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Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 3 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)DescriptionActionsGraphical viewLength
Binding sitei70SubstrateBy similarity1
Metal bindingi115Iron 1By similarity1
Metal bindingi120Iron 1By similarity1
Binding sitei143SubstrateBy similarity1
Binding sitei150SubstrateBy similarity1
Binding sitei151SubstrateBy similarity1
Metal bindingi152Iron 1By similarity1
Metal bindingi155Iron 2By similarity1
Metal bindingi156Iron 1By similarity1
Binding sitei183SubstrateBy similarity1
Binding sitei184SubstrateBy similarity1
Binding sitei257SubstrateBy similarity1
Metal bindingi264Iron 2By similarity1
Metal bindingi293Iron 2By similarity1
Metal bindingi296Iron 1By similarity1
Metal bindingi297Iron 2By similarity1

GO - Molecular functioni

GO - Biological processi

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. 3239.

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 desaturase
Gene namesi
Name:SCD
Synonyms:FAR-17c
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 67CytoplasmicBy similarityAdd BLAST67
Transmembranei68 – 88HelicalBy similarityAdd BLAST21
Topological domaini89 – 92LumenalBy similarity4
Transmembranei93 – 113HelicalBy similarityAdd BLAST21
Topological domaini114 – 212CytoplasmicBy similarityAdd BLAST99
Transmembranei213 – 232HelicalBy similarityAdd BLAST20
Topological domaini233 – 236LumenalBy similarity4
Transmembranei237 – 258HelicalBy similarityAdd BLAST22
Topological domaini259 – 354CytoplasmicBy similarityAdd BLAST96

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001853961 – 354Acyl-CoA desaturaseAdd BLAST354

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei198PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi115 – 120Histidine box-1Curated6
Motifi152 – 156Histidine box-2Curated5
Motifi293 – 297Histidine 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

HOVERGENiHBG003367.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiIPR015876. Acyl-CoA_DS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q64420-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGHLLQEEM TSSYTTTTTT ITEPPSESLQ KTVPLYLEED IRPEMKEDIY
60 70 80 90 100
DPSYQDEEGP PPKLEYVWRN IILMALLHLG ALYGLVLVPS SKVYTLLWAF
110 120 130 140 150
VYYVISIEGI GAGVHRLWSH RTYKARLPLR IFLIIANTMA FQNDVYEWAR
160 170 180 190 200
DHRAHHKFSE TYADPHDSRR GFFFSHVGWL LVRKHPAVKE KGGKLDMSDL
210 220 230 240 250
KAEKLVMFQR RYYKPAILLM CFILPTFVPW YFWGEAFVNS LCVSTFLRYT
260 270 280 290 300
LVLNATWLVN SAAHLYGYRP YDKNIDPREN ALVSLGCLGE GFHNYHHAFP
310 320 330 340 350
YDYSASEYRW HINFTTFFID CMAALGLAYD RKKVSKAAVL ARIKRTGDGS

CKSG
Length:354
Mass (Da):40,968
Last modified:November 1, 1996 - v1
Checksum:iB41A0831845EB874
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26956 mRNA. Translation: AAC42058.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26956 mRNA. Translation: AAC42058.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG003367.

Enzyme and pathway databases

BRENDAi1.14.19.1. 3239.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiIPR015876. Acyl-CoA_DS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACOD_MESAU
AccessioniPrimary (citable) accession number: Q64420
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.