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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

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 activityi

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

Cofactori

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. stearoyl-CoA 9-desaturase activity Source: UniProtKB-EC

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

Iron

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase (EC:1.14.19.1)
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 – 6666CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei67 – 8822HelicalSequence AnalysisAdd
BLAST
Topological domaini89 – 979LumenalSequence Analysis
Transmembranei98 – 11417HelicalSequence AnalysisAdd
BLAST
Topological domaini115 – 21197CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei212 – 23019HelicalSequence AnalysisAdd
BLAST
Topological domaini231 – 24515LumenalSequence AnalysisAdd
BLAST
Transmembranei246 – 26823HelicalSequence AnalysisAdd
BLAST
Topological domaini269 – 35486CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
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-1
Motifi152 – 1565Histidine box-2
Motifi293 – 2975Histidine box-3

Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similaritiesi

Belongs to the fatty acid desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG003367.

Family and domain databases

InterProiIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[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.

Family and domain databases

InterProiIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[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 4, 2015
This is version 85 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

External Data

Dasty 3

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 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.