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Q920L1

- FADS1_MOUSE

UniProt

Q920L1 - FADS1_MOUSE

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Protein

Fatty acid desaturase 1

Gene
Fads1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

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
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_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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 124124Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei125 – 14521Helical; Reviewed predictionAdd
BLAST
Topological domaini146 – 16015Lumenal Reviewed predictionAdd
BLAST
Transmembranei161 – 18020Helical; Reviewed predictionAdd
BLAST
Topological domaini181 – 26888Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei269 – 28921Helical; Reviewed predictionAdd
BLAST
Topological domaini290 – 30819Lumenal Reviewed predictionAdd
BLAST
Transmembranei309 – 32921Helical; Reviewed predictionAdd
BLAST
Topological domaini330 – 447118Cytoplasmic Reviewed predictionAdd
BLAST

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
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-acetylmethionine By 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 9779Cytochrome b5 heme-bindingAdd
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

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321G → W in BAE32539. 1 Publication
Sequence conflicti297 – 2971V → L in AAH26848. 1 Publication
Sequence conflicti369 – 3691V → I in AAH26848. 1 Publication
Sequence conflicti369 – 3691V → I in AAH22139. 1 Publication
Sequence conflicti369 – 3691V → I in AAH26831. 1 Publication

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

« 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: September 3, 2014
This is version 105 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