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Protein

Fatty acid desaturase 1

Gene

Fads1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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

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

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1923517. Fads1.

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 124CytoplasmicSequence analysisAdd BLAST124
Transmembranei125 – 145HelicalSequence analysisAdd BLAST21
Topological domaini146 – 160LumenalSequence analysisAdd BLAST15
Transmembranei161 – 180HelicalSequence analysisAdd BLAST20
Topological domaini181 – 268CytoplasmicSequence analysisAdd BLAST88
Transmembranei269 – 289HelicalSequence analysisAdd BLAST21
Topological domaini290 – 308LumenalSequence analysisAdd BLAST19
Transmembranei309 – 329HelicalSequence analysisAdd BLAST21
Topological domaini330 – 447CytoplasmicSequence analysisAdd BLAST118

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5725.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003070971 – 447Fatty acid desaturase 1Add BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ920L1.
PaxDbiQ920L1.
PeptideAtlasiQ920L1.
PRIDEiQ920L1.

PTM databases

iPTMnetiQ920L1.
PhosphoSitePlusiQ920L1.

Expressioni

Tissue specificityi

Highly expressed in the adrenal gland, liver, brain, and testis, tissues where lipogenesis and steroidogenesis are active.1 Publication

Inductioni

Expression in liver is down-regulated by dietary PUFA.1 Publication

Gene expression databases

BgeeiENSMUSG00000010663.
CleanExiMM_FADS1.
GenevisibleiQ920L1. MM.

Interactioni

Protein-protein interaction databases

IntActiQ920L1. 2 interactors.
MINTiMINT-1867264.
STRINGi10090.ENSMUSP00000010807.

Chemistry databases

BindingDBiQ920L1.

Structurei

3D structure databases

ProteinModelPortaliQ920L1.
SMRiQ920L1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 97Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST79

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi182 – 186Histidine box-15
Motifi219 – 223Histidine box-25
Motifi385 – 389Histidine box-35

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.
InParanoidiQ920L1.
KOiK10224.
OMAiFMVRFLE.
OrthoDBiEOG091G0E0W.
PhylomeDBiQ920L1.
TreeFamiTF313604.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR005804. FA_desaturase_dom.
IPR012171. Fatty_acid_desaturase.
[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.

Q920L1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPDPVPTPG PASAQLRQTR YFTWEEVAQR SGREKERWLV IDRKVYNISD
60 70 80 90 100
FSRRHPGGSR VISHYAGQDA TDPFVAFHIN KGLVRKYMNS LLIGELAPEQ
110 120 130 140 150
PSFEPTKNKA LTDEFRELRA TVERMGLMKA NHLFFLVYLL HILLLDVAAW
160 170 180 190 200
LTLWIFGTSL VPFILCAVLL STVQAQAGWL QHDFGHLSVF GTSTWNHLLH
210 220 230 240 250
HFVIGHLKGA PASWWNHMHF QHHAKPNCFR KDPDINMHPL FFALGKVLPV
260 270 280 290 300
ELGREKKKHM PYNHQHKYFF LIGPPALLPL YFQWYIFYFV VQRKKWVDLA
310 320 330 340 350
WMLSFYARIF FTYMPLLGLK GFLGLFFIVR 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):52,323
Last modified:December 1, 2001 - v1
Checksum:i1C69B61DF919A009
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32G → W in BAE32539 (PubMed:16141072).Curated1
Sequence conflicti297V → L in AAH26848 (PubMed:15489334).Curated1
Sequence conflicti369V → I in AAH26848 (PubMed:15489334).Curated1
Sequence conflicti369V → I in AAH22139 (PubMed:15489334).Curated1
Sequence conflicti369V → I in AAH26831 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB072976 mRNA. Translation: BAB69894.1.
AK033308 mRNA. Translation: BAC28228.1.
AK083959 mRNA. Translation: BAC39079.1.
AK154367 mRNA. Translation: BAE32539.1.
BC022139 mRNA. Translation: AAH22139.1.
BC026831 mRNA. Translation: AAH26831.1.
BC026848 mRNA. Translation: AAH26848.1.
BC063053 mRNA. Translation: AAH63053.1.
CCDSiCCDS29572.1.
RefSeqiNP_666206.1. NM_146094.2.
UniGeneiMm.30158.

Genome annotation databases

EnsembliENSMUST00000010807; ENSMUSP00000010807; ENSMUSG00000010663.
GeneIDi76267.
KEGGimmu:76267.
UCSCiuc008gpd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB072976 mRNA. Translation: BAB69894.1.
AK033308 mRNA. Translation: BAC28228.1.
AK083959 mRNA. Translation: BAC39079.1.
AK154367 mRNA. Translation: BAE32539.1.
BC022139 mRNA. Translation: AAH22139.1.
BC026831 mRNA. Translation: AAH26831.1.
BC026848 mRNA. Translation: AAH26848.1.
BC063053 mRNA. Translation: AAH63053.1.
CCDSiCCDS29572.1.
RefSeqiNP_666206.1. NM_146094.2.
UniGeneiMm.30158.

3D structure databases

ProteinModelPortaliQ920L1.
SMRiQ920L1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ920L1. 2 interactors.
MINTiMINT-1867264.
STRINGi10090.ENSMUSP00000010807.

Chemistry databases

BindingDBiQ920L1.
ChEMBLiCHEMBL5725.

PTM databases

iPTMnetiQ920L1.
PhosphoSitePlusiQ920L1.

Proteomic databases

EPDiQ920L1.
PaxDbiQ920L1.
PeptideAtlasiQ920L1.
PRIDEiQ920L1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000010807; ENSMUSP00000010807; ENSMUSG00000010663.
GeneIDi76267.
KEGGimmu:76267.
UCSCiuc008gpd.2. mouse.

Organism-specific databases

CTDi3992.
MGIiMGI:1923517. Fads1.

Phylogenomic databases

eggNOGiKOG4232. Eukaryota.
ENOG410XVSZ. LUCA.
GeneTreeiENSGT00510000046574.
HOGENOMiHOG000012997.
HOVERGENiHBG002839.
InParanoidiQ920L1.
KOiK10224.
OMAiFMVRFLE.
OrthoDBiEOG091G0E0W.
PhylomeDBiQ920L1.
TreeFamiTF313604.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiFads1. mouse.
PROiQ920L1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000010663.
CleanExiMM_FADS1.
GenevisibleiQ920L1. MM.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR005804. FA_desaturase_dom.
IPR012171. Fatty_acid_desaturase.
[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...

Entry informationi

Entry nameiFADS1_MOUSE
AccessioniPrimary (citable) accession number: Q920L1
Secondary accession number(s): Q3U494
, Q8BZX7, Q8R0G8, Q8VC07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 127 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.