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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	501 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.7 Ref.8
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.3 Ref.7 Ref.8
Developmental stage	Highly expressed in fetal liver and fetal brain. Ref.7 Ref.8
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.
Caution	It is uncertain whether Met-1 or Met-58 is the initiator.
Sequence caution	The sequence AAC23397.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAG23120.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH07846.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB55103.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB55173.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAD96626.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAG36877.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAC21679.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Electron transport Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism 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	aging Inferred from electronic annotation. Source: Compara alpha-linolenic acid metabolic process Traceable author statement. Source: Reactome arachidonic acid metabolic process Inferred from electronic annotation. Source: Compara cell-cell signaling Non-traceable author statement Ref.7. Source: UniProtKB cellular response to starvation Inferred from direct assay Ref.7. Source: UniProtKB electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW icosanoid biosynthetic process Traceable author statement Ref.7. Source: UniProtKB linoleic acid metabolic process Traceable author statement. Source: Reactome phospholipid biosynthetic process Traceable author statement Ref.7. Source: UniProtKB regulation of cell differentiation Non-traceable author statement Ref.7. Source: UniProtKB regulation of transcription, DNA-dependent Non-traceable author statement Ref.7. Source: UniProtKB response to insulin stimulus Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from electronic annotation. Source: Compara response to sucrose stimulus Inferred from electronic annotation. Source: Compara response to vitamin A Inferred from electronic annotation. Source: Compara unsaturated fatty acid biosynthetic process Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Non-traceable author statement Ref.7. Source: UniProtKB nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	C-5 sterol desaturase activity Traceable author statement Ref.7. Source: ProtInc heme binding Inferred from electronic annotation. Source: InterPro iron ion 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 – 501	501	Fatty acid desaturase 1		PRO_0000307096
Regions
	Topological domain	58 – 178	121	Cytoplasmic Potential
	Transmembrane	179 – 199	21	Helical; Potential
	Topological domain	200 – 202	3	Lumenal Potential
	Transmembrane	203 – 227	25	Helical; Potential
	Topological domain	228 – 324	97	Cytoplasmic Potential
	Transmembrane	325 – 345	21	Helical; Potential
	Topological domain	346 – 362	17	Lumenal Potential
	Transmembrane	363 – 383	21	Helical; Potential
	Topological domain	384 – 501	118	Cytoplasmic Potential
	Domain	74 – 151	78	Cytochrome b5 heme-binding
	Motif	236 – 240	5	Histidine box-1
	Motif	273 – 277	5	Histidine box-2
	Motif	439 – 443	5	Histidine box-3
Natural variations
	Natural variant	329	1	P → S. Ref.6 Corresponds to variant rs17856235 [ dbSNP | Ensembl ].		VAR_035340
Experimental info
	Sequence conflict	39	1	P → T in BAB55173. Ref.1
	Sequence conflict	63	1	V → L in AAF29378. Ref.7
	Sequence conflict	66	1	E → G in BAB55103. Ref.1
	Sequence conflict	72	1	P → L in AAF29378. Ref.7
	Sequence conflict	157	1	F → L in BAC11182. Ref.1
	Sequence conflict	200	1	D → E in BAC11182. Ref.1
	Sequence conflict	237	1	D → G in BAD96626. Ref.5
	Sequence conflict	269	1	W → R in BAB55173. Ref.1
	Sequence conflict	270	1	N → S in BAC11182. Ref.1
