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Protein

Fatty acid desaturase 1

Gene

Fads1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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 desaturation of dihomo-gamma-linoleic acid (DHGLA) (20:3n-6) and eicosatetraenoic acid (20:4n-3) to generate arachidonic acid (AA) (20:4n-6) and eicosapentaenoic acid (EPA)(20:5n-3) respectively (By similarity).By similarity

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

  • aging Source: RGD
  • arachidonic acid metabolic process Source: RGD
  • response to insulin Source: RGD
  • response to isolation stress Source: RGD
  • response to nutrient Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organic substance Source: RGD
  • response to sucrose Source: RGD
  • response to vitamin A Source: RGD
  • unsaturated fatty acid biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

Enzyme and pathway databases

ReactomeiR-RNO-2046105. Linoleic acid (LA) metabolism.
R-RNO-2046106. alpha-linolenic acid (ALA) metabolism.
UniPathwayiUPA00658.

Chemistry

SwissLipidsiSLP:000001191.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid desaturase 1 (EC:1.14.19.-)
Alternative name(s):
Delta(5) fatty acid desaturase
Short name:
D5D
Short name:
Delta(5) desaturase
Short name:
Delta-5 desaturase
Gene namesi
Name:Fads1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi621678. Fads1.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Mitochondrion By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 132132CytoplasmicSequence analysisAdd
BLAST
Transmembranei133 – 15321HelicalSequence analysisAdd
BLAST
Topological domaini154 – 1618LumenalSequence analysis
Transmembranei162 – 18019HelicalSequence analysisAdd
BLAST
Topological domaini181 – 26888CytoplasmicSequence analysisAdd
BLAST
Transmembranei269 – 28921HelicalSequence analysisAdd
BLAST
Topological domaini290 – 30819LumenalSequence analysisAdd
BLAST
Transmembranei309 – 32921HelicalSequence analysisAdd
BLAST
Topological domaini330 – 447118CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: RGD
  • mitochondrion Source: UniProtKB-SubCell
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5727.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Fatty acid desaturase 1PRO_0000307099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ920R3.
PRIDEiQ920R3.

PTM databases

PhosphoSiteiQ920R3.

Expressioni

Tissue specificityi

Highly abundant in adrenal gland and mammary tissue and moderately in liver, kidney, lung, spleen, thymus, brain, and eye.1 Publication

Inductioni

Regulated by dietary vitamin A and exogenous retinoic acid in liver.1 Publication

Gene expression databases

GenevisibleiQ920R3. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027834.

Chemistry

BindingDBiQ920R3.

Structurei

3D structure databases

ProteinModelPortaliQ920R3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 9779Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi182 – 1865Histidine box-1
Motifi219 – 2235Histidine box-2
Motifi385 – 3895Histidine box-3

