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Q920L1

- FADS1_MOUSE

UniProt

Q920L1 - FADS1_MOUSE

Protein

Fatty acid desaturase 1

Gene

Fads1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water Source: Ensembl

    GO - Biological processi

    1. aging Source: Ensembl
    2. arachidonic acid metabolic process Source: Ensembl
    3. cellular response to starvation Source: Ensembl
    4. response to insulin Source: Ensembl
    5. response to organic cyclic compound Source: Ensembl
    6. response to sucrose Source: Ensembl
    7. response to vitamin A Source: Ensembl
    8. unsaturated fatty acid biosynthetic process Source: UniProtKB-UniPathway

    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_196530. Linoleic acid (LA) metabolism.
    REACT_196541. alpha-linolenic acid (ALA) metabolism.
    REACT_198602. PPARA activates gene expression.
    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: Chromosome 19

    Organism-specific databases

    MGIiMGI:1923517. Fads1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. mitochondrion Source: UniProtKB-SubCell
    4. nucleus Source: Ensembl

    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.
    GenevestigatoriQ920L1.

    Interactioni

    Protein-protein interaction databases

    IntActiQ920L1. 2 interactions.
    MINTiMINT-1867264.

    Structurei

    3D structure databases

    ProteinModelPortaliQ920L1.
    SMRiQ920L1. Positions 21-74.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 124124CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini146 – 16015LumenalSequence AnalysisAdd
    BLAST
    Topological domaini181 – 26888CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini290 – 30819LumenalSequence AnalysisAdd
    BLAST
    Topological domaini330 – 447118CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei125 – 14521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei161 – 18020HelicalSequence AnalysisAdd
    BLAST
    Transmembranei269 – 28921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei309 – 32921HelicalSequence AnalysisAdd
    BLAST

    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/sphinglp_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

    MAPDPVPTPG PASAQLRQTR YFTWEEVAQR SGREKERWLV IDRKVYNISD    50
    FSRRHPGGSR VISHYAGQDA TDPFVAFHIN KGLVRKYMNS LLIGELAPEQ 100
    PSFEPTKNKA LTDEFRELRA TVERMGLMKA NHLFFLVYLL HILLLDVAAW 150
    LTLWIFGTSL VPFILCAVLL STVQAQAGWL QHDFGHLSVF GTSTWNHLLH 200
    HFVIGHLKGA PASWWNHMHF QHHAKPNCFR KDPDINMHPL FFALGKVLPV 250
    ELGREKKKHM PYNHQHKYFF LIGPPALLPL YFQWYIFYFV VQRKKWVDLA 300
    WMLSFYARIF FTYMPLLGLK GFLGLFFIVR FLESNWFVWV TQMNHIPMHI 350
    DHDRNVDWVS TQLQATCNVH QSAFNNWFSG HLNFQIEHHL FPTMPRHNYH 400
    KVAPLVQSLC AKYGIKYESK PLLTAFADIV YSLKESGQLW LDAYLHQ 447
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS29572.1.
    RefSeqi NP_666206.1. NM_146094.2.
    UniGenei Mm.30158.

    3D structure databases

    ProteinModelPortali Q920L1.
    SMRi Q920L1. Positions 21-74.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q920L1. 2 interactions.
    MINTi MINT-1867264.

    Chemistry

    BindingDBi Q920L1.
    ChEMBLi CHEMBL5725.

    PTM databases

    PhosphoSitei Q920L1.

    Proteomic databases

    MaxQBi Q920L1.
    PaxDbi Q920L1.
    PRIDEi Q920L1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000010807 ; ENSMUSP00000010807 ; ENSMUSG00000010663 .
    GeneIDi 76267.
    KEGGi mmu:76267.
    UCSCi uc008gpd.2. mouse.

    Organism-specific databases

    CTDi 3992.
    MGIi MGI:1923517. Fads1.

    Phylogenomic databases

    eggNOGi COG5274.
    GeneTreei ENSGT00510000046574.
    HOGENOMi HOG000012997.
    HOVERGENi HBG002839.
    InParanoidi Q920L1.
    KOi K10224.
    OMAi FMVRFLE.
    OrthoDBi EOG7G1V6P.
    PhylomeDBi Q920L1.
    TreeFami TF313604.

    Enzyme and pathway databases

    UniPathwayi UPA00658 .
    Reactomei REACT_196530. Linoleic acid (LA) metabolism.
    REACT_196541. alpha-linolenic acid (ALA) metabolism.
    REACT_198602. PPARA activates gene expression.

    Miscellaneous databases

    ChiTaRSi FADS1. mouse.
    NextBioi 344887.
    PROi Q920L1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q920L1.
    CleanExi MM_FADS1.
    Genevestigatori Q920L1.

    Family and domain databases

    Gene3Di 3.10.120.10. 1 hit.
    InterProi IPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR012171. Fatty_acid/sphinglp_desaturase.
    IPR005804. Fatty_acid_desaturase-1.
    [Graphical view ]
    Pfami PF00173. Cyt-b5. 1 hit.
    PF00487. FA_desaturase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015921. FA_sphinglp_des. 1 hit.
    PRINTSi PR00363. CYTOCHROMEB5.
    SUPFAMi SSF55856. SSF55856. 1 hit.
    PROSITEi PS50255. CYTOCHROME_B5_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 106 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