	Sequence conflict	312	1	K → N in AAF29378. Ref.7
	Sequence conflict	376	1	F → L in BAB55103. Ref.1
	Sequence conflict	418	1	Q → L in AAF70457. Ref.8
	Sequence conflict	438	1	F → S in BAC11229. Ref.1
	Sequence conflict	467	1	H → R in AAF70457. Ref.8
	Sequence conflict	488	1	K → E in BAC11229. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O60427 [UniParc]. Last modified March 6, 2013. Version 2. Checksum: DB59ACB64C59B329	FASTA	501	57,886
	10 20 30 40 50 60 MGTRAARPAG LPCGAENPAR RRLALGARQQ IHSWSPRTPS TRLTAPAGPA RGVARPAMAP 70 80 90 100 110 120 DPVAAETAAQ GPTPRYFTWD EVAQRSGCEE RWLVIDRKVY NISEFTRRHP GGSRVISHYA 130 140 150 160 170 180 GQDATDPFVA FHINKGLVKK YMNSLLIGEL SPEQPSFEPT KNKELTDEFR ELRATVERMG 190 200 210 220 230 240 LMKANHVFFL LYLLHILLLD GAAWLTLWVF GTSFLPFLLC AVLLSAVQAQ AGWLQHDFGH 250 260 270 280 290 300 LSVFSTSKWN HLLHHFVIGH LKGAPASWWN HMHFQHHAKP NCFRKDPDIN MHPFFFALGK 310 320 330 340 350 360 ILSVELGKQK KKYMPYNHQH KYFFLIGPPA LLPLYFQWYI FYFVIQRKKW VDLAWMITFY 370 380 390 400 410 420 VRFFLTYVPL LGLKAFLGLF FIVRFLESNW FVWVTQMNHI PMHIDHDRNM DWVSTQLQAT 430 440 450 460 470 480 CNVHKSAFND WFSGHLNFQI EHHLFPTMPR HNYHKVAPLV QSLCAKHGIE YQSKPLLSAF 490 500 ADIIHSLKES GQLWLDAYLH Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] OF 32-501, TISSUE SPECIFICITY. Tissue: Retina.
[4]	"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 32-501. Tissue: Melanoma.
[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] OF 44-501. Tissue: Kidney.
[6]	"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] OF 51-501, VARIANT SER-329. Tissue: Brain.
[7]	"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] OF 58-501, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]	"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] OF 58-501, FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK027427 mRNA. Translation: BAB55103.1. Different initiation. AK027522 mRNA. Translation: BAB55173.1. Different initiation. AK074754 mRNA. Translation: BAC11182.1. AK074819 mRNA. Translation: BAC11229.1. AK314199 mRNA. Translation: BAG36877.1. Different initiation. AC004770 Genomic DNA. Translation: AAC23397.1. Different initiation. AF084558 mRNA. Translation: AAG23120.1. Different initiation. AL512760 mRNA. Translation: CAC21679.1. Different initiation. AL834479 mRNA. Translation: CAD39138.1. AK222906 mRNA. Translation: BAD96626.1. Different initiation. BC007846 mRNA. Translation: AAH07846.1. Different initiation. AF199596 mRNA. Translation: AAF29378.1. AF226273 mRNA. Translation: AAF70457.1.
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.
ModBase	Search...
PTM databases
PhosphoSite	O60427.
Proteomic databases
PaxDb	O60427.
PRIDE	O60427.
Protocols and materials databases
DNASU	3992.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000350997; ENSP00000322229; ENSG00000149485.
GeneID	3992.
KEGG	hsa:3992.
UCSC	uc001nsh.3. human.
Organism-specific databases
CTD	3992.
GeneCards	GC11M061567.
HGNC	HGNC:3574. FADS1.
HPA	HPA042705.
MIM	606148. gene.
neXtProt	NX_O60427.
PharmGKB	PA27973.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5274.
HOVERGEN	HBG002839.
InParanoid	O60427.
KO	K10224.
OrthoDB	EOG4G7BZ9.
Enzyme and pathway databases
BioCyc	MetaCyc:HS07617-MONOMER.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00658.
Gene expression databases
ArrayExpress	O60427.
Bgee	O60427.
Genevestigator	O60427.
Family and domain databases
Gene3D	3.10.120.10. 1 hit.
InterPro	IPR001199. Cyt_B5-like_heme/steroid-bd. IPR012171. Fatty_acid/sphinglp_desaturase. IPR005804. Fatty_acid_desaturase-1. [Graphical view]
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
BindingDB	O60427.
ChEMBL	CHEMBL5840.
ChiTaRS	FADS1. human.
DrugBank	DB00132. Alpha-Linolenic Acid. DB00159. Icosapent.
GenomeRNAi	3992.
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:	March 6, 2013
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 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.