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Q920L1 (FADS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Fads1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Pathway

Lipid metabolism; polyunsaturated fatty acid biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Mitochondrion By similarity.

Tissue specificity

Highly expressed in the adrenal gland, liver, brain, and testis, tissues where lipogenesis and steroidogenesis are active. Ref.1

Induction

Expression in liver is down-regulated by dietary PUFA. Ref.1

Domain

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similarities

Belongs to the fatty acid desaturase family.

Contains 1 cytochrome b5 heme-binding domain.

Ontologies

Keywords
   Biological processElectron transport
Fatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Transport
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
   DomainTransmembrane
Transmembrane helix
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

arachidonic acid metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to starvation

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to sucrose

Inferred from electronic annotation. Source: Ensembl

response to vitamin A

Inferred from electronic annotation. Source: Ensembl

unsaturated fatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionheme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

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

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Fatty acid desaturase 1
PRO_0000307097

Regions

Topological domain1 – 124124Cytoplasmic Potential
Transmembrane125 – 14521Helical; Potential
Topological domain146 – 16015Lumenal Potential
Transmembrane161 – 18020Helical; Potential
Topological domain181 – 26888Cytoplasmic Potential
Transmembrane269 – 28921Helical; Potential
Topological domain290 – 30819Lumenal Potential
Transmembrane309 – 32921Helical; Potential
Topological domain330 – 447118Cytoplasmic Potential
Domain19 – 9779Cytochrome b5 heme-binding
Motif182 – 1865Histidine box-1
Motif219 – 2235Histidine box-2
Motif385 – 3895Histidine box-3

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Experimental info

Sequence conflict321G → W in BAE32539. Ref.2
Sequence conflict2971V → L in AAH26848. Ref.3
Sequence conflict3691V → I in AAH26848. Ref.3
Sequence conflict3691V → I in AAH22139. Ref.3
Sequence conflict3691V → I in AAH26831. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q920L1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1C69B61DF919A009

FASTA44752,323
        10         20         30         40         50         60 
MAPDPVPTPG PASAQLRQTR YFTWEEVAQR SGREKERWLV IDRKVYNISD FSRRHPGGSR 

        70         80         90        100        110        120 
VISHYAGQDA TDPFVAFHIN KGLVRKYMNS LLIGELAPEQ PSFEPTKNKA LTDEFRELRA 

       130        140        150        160        170        180 
TVERMGLMKA NHLFFLVYLL HILLLDVAAW LTLWIFGTSL VPFILCAVLL STVQAQAGWL 

       190        200        210        220        230        240 
QHDFGHLSVF GTSTWNHLLH HFVIGHLKGA PASWWNHMHF QHHAKPNCFR KDPDINMHPL 

       250        260        270        280        290        300 
FFALGKVLPV ELGREKKKHM PYNHQHKYFF LIGPPALLPL YFQWYIFYFV VQRKKWVDLA 

       310        320        330        340        350        360 
WMLSFYARIF FTYMPLLGLK GFLGLFFIVR FLESNWFVWV TQMNHIPMHI DHDRNVDWVS 

       370        380        390        400        410        420 
TQLQATCNVH QSAFNNWFSG HLNFQIEHHL FPTMPRHNYH KVAPLVQSLC AKYGIKYESK 

       430        440 
PLLTAFADIV YSLKESGQLW LDAYLHQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS29572.1.
RefSeqNP_666206.1. NM_146094.2.
UniGeneMm.30158.

3D structure databases

ProteinModelPortalQ920L1.
SMRQ920L1. Positions 21-74.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ920L1. 2 interactions.
MINTMINT-1867264.

Chemistry

BindingDBQ920L1.
ChEMBLCHEMBL5725.

PTM databases

PhosphoSiteQ920L1.

Proteomic databases

MaxQBQ920L1.
PaxDbQ920L1.
PRIDEQ920L1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000010807; ENSMUSP00000010807; ENSMUSG00000010663.
GeneID76267.
KEGGmmu:76267.
UCSCuc008gpd.2. mouse.

Organism-specific databases

CTD3992.
MGIMGI:1923517. Fads1.

Phylogenomic databases

eggNOGCOG5274.
GeneTreeENSGT00510000046574.
HOGENOMHOG000012997.
HOVERGENHBG002839.
InParanoidQ920L1.
KOK10224.
OMAFMVRFLE.
OrthoDBEOG7G1V6P.
PhylomeDBQ920L1.
TreeFamTF313604.

Enzyme and pathway databases

UniPathwayUPA00658.

Gene expression databases

BgeeQ920L1.
CleanExMM_FADS1.
GenevestigatorQ920L1.

Family and domain databases

Gene3D3.10.120.10. 1 hit.
InterProIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR012171. Fatty_acid/sphinglp_desaturase.
IPR005804. Fatty_acid_desaturase-1.
[Graphical view]
PfamPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFPIRSF015921. FA_sphinglp_des. 1 hit.
PRINTSPR00363. CYTOCHROMEB5.
SUPFAMSSF55856. SSF55856. 1 hit.
PROSITEPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFADS1. mouse.
NextBio344887.
PROQ920L1.
SOURCESearch...

Entry information

Entry nameFADS1_MOUSE
AccessionPrimary (citable) accession number: Q920L1
Secondary accession number(s): Q3U494 expand/collapse secondary AC list , Q8BZX7, Q8R0G8, Q8VC07
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot