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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 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

Pathway:ipolyunsaturated 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

ReactomeiREACT_306137. alpha-linolenic acid (ALA) metabolism.
REACT_313684. Linoleic acid (LA) 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
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1923517. Fads1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 124124CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence AnalysisAdd
BLAST
Topological domaini146 – 16015LumenalSequence AnalysisAdd
BLAST
Transmembranei161 – 18020HelicalSequence 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

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Fatty acid desaturase 1PRO_0000307097Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ920L1.
PaxDbiQ920L1.
PRIDEiQ920L1.

PTM databases

PhosphoSiteiQ920L1.

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

BgeeiQ920L1.
CleanExiMM_FADS1.
GenevisibleiQ920L1. MM.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ920L1.
SMRiQ920L1. Positions 21-74.
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

Belongs to the fatty acid desaturase family.Curated
Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5274.
GeneTreeiENSGT00510000046574.
HOGENOMiHOG000012997.
HOVERGENiHBG002839.
InParanoidiQ920L1.
KOiK10224.
OMAiFMVRFLE.
OrthoDBiEOG7G1V6P.
PhylomeDBiQ920L1.
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-1.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321G → W in BAE32539 (PubMed:16141072).Curated
Sequence conflicti297 – 2971V → L in AAH26848 (PubMed:15489334).Curated
Sequence conflicti369 – 3691V → I in AAH26848 (PubMed:15489334).Curated
Sequence conflicti369 – 3691V → I in AAH22139 (PubMed:15489334).Curated
Sequence conflicti369 – 3691V → I in AAH26831 (PubMed:15489334).Curated

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. Positions 21-74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiQ920L1.
ChEMBLiCHEMBL5725.

PTM databases

PhosphoSiteiQ920L1.

Proteomic databases

MaxQBiQ920L1.
PaxDbiQ920L1.
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

eggNOGiCOG5274.
GeneTreeiENSGT00510000046574.
HOGENOMiHOG000012997.
HOVERGENiHBG002839.
InParanoidiQ920L1.
KOiK10224.
OMAiFMVRFLE.
OrthoDBiEOG7G1V6P.
PhylomeDBiQ920L1.
TreeFamiTF313604.

Enzyme and pathway databases

UniPathwayiUPA00658.
ReactomeiREACT_306137. alpha-linolenic acid (ALA) metabolism.
REACT_313684. Linoleic acid (LA) metabolism.

Miscellaneous databases

ChiTaRSiFads1. mouse.
NextBioi344887.
PROiQ920L1.
SOURCEiSearch...

Gene expression databases

BgeeiQ920L1.
CleanExiMM_FADS1.
GenevisibleiQ920L1. MM.

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-1.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Dual regulation of mouse Delta(5)- and Delta(6)-desaturase gene expression by SREBP-1 and PPARalpha."
    Matsuzaka T., Shimano H., Yahagi N., Amemiya-Kudo M., Yoshikawa T., Hasty A.H., Tamura Y., Osuga J., Okazaki H., Iizuka Y., Takahashi A., Sone H., Gotoda T., Ishibashi S., Yamada N.
    J. Lipid Res. 43:107-114(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Spinal ganglion and Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain, Kidney and Liver.

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: June 24, 2015
This is version 115 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

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.