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Q9Z0R9

- FADS2_MOUSE

UniProt

Q9Z0R9 - FADS2_MOUSE

Protein

Fatty acid desaturase 2

Gene

Fads2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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 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 By similarity.By similarity

    Pathwayi

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. stearoyl-CoA 9-desaturase activity Source: MGI

    GO - Biological processi

    1. 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.
    UniPathwayiUPA00658.

    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:Fadsd2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1930079. Fads2.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Fatty acid desaturase 2PRO_0000307103Add
    BLAST

    Proteomic databases

    MaxQBiQ9Z0R9.
    PaxDbiQ9Z0R9.
    PRIDEiQ9Z0R9.

    PTM databases

    PhosphoSiteiQ9Z0R9.

    Expressioni

    Tissue specificityi

    Highly expressed in the adrenal gland, liver, brain, and testis, tissues where lipogenesis and steroidogenesis are active. Also detected in lung, heart, and skeletal muscle.2 Publications

    Developmental stagei

    Found in 13-day-old embryo heart.

    Inductioni

    Induced by dietary PUFA-deficient diet. Induced by a fat-free diet and by a diet containing triolein (18:1n-9) as the only fat source. Down-regulated in liver by dietary PUFA.2 Publications

    Gene expression databases

    ArrayExpressiQ9Z0R9.
    BgeeiQ9Z0R9.
    CleanExiMM_FADS2.
    GenevestigatoriQ9Z0R9.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9Z0R9. 1 interaction.
    MINTiMINT-4131280.
    STRINGi10090.ENSMUSP00000025567.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z0R9.
    SMRiQ9Z0R9. Positions 21-98.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 130130CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini152 – 1521LumenalSequence Analysis
    Topological domaini174 – 26491CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini286 – 30520LumenalSequence AnalysisAdd
    BLAST
    Topological domaini327 – 444118CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei131 – 15121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei153 – 17321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei265 – 28521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei306 – 32621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 9578Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi180 – 1845Histidine box-1
    Motifi217 – 2215Histidine box-2
    Motifi382 – 3865Histidine 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

    eggNOGiNOG70688.
    GeneTreeiENSGT00510000046574.
    HOGENOMiHOG000012997.
    HOVERGENiHBG002839.
    InParanoidiQ9Z0R9.
    KOiK10226.
    OMAiQPLEYGK.
    OrthoDBiEOG7G1V6P.
    PhylomeDBiQ9Z0R9.
    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.
    SUPFAMiSSF55856. SSF55856. 1 hit.
    PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Z0R9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKGGNQGEG STERQAPMPT FRWEEIQKHN LRTDRWLVID RKVYNVTKWS    50
    QRHPGGHRVI GHYSGEDATD AFRAFHLDLD FVGKFLKPLL IGELAPEEPS 100
    LDRGKSSQIT EDFRALKKTA EDMNLFKTNH LFFFLLLSHI IVMESLAWFI 150
    LSYFGTGWIP TLVTAFVLAT SQAQAGWLQH DYGHLSVYKK SIWNHVVHKF 200
    VIGHLKGASA NWWNHRHFQH HAKPNIFHKD PDIKSLHVFV LGEWQPLEYG 250
    KKKLKYLPYN HQHEYFFLIG PPLLIPMYFQ YQIIMTMISR RDWVDLAWAI 300
    SYYMRFFYTY IPFYGILGAL VFLNFIRFLE SHWFVWVTQM NHLVMEIDLD 350
    HYRDWFSSQL AATCNVEQSF FNDWFSGHLN FQIEHHLFPT MPRHNLHKIA 400
    PLVKSLCAKH GIEYQEKPLL RALIDIVSSL KKSGELWLDA YLHK 444
    Length:444
    Mass (Da):52,387
    Last modified:May 1, 1999 - v1
    Checksum:i7615D17024D3B771
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126798 mRNA. Translation: AAD20017.1.
    AK143524 mRNA. Translation: BAE25416.1.
    BC057189 mRNA. Translation: AAH57189.1.
    CCDSiCCDS29571.1.
    RefSeqiNP_062673.1. NM_019699.1.
    UniGeneiMm.38901.

    Genome annotation databases

    EnsembliENSMUST00000025567; ENSMUSP00000025567; ENSMUSG00000024665.
    GeneIDi56473.
    KEGGimmu:56473.
    UCSCiuc008gpb.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126798 mRNA. Translation: AAD20017.1 .
    AK143524 mRNA. Translation: BAE25416.1 .
    BC057189 mRNA. Translation: AAH57189.1 .
    CCDSi CCDS29571.1.
    RefSeqi NP_062673.1. NM_019699.1.
    UniGenei Mm.38901.

    3D structure databases

    ProteinModelPortali Q9Z0R9.
    SMRi Q9Z0R9. Positions 21-98.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9Z0R9. 1 interaction.
    MINTi MINT-4131280.
    STRINGi 10090.ENSMUSP00000025567.

    Chemistry

    BindingDBi Q9Z0R9.
    ChEMBLi CHEMBL5087.

    PTM databases

    PhosphoSitei Q9Z0R9.

    Proteomic databases

    MaxQBi Q9Z0R9.
    PaxDbi Q9Z0R9.
    PRIDEi Q9Z0R9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025567 ; ENSMUSP00000025567 ; ENSMUSG00000024665 .
    GeneIDi 56473.
    KEGGi mmu:56473.
    UCSCi uc008gpb.1. mouse.

    Organism-specific databases

    CTDi 9415.
    MGIi MGI:1930079. Fads2.

    Phylogenomic databases

    eggNOGi NOG70688.
    GeneTreei ENSGT00510000046574.
    HOGENOMi HOG000012997.
    HOVERGENi HBG002839.
    InParanoidi Q9Z0R9.
    KOi K10226.
    OMAi QPLEYGK.
    OrthoDBi EOG7G1V6P.
    PhylomeDBi Q9Z0R9.
    TreeFami TF313604.

    Enzyme and pathway databases

    UniPathwayi UPA00658 .
    Reactomei REACT_196530. Linoleic acid (LA) metabolism.
    REACT_196541. alpha-linolenic acid (ALA) metabolism.

    Miscellaneous databases

    ChiTaRSi FADS2. mouse.
    NextBioi 312742.
    PROi Q9Z0R9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z0R9.
    Bgeei Q9Z0R9.
    CleanExi MM_FADS2.
    Genevestigatori Q9Z0R9.

    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.
    SUPFAMi SSF55856. SSF55856. 1 hit.
    PROSITEi PS50255. CYTOCHROME_B5_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and nutritional regulation of the mammalian Delta-6 desaturase."
      Cho H.P., Nakamura M.T., Clarke S.D.
      J. Biol. Chem. 274:471-477(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    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.
      Tissue: Embryo.
    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: FVB/N.
      Tissue: Liver.
    4. "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: TISSUE SPECIFICITY, INDUCTION.
      Strain: C57BL/6J.
      Tissue: Liver.

    Entry informationi

    Entry nameiFADS2_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z0R9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 109 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