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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701SubstrateBy similarity
Metal bindingi115 – 1151Iron 1By similarity
Metal bindingi120 – 1201Iron 1By similarity
Binding sitei143 – 1431SubstrateBy similarity
Binding sitei150 – 1501SubstrateBy similarity
Binding sitei151 – 1511SubstrateBy similarity
Metal bindingi152 – 1521Iron 1By similarity
Metal bindingi155 – 1551Iron 2By similarity
Metal bindingi156 – 1561Iron 1By similarity
Binding sitei183 – 1831SubstrateBy similarity
Binding sitei184 – 1841SubstrateBy similarity
Binding sitei257 – 2571SubstrateBy similarity
Metal bindingi264 – 2641Iron 2By similarity
Metal bindingi293 – 2931Iron 2By similarity
Metal bindingi296 – 2961Iron 1By similarity
Metal bindingi297 – 2971Iron 2By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6767CytoplasmicBy similarityAdd
BLAST
Transmembranei68 – 8821HelicalBy similarityAdd
BLAST
Topological domaini89 – 924LumenalBy similarity
Transmembranei93 – 11321HelicalBy similarityAdd
BLAST
Topological domaini114 – 21299CytoplasmicBy similarityAdd
BLAST
Transmembranei213 – 23220HelicalBy similarityAdd
BLAST
Topological domaini233 – 2364LumenalBy similarity
Transmembranei237 – 25822HelicalBy similarityAdd
BLAST
Topological domaini259 – 35496CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Acyl-CoA desaturasePRO_0000185396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi115 – 1206Histidine box-1Curated
Motifi152 – 1565Histidine box-2Curated
Motifi293 – 2975Histidine 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

HOVERGENiHBG003367.

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.

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

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

  1. "Sequence analysis and characterization of FAR-17c, an androgen-dependent gene in the flank organs of hamsters."
    Ideta R., Seki T., Adachi K.
    J. Dermatol. Sci. 9:94-102(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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: March 16, 2016
This is version 90 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.