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O95864 (FADS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:FADS2
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

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. It catalizes as well the introduction of a cis double bond in palmitate to produce the mono-unsaturated fatty acid sapienate, the most abundant fatty acid in sebum. Ref.1 Ref.10

Pathway

Lipid metabolism; polyunsaturated fatty acid biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Tissue specificity

Expressed in a wide array of tissues, highest expression is found in liver followed by brain, lung, heart, and retina. A lower level is found in breast tumor when compared with normal tissues; lowest levels were found in patients with poor prognostic index. Ref.1 Ref.2 Ref.13

Developmental stage

Found in fetal heart.

Induction

Repressed by dietary highly unsaturated fatty acids. Ref.9 Ref.12

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.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95864-1)

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: O95864-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: MGKGGNQGEG...IGHYAGEDAT → MHGREAGPFV...SAGHPITGQQ
Isoform 3 (identifier: O95864-3)

The sequence of this isoform differs from the canonical sequence as follows:
     386-444: HLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGKLWLDAYLHK → Q
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Fatty acid desaturase 2
PRO_0000307101

Regions

Topological domain1 – 131131Cytoplasmic Potential
Transmembrane132 – 15221Helical; Potential
Topological domain153 – 1575Lumenal Potential
Transmembrane158 – 17821Helical; Potential
Topological domain179 – 26486Cytoplasmic Potential
Transmembrane265 – 28521Helical; Potential
Topological domain286 – 30520Lumenal Potential
Transmembrane306 – 32621Helical; Potential
Topological domain327 – 444118Cytoplasmic Potential
Domain18 – 9578Cytochrome b5 heme-binding
Motif180 – 1845Histidine box-1
Motif217 – 2215Histidine box-2
Motif382 – 3865Histidine box-3

Natural variations

Alternative sequence1 – 6969MGKGG…GEDAT → MHGREAGPFVCVCVLLASIP TPQTPLLQASLPPFHPASAG HPITGQQ in isoform 2.
VSP_028568
Alternative sequence386 – 44459HLFPT…AYLHK → Q in isoform 3.
VSP_028569

Experimental info

Sequence conflict134 – 1374LLLL → RTRG in CAB43280. Ref.8
Sequence conflict380 – 3812NF → SL in BAB55167. Ref.4
Sequence conflict429 – 4313SLK → DLM in CAB43280. Ref.8

Sequences

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

Last modified May 1, 1999. Version 1.
Checksum: F65CE58076961A7A

FASTA44452,259
        10         20         30         40         50         60 
MGKGGNQGEG AAEREVSVPT FSWEEIQKHN LRTDRWLVID RKVYNITKWS IQHPGGQRVI 

        70         80         90        100        110        120 
GHYAGEDATD AFRAFHPDLE FVGKFLKPLL IGELAPEEPS QDHGKNSKIT EDFRALRKTA 

       130        140        150        160        170        180 
EDMNLFKTNH VFFLLLLAHI IALESIAWFT VFYFGNGWIP TLITAFVLAT SQAQAGWLQH 

       190        200        210        220        230        240 
DYGHLSVYRK PKWNHLVHKF VIGHLKGASA NWWNHRHFQH HAKPNIFHKD PDVNMLHVFV 

       250        260        270        280        290        300 
LGEWQPIEYG KKKLKYLPYN HQHEYFFLIG PPLLIPMYFQ YQIIMTMIVH KNWVDLAWAV 

       310        320        330        340        350        360 
SYYIRFFITY IPFYGILGAL LFLNFIRFLE SHWFVWVTQM NHIVMEIDQE AYRDWFSSQL 

       370        380        390        400        410        420 
TATCNVEQSF FNDWFSGHLN FQIEHHLFPT MPRHNLHKIA PLVKSLCAKH GIEYQEKPLL 

       430        440 
RALLDIIRSL KKSGKLWLDA YLHK 

« Hide

Isoform 2 [UniParc].

Checksum: A4A7EB76FBF1FFA4
Show »

FASTA42249,326
Isoform 3 [UniParc].

