similarity
Metal bindingi120 – 1201Iron 1By similarity
Metal bindingi125 – 1251Iron 1By similarity
Binding sitei148 – 1481SubstrateBy similarity
Binding sitei155 – 1551SubstrateBy similarity
Binding sitei156 – 1561SubstrateBy similarity
Metal bindingi157 – 1571Iron 1By similarity
Metal bindingi160 – 1601Iron 2By similarity
Metal bindingi161 – 1611Iron 1By similarity
Binding sitei188 – 1881SubstrateBy similarity
Binding sitei189 – 1891SubstrateBy similarity
Binding sitei262 – 2621SubstrateBy similarity
Metal bindingi269 – 2691Iron 2By similarity
Metal bindingi298 – 2981Iron 2By similarity
Metal bindingi301 – 3011Iron 1By similarity
Metal bindingi302 – 3021Iron 2By similarity

GO - Molecular functioni

GO - Biological processi

  • response to fatty acid Source: AgBase
  • unsaturated fatty acid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.19.1. 908.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase (EC:1.14.19.1By similarity)
Alternative name(s):
Delta(9)-desaturase
Short name:
Delta-9 desaturase
Fatty acid desaturase
Stearoyl-CoA desaturase1 PublicationCurated
Gene namesi
Name:SCD
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7272CytoplasmicBy similarityAdd
BLAST
Transmembranei73 – 9321HelicalBy similarityAdd
BLAST
Topological domaini94 – 974LumenalBy similarity
Transmembranei98 – 11821HelicalBy similarityAdd
BLAST
Topological domaini119 – 21799CytoplasmicBy similarityAdd
BLAST
Transmembranei218 – 23720HelicalBy similarityAdd
BLAST
Topological domaini238 – 2414LumenalBy similarity
Transmembranei242 – 26322HelicalBy similarityAdd
BLAST
Topological domaini264 – 35996CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • cell Source: AgBase
  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Acyl-CoA desaturasePRO_0000185394Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9TT94.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000056263.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi120 – 1256Histidine box-1Curated
Motifi157 – 1615Histidine box-2Curated
Motifi298 – 3025Histidine box-3Curated

Domaini

The histidine box domains are involved in binding the catalytic metal ions.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
HOVERGENiHBG003367.
InParanoidiQ9TT94.
KOiK00507.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9TT94-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAHLLQEEI SSSYTTTTTI TAPPSRVLQN GGGKLEKTPL YLEEDIRPEM
60 70 80 90 100
RDDIYDPTYQ DKEGPKPKLE YVWRNIILMS LLHLGALYGI TLIPTCKIYT
110 120 130 140 150
YIWVLFYYLM GALGITAGAH RLWSHRTYKA RLPLRVFLII GNTMAFQNDV
160 170 180 190 200
FEWSRDHRAH HKFSETDADP HNSRRGFFFS HVGWLLVRKH PAVKEKGSTL
210 220 230 240 250
NLSDLRAEKL VMFQRRYYKP GVLLLCFILP TLVPWYLWDE TFQNSLFFAT
260 270 280 290 300
LFRYALGLNV TWLVNSAAHM YGYRPYDKTI NPRENILVSL GAAGEGFHNY
310 320 330 340 350
HHTFPYDYSA SEYRWHINFT TFFIDCMAAI GLAYDRKKVS KAAILARIKR

TGEESYKSG
Length:359
Mass (Da):41,705
Last modified:June 27, 2006 - v2
Checksum:iC7C9E9FA3A8FD205
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51L → M in AAF22305 (PubMed:10945276).Curated
Sequence conflicti293 – 2931A → V in AAF22305 (PubMed:10945276).Curated
Sequence conflicti293 – 2931A → V in AAL99940 (Ref. 2) Curated
Sequence conflicti356 – 3561Y → H in AAF22305 (PubMed:10945276).Curated
Sequence conflicti359 – 3591G → S in AAF22305 (PubMed:10945276).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiPC7092.
RefSeqiNP_776384.3. NM_173959.4.
UniGeneiBt.65021.

Genome annotation databases

GeneIDi280924.
KEGGibta:280924.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiPC7092.
RefSeqiNP_776384.3. NM_173959.4.
UniGeneiBt.65021.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000056263.

Proteomic databases

PaxDbiQ9TT94.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280924.
KEGGibta:280924.

Organism-specific databases

CTDi6319.

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
HOVERGENiHBG003367.
InParanoidiQ9TT94.
KOiK00507.

Enzyme and pathway databases

BRENDAi1.14.19.1. 908.

Miscellaneous databases

NextBioi20805045.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of bovine stearoyl CoA desaturase l 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.

Entry informationi

Entry nameiACOD_BOVIN
AccessioniPrimary (citable) accession number: Q9TT94
Secondary accession number(s): Q861R6, Q8SQ76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 27, 2006
Last modified: April 13, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.