O60427 (FADS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	FADS1
Synonyms:	FADSD5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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	Endoplasmic reticulum membrane; Multi-pass membrane protein Potential.
Tissue specificity	Expressed in many tissues, it is most abundant in the liver, brain, adrenal gland and heart. Found as well in skeletal muscle, lung, placenta, kidney, pancreas and retina. Ref.1 Ref.2 Ref.3
Developmental stage	Highly expressed in fetal liver and fetal brain. Ref.1 Ref.2
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. The sequence BAC11229.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Electron transport Fatty acid biosynthesis Lipid synthesis Transport
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell-cell signaling Non-traceable author statement Ref.1. Source: UniProtKB cellular response to starvation Inferred from direct assay Ref.1. Source: UniProtKB electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW icosanoid biosynthetic process Traceable author statement Ref.1. Source: UniProtKB 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-dependent Non-traceable author statement Ref.1. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Non-traceable author statement Ref.1. Source: UniProtKB microsome Non-traceable author statement Ref.1. Source: UniProtKB
Molecular function	C-5 sterol desaturase activity Traceable author statement. Source: ProtInc heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DHCR7	Q9UBM7	1	EBI-1055473,EBI-1054468
PAAF1	Q9BRP4	1	EBI-1055473,EBI-1056358

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Fatty acid desaturase 1		PRO_0000307096
Regions
	Topological domain	1 – 121	121	Cytoplasmic Potential
	Transmembrane	122 – 142	21	Helical; Potential
	Topological domain	143 – 145	3	Lumenal Potential
	Transmembrane	146 – 170	25	Helical; Potential
	Topological domain	171 – 267	97	Cytoplasmic Potential
	Transmembrane	268 – 288	21	Helical; Potential
	Topological domain	289 – 305	17	Lumenal Potential
	Transmembrane	306 – 326	21	Helical; Potential
	Topological domain	327 – 444	118	Cytoplasmic Potential
	Domain	17 – 94	78	Cytochrome b5 heme-binding
	Motif	179 – 183	5	Histidine box-1
	Motif	216 – 220	5	Histidine box-2
	Motif	382 – 386	5	Histidine box-3
Natural variations
	Natural variant	272	1	P → S. Ref.8 Corresponds to variant rs17856235 [ dbSNP | Ensembl ].		VAR_035340
Experimental info
	Sequence conflict	6	1	V → L in AAF29378. Ref.1
	Sequence conflict	9	1	E → G in BAB55103. Ref.4
	Sequence conflict	15	1	P → L in AAF29378. Ref.1
	Sequence conflict	100	1	F → L in BAC11182. Ref.4
	Sequence conflict	143	1	D → E in BAC11182. Ref.4
	Sequence conflict	180	1	D → G in BAD96626. Ref.5
	Sequence conflict	212	1	W → R in BAB55173. Ref.4
	Sequence conflict	213	1	N → S in BAC11182. Ref.4
	Sequence conflict	255	1	K → N in AAF29378. Ref.1
	Sequence conflict	319	1	F → L in BAB55103. Ref.4
	Sequence conflict	361	1	Q → L in AAF70457. Ref.2
	Sequence conflict	381	1	F → S in BAC11229. Ref.4
	Sequence conflict	410	1	H → R in AAF70457. Ref.2
	Sequence conflict	431	1	K → E in BAC11229. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O60427 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: CC3C28D82AA49BF2	FASTA	444	51,964
	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

References

	« Hide 'large scale' referencesShow '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: 10601301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[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: 10769175] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, 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: 10860662] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	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]. Tissue: Kidney.
[6]	"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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Melanoma.
[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. , 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: 16554811] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-272. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF199596 mRNA. Translation: AAF29378.1. AF226273 mRNA. Translation: AAF70457.1. AF084558 mRNA. Translation: AAG23120.1. AK027427 mRNA. Translation: BAB55103.1. AK027522 mRNA. Translation: BAB55173.1. AK074754 mRNA. Translation: BAC11182.1. Different initiation. AK074819 mRNA. Translation: BAC11229.1. Different initiation. AK222906 mRNA. Translation: BAD96626.1. AK314199 mRNA. Translation: BAG36877.1. AL512760 mRNA. Translation: CAC21679.1. AL834479 mRNA. Translation: CAD39138.1. AC004770 Genomic DNA. Translation: AAC23397.1. BC007846 mRNA. Translation: AAH07846.1.
IPI	IPI00784651.
RefSeq	NP_037534.3. NM_013402.4.
UniGene	Hs.503546.
3D structure databases
HSSP	HSSP built from PDB template 1B5M based on UniProtKB P04166.
ProteinModelPortal	O60427.
SMR	O60427. Positions 15-98.
ModBase	Search...
Protein-protein interaction databases
STRING	O60427.
Proteomic databases
PRIDE	O60427.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000350997; ENSP00000322229; ENSG00000149485. ENST00000412725; ENSP00000396367; ENSG00000149485.
GeneID	3992.
KEGG	hsa:3992.
UCSC	uc001nsi.1. human.
Organism-specific databases
CTD	3992.
GeneCards	GC11M061567.
H-InvDB	HIX0009700.
HGNC	HGNC:3574. FADS1.
HPA	HPA042705.
MIM	606148. gene.
neXtProt	NX_O60427.
PharmGKB	PA27973.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04626.
GeneTree	ENSGT00510000046574.
HOVERGEN	HBG002839.
InParanoid	O60427.
OrthoDB	EOG4G7BZ9.
PhylomeDB	O60427.
Enzyme and pathway databases
Reactome	REACT_22258. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	O60427.
Bgee	O60427.
Genevestigator	O60427.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR012171. Fatty_acid/sphinglp_desaturase. IPR005804. Fatty_acid_desaturase-1. [Graphical view]
Gene3D	G3DSA:3.10.120.10. Cyt_B5. 1 hit.
KO	K10224.
Pfam	PF00173. Cyt-b5. 1 hit. PF00487. FA_desaturase. 1 hit. [Graphical view]
PIRSF	PIRSF015921. FA_sphinglp_des. 1 hit.
PRINTS	PR00363. CYTOCHROMEB5.
SUPFAM	SSF55856. Cyt_B5. 1 hit.
PROSITE	PS00191. CYTOCHROME_B5_1. False negative. PS50255. CYTOCHROME_B5_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00132. Alpha-Linolenic Acid. DB00159. Icosapent.
NextBio	15660.
SOURCE	Search...

Entry information

Entry name

FADS1_HUMAN

Accession

Primary (citable) accession number: O60427
Secondary accession number(s): B2RAI0 , Q53GM5, Q8N3A6, Q8NCC7, Q8NCG0, Q96I39, Q96SV3, Q96T10, Q9NRP8, Q9NYX1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.