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Protein

Fatty acid desaturase 2

Gene

Fads2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 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

  • heme binding Source: InterPro
  • iron ion binding Source: InterPro
  • stearoyl-CoA 9-desaturase activity Source: MGI

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 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 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1930079. Fads2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 130130CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei131 – 15121HelicalSequence AnalysisAdd
BLAST
Topological domaini152 – 1521LumenalSequence Analysis
Transmembranei153 – 17321HelicalSequence AnalysisAdd
BLAST
Topological domaini174 – 26491CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei265 – 28521HelicalSequence AnalysisAdd
BLAST
Topological domaini286 – 30520LumenalSequence AnalysisAdd
BLAST
Transmembranei306 – 32621HelicalSequence AnalysisAdd
BLAST
Topological domaini327 – 444118CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

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

BgeeiQ9Z0R9.
CleanExiMM_FADS2.
ExpressionAtlasiQ9Z0R9. baseline and differential.
GenevestigatoriQ9Z0R9.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

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

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_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

        10         20         30         40         50
MGKGGNQGEG STERQAPMPT FRWEEIQKHN LRTDRWLVID RKVYNVTKWS
60 70 80 90 100
QRHPGGHRVI GHYSGEDATD AFRAFHLDLD FVGKFLKPLL IGELAPEEPS
110 120 130 140 150
LDRGKSSQIT EDFRALKKTA EDMNLFKTNH LFFFLLLSHI IVMESLAWFI
160 170 180 190 200
LSYFGTGWIP TLVTAFVLAT SQAQAGWLQH DYGHLSVYKK SIWNHVVHKF
210 220 230 240 250
VIGHLKGASA NWWNHRHFQH HAKPNIFHKD PDIKSLHVFV LGEWQPLEYG
260 270 280 290 300
KKKLKYLPYN HQHEYFFLIG PPLLIPMYFQ YQIIMTMISR RDWVDLAWAI
310 320 330 340 350
SYYMRFFYTY IPFYGILGAL VFLNFIRFLE SHWFVWVTQM NHLVMEIDLD
360 370 380 390 400
HYRDWFSSQL AATCNVEQSF FNDWFSGHLN FQIEHHLFPT MPRHNLHKIA
410 420 430 440
PLVKSLCAKH GIEYQEKPLL RALIDIVSSL KKSGELWLDA YLHK
Length:444
Mass (Da):52,387
Last modified:May 1, 1999 - v1
Checksum:i7615D17024D3B771
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBiQ9Z0R9.
ChEMBLiCHEMBL5087.

PTM databases

PhosphoSiteiQ9Z0R9.

Proteomic databases

MaxQBiQ9Z0R9.
PaxDbiQ9Z0R9.
PRIDEiQ9Z0R9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9415.
MGIiMGI:1930079. Fads2.

Phylogenomic databases

eggNOGiNOG70688.
GeneTreeiENSGT00510000046574.
HOGENOMiHOG000012997.
HOVERGENiHBG002839.
InParanoidiQ9Z0R9.
KOiK10226.
OMAiQPLEYGK.
OrthoDBiEOG7G1V6P.
PhylomeDBiQ9Z0R9.
TreeFamiTF313604.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiFads2. mouse.
NextBioi312742.
PROiQ9Z0R9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z0R9.
CleanExiMM_FADS2.
ExpressionAtlasiQ9Z0R9. baseline and differential.
GenevestigatoriQ9Z0R9.

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.
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 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.