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O60427 (FADS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
Synonyms:FADSD5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 2 does not exhibit any catalytic activity toward 20:3n-6, but it may enhance FADS2 activity By similarity. Isoform 1 is a 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. Ref.1 Ref.2

Pathway

Lipid metabolism; polyunsaturated fatty acid biosynthesis.

Subcellular location

Isoform 1: Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Mitochondrion Ref.9.

Isoform 2: Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.9.

Tissue specificity

Widely expressed, with highest levels in liver, brain, adrenal gland and heart. Highly expressed in fetal liver and brain. Ref.1 Ref.2 Ref.3

Induction

Strongly down-regulated upon differentiation in a neuroblastoma cell line (at protein level). Ref.9

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.

Sequence caution

The sequence BAC11182.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAC11229.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

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

Inferred from electronic annotation. Source: Ensembl

alpha-linolenic acid metabolic process

Traceable author statement. Source: Reactome

arachidonic acid metabolic process

Inferred from electronic annotation. Source: Ensembl

cell-cell signaling

Non-traceable author statement Ref.1. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular response to starvation

Inferred from direct assay Ref.1. Source: UniProtKB

icosanoid biosynthetic process

Traceable author statement Ref.1. Source: UniProtKB

linoleic acid metabolic process

Traceable author statement. Source: Reactome

phospholipid biosynthetic process

Traceable author statement Ref.1. Source: UniProtKB

regulation of cell differentiation

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

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

small molecule metabolic process

Traceable author statement. Source: Reactome

unsaturated fatty acid biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

unsaturated fatty acid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Non-traceable author statement Ref.1. Source: UniProtKB

intracellular membrane-bounded organelle

Non-traceable author statement Ref.1. Source: UniProtKB

membrane

Non-traceable author statement Ref.1. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionC-5 sterol desaturase activity

Traceable author statement Ref.1. Source: ProtInc

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60427-1)

Also known as: FADS1CS;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O60427-2)

Also known as: FADS1AT1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Fatty acid desaturase 1
PRO_0000307096

Regions

Topological domain1 – 121121Cytoplasmic Potential
Transmembrane122 – 14221Helical; Potential
Topological domain143 – 1453Lumenal Potential
Transmembrane146 – 17025Helical; Potential
Topological domain171 – 26797Cytoplasmic Potential
Transmembrane268 – 28821Helical; Potential
Topological domain289 – 30517Lumenal Potential
Transmembrane306 – 32621Helical; Potential
Topological domain327 – 444118Cytoplasmic Potential
Domain17 – 9478Cytochrome b5 heme-binding
Motif179 – 1835Histidine box-1
Motif216 – 2205Histidine box-2
Motif382 – 3865Histidine box-3

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10

Natural variations

Alternative sequence1 – 8484Missing in isoform 2.
VSP_047521
Natural variant2721P → S. Ref.8
Corresponds to variant rs17856235 [ dbSNP | Ensembl ].
VAR_035340

Experimental info

Sequence conflict61V → L in AAF29378. Ref.7
Sequence conflict91E → G in BAB55103. Ref.1
Sequence conflict151P → L in AAF29378. Ref.7
Sequence conflict1001F → L in BAC11182. Ref.1
Sequence conflict1431D → E in BAC11182. Ref.1
Sequence conflict1801D → G in BAD96626. Ref.5
Sequence conflict2121W → R in BAB55173. Ref.1
Sequence conflict2131N → S in BAC11182. Ref.1
Sequence conflict2551K → N in AAF29378. Ref.7
Sequence conflict3191F → L in BAB55103. Ref.1
Sequence conflict3611Q → L in AAF70457. Ref.8
Sequence conflict3811F → S in BAC11229. Ref.1
Sequence conflict4101H → R in AAF70457. Ref.8
Sequence conflict4311K → E in BAC11229. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (FADS1CS) [UniParc].

Last modified December 11, 2013. Version 3.
Checksum: CC3C28D82AA49BF2

FASTA44451,964
        10         20         30         40         50         60 
MAPDPVAAET AAQGPTPRYF TWDEVAQRSG CEERWLVIDR KVYNISEFTR RHPGGSRVIS 

        70         80         90        100        110        120 
HYAGQDATDP FVAFHINKGL VKKYMNSLLI GELSPEQPSF EPTKNKELTD EFRELRATVE 

       130        140        150        160        170        180 
RMGLMKANHV FFLLYLLHIL LLDGAAWLTL WVFGTSFLPF LLCAVLLSAV QAQAGWLQHD 

       190        200        210        220        230        240 
FGHLSVFSTS KWNHLLHHFV IGHLKGAPAS WWNHMHFQHH AKPNCFRKDP DINMHPFFFA 

       250        260        270        280        290        300 
LGKILSVELG KQKKKYMPYN HQHKYFFLIG PPALLPLYFQ WYIFYFVIQR KKWVDLAWMI 

       310        320        330        340        350        360 
TFYVRFFLTY VPLLGLKAFL GLFFIVRFLE SNWFVWVTQM NHIPMHIDHD RNMDWVSTQL 

       370        380        390        400        410        420 
QATCNVHKSA FNDWFSGHLN FQIEHHLFPT MPRHNYHKVA PLVQSLCAKH GIEYQSKPLL 

       430        440 
SAFADIIHSL KESGQLWLDA YLHQ 

« Hide

Isoform 2 (FADS1AT1) [UniParc].

