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Protein

Fatty acid desaturase 2

Gene

Fads2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleic acid (GLA) (18:3n-6) and stearidonic acid (18:4n-3) respectively and other desaturation steps. Highly unsaturated fatty acids (HUFA) play pivotal roles in many biological functions.3 Publications

Pathwayi: polyunsaturated fatty acid biosynthesis

This protein is involved in the pathway polyunsaturated fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway polyunsaturated fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

Enzyme and pathway databases

UniPathwayiUPA00658.

Chemistry databases

SwissLipidsiSLP:000000272.
SLP:000001190.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid desaturase 2 (EC:1.14.19.-)
Alternative name(s):
Delta(6) fatty acid desaturase
Short name:
D6D
Short name:
Delta(6) desaturase
Short name:
Delta-6 desaturase
Gene namesi
Name:Fads2
Synonyms:Fadsd6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68339. Fads2.

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 – 130CytoplasmicSequence analysisAdd BLAST130
Transmembranei131 – 151HelicalSequence analysisAdd BLAST21
Topological domaini152 – 157LumenalSequence analysis6
Transmembranei158 – 178HelicalSequence analysisAdd BLAST21
Topological domaini179 – 264CytoplasmicSequence analysisAdd BLAST86
Transmembranei265 – 285HelicalSequence analysisAdd BLAST21
Topological domaini286 – 305LumenalSequence analysisAdd BLAST20
Transmembranei306 – 326HelicalSequence analysisAdd BLAST21
Topological domaini327 – 444CytoplasmicSequence analysisAdd BLAST118

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5088.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003071051 – 444Fatty acid desaturase 2Add BLAST444

Proteomic databases

PaxDbiQ9Z122.
PRIDEiQ9Z122.

Expressioni

Tissue specificityi

Highest activity is found in the liver and adrenals followed by the testes and other organs, absent in adipose tissue.1 Publication

Inductioni

Inhibited by a shortage of insulin and an increase of glucagon.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027756.

Chemistry databases

BindingDBiQ9Z122.

Structurei

3D structure databases

ProteinModelPortaliQ9Z122.
SMRiQ9Z122.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 95Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST78

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi180 – 184Histidine box-15
Motifi217 – 221Histidine box-25
Motifi382 – 386Histidine box-35

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4232. Eukaryota.
ENOG410XVSZ. LUCA.
HOGENOMiHOG000012997.
HOVERGENiHBG002839.
InParanoidiQ9Z122.
KOiK10226.
OrthoDBiEOG091G0E0W.
PhylomeDBiQ9Z122.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiView protein in InterPro
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR036400. Cyt_B5-like_heme/steroid_sf.
IPR005804. FA_desaturase_dom.
IPR012171. Fatty_acid_desaturase.
PfamiView protein in Pfam
PF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
SMARTiView protein in SMART
SM01117. Cyt-b5. 1 hit.
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiView protein in PROSITE
PS50255. CYTOCHROME_B5_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Z122-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGGNQGEG STELQAPMPT FRWEEIQKHN LRTDRWLVID RKVYNVTKWS
60 70 80 90 100
QRHPGGHRVI GHYSGEDATD AFRAFHLDLD FVGKFLKPLL IGELAPEEPS
110 120 130 140 150
LDRGKSSQIT EDFRALKKTA EDMNLFKTNH LFFFLLLSHI IVMESIAWFI
160 170 180 190 200
LSYFGNGWIP TVITAFVLAT SQAQAGWLQH DYGHLSVYKK SIWNHIVHKF
210 220 230 240 250
VIGHLKGASA NWWNHRHFQH HAKPNIFHKD PDIKSLHVFV LGEWQPLEYG
260 270 280 290 300
KKKLKYLPYN HQHEYFFLIG PPLLIPMYFQ YQIIMTMIRR RDWVDLAWAI
310 320 330 340 350
SYYARFFYTY IPFYGILGAL VFLNFIRFLE SHWFVWVTQM NHIVMEIDLD
360 370 380 390 400
HYRDWFSSQL AATCNVEQSF FNDWFSGHLN FQIEHHLFPT MPRHNLHKIA
410 420 430 440
PLVKSLCAKH GIEYQEKPLL RALLDIVSSL KKSGELWLDA YLHK
Length:444
Mass (Da):52,380
Last modified:May 1, 1999 - v1
Checksum:iD9AE0C7AE499A1AE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti101L → M in AEX15918 (PubMed:22216341).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021980 mRNA. Translation: BAA75496.1.
HQ909027 mRNA. Translation: AEX15918.1.
BC081776 mRNA. Translation: AAH81776.1.
PIRiJG0180.
RefSeqiNP_112634.1. NM_031344.2.
UniGeneiRn.162483.

Genome annotation databases

GeneIDi83512.
KEGGirno:83512.

Similar proteinsi

Entry informationi

Entry nameiFADS2_RAT
AccessioniPrimary (citable) accession number: Q9Z122
Secondary accession number(s): H2BF31
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 1, 1999
Last modified: November 22, 2017
This is version 121 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families