Checksum: 2A18FA9CBFBFE432
Show »

FASTA38645,524

References

« Hide 'large scale' references
[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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[2]"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.
[3]Zhang J.S.S., Reddel R.R.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Mesothelium.
[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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 277-444 (ISOFORMS 1/2).
Tissue: Tongue.
[5]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 3).
Tissue: Brain.
[8]"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] OF 134-444 (ISOFORMS 1/2).
Tissue: Uterus.
[9]"The E-box like sterol regulatory element mediates the suppression of human Delta-6 desaturase gene by highly unsaturated fatty acids."
Nara T.Y., He W.S., Tang C., Clarke S.D., Nakamura M.T.
Biochem. Biophys. Res. Commun. 296:111-117(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"Identification of the delta-6 desaturase of human sebaceous glands: expression and enzyme activity."
Ge L., Gordon J.S., Hsuan C., Stenn K., Prouty S.M.
J. Invest. Dermatol. 120:707-714(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]Erratum
Ge L., Gordon J.S., Hsuan C., Stenn K., Prouty S.M.
J. Invest. Dermatol. 121:434-434(2003)
[12]"Regulation of human delta-6 desaturase gene transcription: identification of a functional direct repeat-1 element."
Tang C., Cho H.P., Nakamura M.T., Clarke S.D.
J. Lipid Res. 44:686-695(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[13]"Expression of human delta-6-desaturase is associated with aggressiveness of human breast cancer."
Lane J., Mansel R.E., Jiang W.G.
Int. J. Mol. Med. 12:253-257(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF126799 mRNA. Translation: AAD20018.1.
AF084559 mRNA. Translation: AAG23121.1.
AF108658 mRNA. Translation: AAG43192.1.
AK027513 mRNA. Translation: BAB55167.1.
AK290291 mRNA. Translation: BAF82980.1.
AK074939 mRNA. Translation: BAC11305.1.
CH471076 Genomic DNA. Translation: EAW73975.1.
BC009011 mRNA. Translation: AAH09011.1.
AL050118 mRNA. Translation: CAB43280.1.
BX640945 mRNA. Translation: CAE45971.1.
PIRT13155.
RefSeqNP_001268430.1. NM_001281501.1.
NP_001268431.1. NM_001281502.1.
NP_004256.1. NM_004265.3.
UniGeneHs.502745.

3D structure databases

ProteinModelPortalO95864.
SMRO95864. Positions 17-98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114810. 3 interactions.
MINTMINT-2866355.
STRING9606.ENSP00000278840.

Chemistry

BindingDBO95864.
ChEMBLCHEMBL6097.
DrugBankDB00132. Alpha-Linolenic Acid.

PTM databases

PhosphoSiteO95864.

Proteomic databases

PaxDbO95864.
PeptideAtlasO95864.
PRIDEO95864.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257261; ENSP00000257261; ENSG00000134824. [O95864-2]
ENST00000278840; ENSP00000278840; ENSG00000134824. [O95864-1]
ENST00000521849; ENSP00000431091; ENSG00000134824. [O95864-3]
GeneID9415.
KEGGhsa:9415.
UCSCuc001nsj.2. human. [O95864-2]
uc001nsk.3. human. [O95864-3]
uc001nsl.1. human. [O95864-1]

Organism-specific databases

CTD9415.
GeneCardsGC11P061583.
HGNCHGNC:3575. FADS2.
HPAHPA006741.
MIM606149. gene.
neXtProtNX_O95864.
PharmGKBPA27974.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5274.
HOVERGENHBG002839.
InParanoidO95864.
KOK10226.
OMAAWFTIFY.
PhylomeDBO95864.
TreeFamTF313604.

Enzyme and pathway databases

BioCycMetaCyc:HS05918-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00658.

Gene expression databases

ArrayExpressO95864.
BgeeO95864.
CleanExHS_FADS2.
GenevestigatorO95864.

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.
SUPFAMSSF55856. SSF55856. 1 hit.
PROSITEPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFADS2. human.
GeneWikiFADS2.
GenomeRNAi9415.
NextBio35274.
PROO95864.
SOURCESearch...

Entry information

Entry nameFADS2_HUMAN
AccessionPrimary (citable) accession number: O95864
Secondary accession number(s): A8K2M6 expand/collapse secondary AC list , Q6MZQ7, Q96H07, Q96SV8, Q9H3G3, Q9Y3X4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 110 of the entry and version 1 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 chromosome 11

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