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UniProtKB/Swiss-Prot entry O60427


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FADS1_HUMAN
Primary accession number O60427
Secondary accession numbers B2RAI0 Q53GM5 Q8N3A6 Q8NCC7 Q8NCG0 Q96I39 Q96SV3 Q96T10 Q9NRP8 Q9NYX1
Integrated into Swiss-Prot on October 2, 2007
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 58)
Name and origin of the protein
Protein name Fatty acid desaturase 1
Synonyms EC 1.14.19.-
Delta(5) fatty acid desaturase
Delta(5) desaturase
D5D
Gene name
Name: FADS1
Synonyms: FADSD5
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
DOI=10.1074/jbc.274.52.37335; PubMed=10601301 [NCBI, ExPASy, EBI, Israel, Japan]
Cho H.P., Nakamura M., Clarke S.D.;
"Cloning, expression, and fatty acid regulation of the human Delta-5 desaturase.";
J. Biol. Chem. 274:37335-37339(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
TISSUE=Liver;
DOI=10.1042/0264-6021:3470719; PubMed=10769175 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"cDNA cloning and characterization of human Delta5-desaturase involved in the biosynthesis of arachidonic acid.";
Biochem. J. 347:719-724(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Retina;
DOI=10.1006/geno.2000.6196; PubMed=10860662 [NCBI, ExPASy, EBI, Israel, Japan]
Marquardt A., Stoehr H., White K., Weber B.H.;
"cDNA cloning, genomic structure, and chromosomal localization of three members of the human fatty acid desaturase family.";
Genomics 66:175-183(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Melanoma;
The German cDNA consortium;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04632; PubMed=16554811 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Human chromosome 11 DNA sequence and analysis including novel gene identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-272.
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF199596; AAF29378.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF226273; AAF70457.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF084558; AAG23120.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL512760; CAC21679.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL834479; CAD39138.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027427; BAB55103.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027522; BAB55173.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK074754; BAC11182.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK074819; BAC11229.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222906; BAD96626.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK314199; BAG36877.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004770; AAC23397.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007846; AAH07846.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_037534.2; -.
UniGene Hs.503546
3D structure databases
HSSP P04166; 1B5M. [HSSP ENTRY / PDB]
ModBase O60427.
Protein-protein interaction databases
IntAct O60427; 3.
PTM databases
PhosphoSite O60427; -.
Organism-specific databases
GeneCards GC11M061323; -.
HGNC HGNC:3574; FADS1.
GenAtlas FADS1.
MIM 606148; gene. [NCBI / EBI]
PharmGKB PA27973; -.
GeneCards O60427.
Gene expression databases
ArrayExpress O60427; -.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (non-traceable author statement from UniProtKB).
GO:0005792; Cellular component: microsome (non-traceable author statement from UniProtKB).
GO:0000248; Molecular function: C-5 sterol desaturase activity (traceable author statement from ProtInc).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007267; Biological process: cell-cell signaling (non-traceable author statement from UniProtKB).
GO:0009267; Biological process: cellular response to starvation (inferred from direct assay from UniProtKB).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0046456; Biological process: icosanoid biosynthetic process (traceable author statement from UniProtKB).
GO:0008654; Biological process: phospholipid biosynthetic process (traceable author statement from UniProtKB).
GO:0045595; Biological process: regulation of cell differentiation (non-traceable author statement from UniProtKB).
GO:0045449; Biological process: regulation of transcription (non-traceable author statement from UniProtKB).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
GO:0006636; Biological process: unsaturated fatty acid biosynthetic process (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001199; Cyt_B5.
IPR012171; Fatty_acid/sphinglp_desaturase.
IPR005804; Fatty_acid_desaturase-1.
Graphical view of domain structure.
Gene3D G3DSA:3.10.120.10; Cyt_B5; 1.
Pfam PF00173; Cyt-b5; 1.
PF00487; FA_desaturase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF015921; FA_sphinglp_des; 1.
PRINTS PR00363; CYTOCHROMEB5.
ProDom PD000612; Cyt_B5; 1.
PD001081; FA_desat_sub; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00191; CYTOCHROME_B5_1; FALSE_NEG.
PS50255; CYTOCHROME_B5_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE O60427; -.
Genome annotation databases
Ensembl ENSG00000149485; Homo sapiens. [Contig view]
GeneID 3992; -.
KEGG hsa:3992; -.
Phylogenomic databases
HOVERGEN O60427; -.
Other
DrugBank DB00132; Alpha-Linolenic Acid.
DB00159; Icosapent.
NextBio 15660; -.
SOURCE FADS1; Homo sapiens.
ProtoNet O60427.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Electron transport; Endoplasmic reticulum; Fatty acid biosynthesis; Lipid synthesis; Membrane; Oxidoreductase; Polymorphism; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   444  444     Fatty acid desaturase 1. PRO_0000307096
TOPO_DOM   1   121  121     Cytoplasmic (Potential). 
TRANSMEM   122   142  21     Potential. 
TOPO_DOM   143   145  3     Lumenal (Potential). 
TRANSMEM   146   170  25     Potential. 
TOPO_DOM   171   267  97     Cytoplasmic (Potential). 
TRANSMEM   268   288  21     Potential. 
TOPO_DOM   289   305  17     Lumenal (Potential). 
TRANSMEM   306   326  21     Potential. 
TOPO_DOM   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. 
VARIANT   272   272  1     P -> S (in dbSNP:rs17856235 [NCBI]). VAR_035340 
CONFLICT   6     6        V -> L (in Ref. 1; AAF29378). 
CONFLICT   9     9        E -> G (in Ref. 5; BAB55103). 
CONFLICT   15    15        P -> L (in Ref. 1; AAF29378). 
CONFLICT   100   100        F -> L (in Ref. 5; BAC11182). 
CONFLICT   143   143        D -> E (in Ref. 5; BAC11182). 
CONFLICT   180   180        D -> G (in Ref. 6; BAD96626). 
CONFLICT   212   212        W -> R (in Ref. 5; BAB55173). 
CONFLICT   213   213        N -> S (in Ref. 5; BAC11182). 
CONFLICT   255   255        K -> N (in Ref. 1; AAF29378). 
CONFLICT   319   319        F -> L (in Ref. 5; BAB55103). 
CONFLICT   361   361        Q -> L (in Ref. 2; AAF70457). 
CONFLICT   381   381        F -> S (in Ref. 5; BAC11229). 
CONFLICT   410   410        H -> R (in Ref. 2; AAF70457). 
CONFLICT   431   431        K -> E (in Ref. 5; BAC11229). 
Sequence information
Length: 444 AA [This is the length of the unprocessed precursor] Molecular weight: 51964 Da [This is the MW of the unprocessed precursor] CRC64: CC3C28D82AA49BF2 [This is a checksum on the sequence]
        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 

O60427 in FASTA format

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