Checksum: CD55B8317E4BF21E
Show »

FASTA36042,474

References

« Hide 'large scale' references
[1]"Cloning, expression, and fatty acid regulation of the human Delta-5 desaturase."
Cho H.P., Nakamura M., Clarke S.D.
J. Biol. Chem. 274:37335-37339(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[2]"cDNA cloning and characterization of human Delta5-desaturase involved in the biosynthesis of arachidonic acid."
Leonard A.E., Kelder B., Bobik E.G., Chuang L.-T., Parker-Barnes J.M., Thurmond J.M., Kroeger P.E., Kopchick J.J., Huang Y.-S., Mukerji P.
Biochem. J. 347:719-724(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Tissue: Liver.
[3]"cDNA cloning, genomic structure, and chromosomal localization of three members of the human fatty acid desaturase family."
Marquardt A., Stoehr H., White K., Weber B.H.
Genomics 66:175-183(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Retina.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Cerebellum, Neuroblastoma and Teratocarcinoma.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Melanoma.
[6]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Kidney epithelium.
[7]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 1), VARIANT SER-272.
Tissue: Brain.
[9]"A novel FADS1 isoform potentiates FADS2-mediated production of eicosanoid precursor fatty acids."
Park W.J., Kothapalli K.S., Reardon H.T., Lawrence P., Qian S.B., Brenna J.T.
J. Lipid Res. 53:1502-1512(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION (ISOFORM 1), INDUCTION.
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK027427 mRNA. Translation: BAB55103.1.
AK027522 mRNA. Translation: BAB55173.1.
AK074754 mRNA. Translation: BAC11182.1. Different initiation.
AK074819 mRNA. Translation: BAC11229.1. Different initiation.
AK096275 mRNA. Translation: BAG53244.1.
AK289552 mRNA. Translation: BAF82241.1.
AK314199 mRNA. Translation: BAG36877.1.
AC004770 Genomic DNA. Translation: AAC23397.1.
AP002380 Genomic DNA. No translation available.
AF084558 mRNA. Translation: AAG23120.1.
AL512760 mRNA. Translation: CAC21679.1.
AL834479 mRNA. Translation: CAD39138.1.
AK222906 mRNA. Translation: BAD96626.1.
BC007846 mRNA. Translation: AAH07846.1.
AF199596 mRNA. Translation: AAF29378.1.
AF226273 mRNA. Translation: AAF70457.1.
RefSeqNP_037534.3. NM_013402.4.
UniGeneHs.503546.

3D structure databases

ProteinModelPortalO60427.
SMRO60427. Positions 19-107.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110180. 4 interactions.

Chemistry

BindingDBO60427.
ChEMBLCHEMBL5840.
DrugBankDB00132. Alpha-Linolenic Acid.
DB00159. Icosapent.

PTM databases

PhosphoSiteO60427.

Proteomic databases

MaxQBO60427.
PaxDbO60427.
PRIDEO60427.

Protocols and materials databases

DNASU3992.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000433932; ENSP00000405087; ENSG00000149485. [O60427-2]
ENST00000542506; ENSP00000441403; ENSG00000149485. [O60427-2]
GeneID3992.
KEGGhsa:3992.
UCSCuc001nsh.3. human. [O60427-1]

Organism-specific databases

CTD3992.
GeneCardsGC11M061567.
HGNCHGNC:3574. FADS1.
HPAHPA042705.
MIM606148. gene.
neXtProtNX_O60427.
PharmGKBPA27973.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5274.
HOVERGENHBG002839.
InParanoidO60427.
KOK10224.
OrthoDBEOG7G1V6P.
PhylomeDBO60427.
TreeFamTF313604.

Enzyme and pathway databases

BioCycMetaCyc:HS07617-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00658.

Gene expression databases

ArrayExpressO60427.
BgeeO60427.
GenevestigatorO60427.

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. human.
GeneWikiFADS1.
GenomeRNAi3992.
NextBio15660.
PROO60427.
SOURCESearch...

Entry information

Entry nameFADS1_HUMAN
AccessionPrimary (citable) accession number: O60427
Secondary accession number(s): A8K0I7 expand/collapse secondary AC list , B2RAI0, Q53GM5, Q8N3A6, Q8NCC7, Q8NCG0, Q96I39, Q96SV3, Q96T10, Q9NRP8, Q9NYX1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 11, 2013
Last modified: June 11, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM