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Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei75SubstrateBy similarity1
Metal bindingi120Iron 1By similarity1
Metal bindingi125Iron 1By similarity1
Binding sitei148SubstrateBy similarity1
Binding sitei155SubstrateBy similarity1
Binding sitei156SubstrateBy similarity1
Metal bindingi157Iron 1By similarity1
Metal bindingi160Iron 2By similarity1
Metal bindingi161Iron 1By similarity1
Binding sitei188SubstrateBy similarity1
Binding sitei189SubstrateBy similarity1
Binding sitei262SubstrateBy similarity1
Metal bindingi269Iron 2By similarity1
Metal bindingi298Iron 2By similarity1
Metal bindingi301Iron 1By similarity1
Metal bindingi302Iron 2By similarity1

GO - Molecular functioni

  • iron ion binding Source: UniProtKB
  • oxidoreductase activity Source: UniProtKB
  • stearoyl-CoA 9-desaturase activity Source: AgBase

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandIron, 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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 72CytoplasmicBy similarityAdd BLAST72
Transmembranei73 – 93HelicalBy similarityAdd BLAST21
Topological domaini94 – 97LumenalBy similarity4
Transmembranei98 – 118HelicalBy similarityAdd BLAST21
Topological domaini119 – 217CytoplasmicBy similarityAdd BLAST99
Transmembranei218 – 237HelicalBy similarityAdd BLAST20
Topological domaini238 – 241LumenalBy similarity4
Transmembranei242 – 263HelicalBy similarityAdd BLAST22
Topological domaini264 – 359CytoplasmicBy similarityAdd BLAST96

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001853941 – 359Acyl-CoA desaturaseAdd BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei198PhosphoserineBy similarity1
Modified residuei203PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9TT94
PRIDEiQ9TT94

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000056263

Structurei

3D structure databases

SMRiQ9TT94
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi120 – 125Histidine box-1Curated6
Motifi157 – 161Histidine box-2Curated5
Motifi298 – 302Histidine box-3Curated5

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

CDDicd03505 Delta9-FADS-like, 1 hit
InterProiView protein in InterPro
IPR015876 Acyl-CoA_DS
IPR005804 FA_desaturase_dom
IPR001522 FADS-1_CS
PANTHERiPTHR11351 PTHR11351, 1 hit
PfamiView protein in Pfam
PF00487 FA_desaturase, 1 hit
PRINTSiPR00075 FACDDSATRASE
PROSITEiView protein in PROSITE
PS00476 FATTY_ACID_DESATUR_1, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.iShow all

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3N2Z2G3N2Z2_BOVIN
Acyl-CoA desaturase
SCD
256Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5L → M in AAF22305 (PubMed:10945276).Curated1
Sequence conflicti293A → V in AAF22305 (PubMed:10945276).Curated1
Sequence conflicti293A → V in AAL99940 (Ref. 2) Curated1
Sequence conflicti356Y → H in AAF22305 (PubMed:10945276).Curated1
Sequence conflicti359G → S in AAF22305 (PubMed:10945276).Curated1

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

Similar proteinsi

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

SMRiQ9TT94
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000056263

Proteomic databases

PaxDbiQ9TT94
PRIDEiQ9TT94

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

Family and domain databases

CDDicd03505 Delta9-FADS-like, 1 hit
InterProiView protein in InterPro
IPR015876 Acyl-CoA_DS
IPR005804 FA_desaturase_dom
IPR001522 FADS-1_CS
PANTHERiPTHR11351 PTHR11351, 1 hit
PfamiView protein in Pfam
PF00487 FA_desaturase, 1 hit
PRINTSiPR00075 FACDDSATRASE
PROSITEiView protein in PROSITE
PS00476 FATTY_ACID_DESATUR_1, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiACOD_BOVIN
AccessioniPrimary (citable) accession number: Q9TT94
Secondary accession number(s): Q861R6, Q8SQ76
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 27, 2006
Last modified: August 30, 2017
This is version 119 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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