Domaini

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

Sequence similaritiesi

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4232. Eukaryota.
ENOG410XVSZ. LUCA.
GeneTreeiENSGT00510000046574.
HOGENOMiHOG000012997.
HOVERGENiHBG002839.
InParanoidiQ920R3.
KOiK10224.
OMAiFMVRFLE.
OrthoDBiEOG7G1V6P.
PhylomeDBiQ920R3.
TreeFamiTF313604.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR012171. Fatty_acid_desaturase.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q920R3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPDPVQTPD PASAQLRQMR YFTWEEVAQR SGREKERWLV IDRKVYNISD
60 70 80 90 100
FSRRHPGGSR VISHYAGQDA TDPFVAFHIN KGLVRKYMNS LLIGELAPEQ
110 120 130 140 150
PSFEPTKNKA LTDEFRELRA TVERMGLMKA NHLFFLFYLL HILLLDVAAW
160 170 180 190 200
LTLWIFGTSL VPFTLCAVLL STVQAQAGWL QHDFGHLSVF STSTWNHLVH
210 220 230 240 250
HFVIGHLKGA PASWWNHMHF QHHAKPNCFR KDPDINMHPL FFALGKVLSV
260 270 280 290 300
ELGKEKKKHM PYNHQHKYFF LIGPPALLPL YFQWYIFYFV VQRKKWVDLA
310 320 330 340 350
WMLSFYVRVF FTYMPLLGLK GLLCLFFIVR FLESNWFVWV TQMNHIPMHI
360 370 380 390 400
DHDRNVDWVS TQLQATCNVH QSAFNNWFSG HLNFQIEHHL FPTMPRHNYH
410 420 430 440
KVAPLVQSLC AKYGIKYESK PLLTAFADIV YSLKESGQLW LDAYLHQ
Length:447
Mass (Da):52,482
Last modified:December 1, 2001 - v1
Checksum:i764D7D7C9AA3F7BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731P → R in AAG35068 (PubMed:11414679).Curated
Sequence conflicti85 – 851R → E in AAG35068 (PubMed:11414679).Curated
Sequence conflicti101 – 1011P → S in AAG35068 (PubMed:11414679).Curated
Sequence conflicti391 – 3911F → L in AAG35068 (PubMed:11414679).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320509 mRNA. Translation: AAG35068.1.
AB052085 mRNA. Translation: BAB69054.1.
RefSeqiNP_445897.2. NM_053445.2.
UniGeneiRn.28161.

Genome annotation databases

EnsembliENSRNOT00000027834; ENSRNOP00000027834; ENSRNOG00000020480.
GeneIDi84575.
KEGGirno:84575.
UCSCiRGD:621678. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320509 mRNA. Translation: AAG35068.1.
AB052085 mRNA. Translation: BAB69054.1.
RefSeqiNP_445897.2. NM_053445.2.
UniGeneiRn.28161.

3D structure databases

ProteinModelPortaliQ920R3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027834.

Chemistry

BindingDBiQ920R3.
ChEMBLiCHEMBL5727.
SwissLipidsiSLP:000001191.

PTM databases

PhosphoSiteiQ920R3.

Proteomic databases

PaxDbiQ920R3.
PRIDEiQ920R3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027834; ENSRNOP00000027834; ENSRNOG00000020480.
GeneIDi84575.
KEGGirno:84575.
UCSCiRGD:621678. rat.

Organism-specific databases

CTDi3992.
RGDi621678. Fads1.

Phylogenomic databases

eggNOGiKOG4232. Eukaryota.
ENOG410XVSZ. LUCA.
GeneTreeiENSGT00510000046574.
HOGENOMiHOG000012997.
HOVERGENiHBG002839.
InParanoidiQ920R3.
KOiK10224.
OMAiFMVRFLE.
OrthoDBiEOG7G1V6P.
PhylomeDBiQ920R3.
TreeFamiTF313604.

Enzyme and pathway databases

UniPathwayiUPA00658.
ReactomeiR-RNO-2046105. Linoleic acid (LA) metabolism.
R-RNO-2046106. alpha-linolenic acid (ALA) metabolism.

Miscellaneous databases

PROiQ920R3.

Gene expression databases

GenevisibleiQ920R3. RN.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR012171. Fatty_acid_desaturase.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Fatty acid Delta(5)-desaturase mRNA is regulated by dietary vitamin A and exogenous retinoic acid in liver of adult rats."
    Zolfaghari R., Cifelli C.J., Banta M.D., Ross A.C.
    Arch. Biochem. Biophys. 391:8-15(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: Lewis.
    Tissue: Liver.
  2. "Cloning and expression of rat liver delta-5 fatty acid desaturase."
    Inagaki K., Aki T., Shimada Y., Kawamoto S., Shigeta S., Ono K., Suzuki O.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.

Entry informationi

Entry nameiFADS1_RAT
AccessioniPrimary (citable) accession number: Q920R3
Secondary accession number(s): Q9EPV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 102 of the entry and version 1 of the sequence. [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

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.