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0FAS_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameFASN
DescriptionFatty acid synthase (ec 2.3.1.85) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0006631 fatty acid metabolism (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Beta-ketoacyl-ACP synthase () (KAS) is the enzyme that catalyzesthe condensation of malonyl-ACP with the growing fatty acid chain. It is found as a componentof a number of enzymatic systems.ncluding fatty acid synthetase (FAS).hich catalyzes theformation of long-chain fatty acids from acetyl-CoA.alonyl-CoA and NADPH; the multi-functional 6-methysalicylic acid synthase (MSAS) from Penicillium patulum .hich isinvolved in the biosynthesis of a polyketide antibiotic; polyketide antibiotic synthase enzymesystems; Emericella nidulans multifunctional protein Wa.hich is involved in the biosynthesisof conidial green pigment; Rhizobium nodulation protein nodE.hich probably acts as a beta-ketoacyl synthase in the synthesis of the nodulation Nod factor fatty acyl chain; and yeastmitochondrial protein CEM1. The condensation reaction is a two step process.irst the acylcomponent of an activated acyl primer is transferred to a cysteine residue of the enzyme andis then condensed with an activated malonyl donor with the concomitant release of carbondioxide.
  IPR000794:Beta-ketoacyl synthase
Thioesterase domains often occur integrated in or associated with peptide synthetaseswhich are involved in the non-ribosomal synthesis of peptide antibiotics .Thioesterases are required for the addition of the last amino acid to the peptideantibiotic.hereby forming a cyclic antibiotic. Next to the operons encoding theseenzymes.n almost all cases.re genes that encode proteins that have similarity tothe type II fatty acid thioesterases of vertebrates.
  IPR001031:Thioesterase
The short-chain dehydrogenases/reductases family (SDR) is a very large family of enzymes.ost of which are known to be NAD- or NADP-dependent oxidoreductases. As the first member of this family to be characterized was Drosophila alcohol dehydrogenase.his family used to be called insect-type.r short-chain alcohol dehydrogenases. Most member of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least 2 domains .he first binding the coenzyme.ften NAD.nd the second binding the substrate. This latter domain determines the substrate specificity and contains amino acids involved in catalysis. Little sequence similarity has been found in the coenzyme binding domain although there is a large degree of structural similarity.nd it has therefore been suggested that the structure of dehydrogenases has arisen through gene fusion of a common ancestral coenzyme nucleotide sequence with various substrate specific domains .
  IPR002198:Short-chain dehydrogenase/reductase SDR
Alcohol dehydrogenase () (ADH) catalyzes the reversible oxidation ofalcohols to their corresponding acetaldehyde or ketone with the concomitant reduction of NAD:alcohol + NAD = aldehyde or ketone + NADHCurrently three structurally and catalytically different types of alcoholdehydrogenases are known:Zinc-containing long-chain alcohol dehydrogenases.Insect-type.r short-chain alcohol dehydrogenases.Iron-containing alcohol dehydrogenases.Zinc-containing ADHs .re dimeric or tetrameric enzymes that bind twoatoms of zinc per subunit. One of the zinc atom is essential for catalyticactivity while the other is not. Both zinc atoms are coordinated by eithercysteine or histidine residues; the catalytic zinc is coordinated by twocysteines and one histidine. Zinc-containing ADHs are found in bacteria.ammals.lants.nd in fungi. In many species there is more than one isozyme(for example.umans have at least six isozymes.east have three.tc.). Anumber of other zinc-dependent dehydrogenases are closely related to zincADH and are included in this family.Sorbitol dehydrogenase ()L-threonine 3-dehydrogenase ()Glutathione-dependent formaldehyde dehydrogenase ()Mannitol dehydrogenase () In addition.his family includes NADP-dependent quinone oxidoreductase ().n enzyme found in bacteria (gene qor).n yeast and in mammals where.n somespecies such as rodents.t has been recruited as an eye lens protein and isknown as zeta-crystallin . The sequence of quinone oxidoreductase isdistantly related to that other zinc-containing alcohol dehydrogenases and itlacks the zinc-ligand residues. The torpedo fish and mammalian synaptic vesiclemembrane protein vat-1 is related to qor.This entry represents the cofactor-binding domain of these enzymes.hich is mornally found towards the C-terminus. Structural studies indicate that it forms a classical Rossman fold that reversibly binds NAD(H) .
  IPR013149:Alcohol dehydrogenase, zinc-binding
Phosphopantetheine (or pantetheine 4 phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a swinging arm for the attachment of activated fatty acid and amino-acid groups . The amino-terminal region of the ACP proteins is well defined and consists of alpha four helices arranged in a right-handedbundle held together by interhelical hydrophobic interactions. The Asp-Ser-Leu (DSL)motif is conserved in all of the ACP sequences.nd the 4-PP prosthetic group is covalently linkedvia a phosphodiester bond to the serine residue. The DSL sequence is present at the amino terminus of helix II. domain of the protein referred to as the recognition helix and which is responsible for theinteraction of ACPs with the enzymes of type II fatty acid synthesis .
  IPR006163:Phosphopantetheine-binding
Methyl transfer from the ubiquitous donor S-adenosyl-L-methionine (SAM) to either nitrogen.xygen or carbon atoms is frequently employed in diverse organisms ranging from bacteria to plants and mammals. The reaction is catalyzed by methyltransferases (Mtases) and modifies DNA.NA.roteins and small molecules.uch as catechol for regulatory purposes. The various aspects of the role of DNA methylation in prokaryotic restriction-modification systems and in a number of cellular processes in eukaryotes including gene regulation and differentiation is well documented.This entry represents a methyltransferase domain found in a large variety of SAM-dependent methyltransferases including.ut not limited to:Hexaprenyldihydroxybenzoate methyltransferase (). mitochodrial enzyme involved in ubiquinone biosynthesis Fatty acid synthase (). biosynthetic enzyme catalysing the formation of long-chain fatty acidsGlycine N-methyltransferase () which catalyses the SAM-dependent methylation of glycine to form sarcosine and may play a role in regulating the methylation potential of the cell Enniatin synthetase.nvolved in non-ribosomal biosynthesis of cyclohexadepsipeptidase.nniatin Histamine N-methyltransferase (). SAM-dependent histamine-inactivating enzyme A probable cobalt-precorrin-6Y C(15)-methyltransferase thought to be involved in adenosylcobalamin biosynthesis Structural studies show that this domain forms the Rossman-like alpha-beta fold typical of SAM-dependent methyltransferases .
  IPR013217:Methyltransferase type 12
Enzymes like bacterial malonyl CoA-acly carrier protein transacylase () and eukaryotic fatty acid synthase () that are involved in fatty acidbiosynthesis belong to this group. Also included are the polyketide synthases 6-methylsalicylic acid synthase (). multifunctional enzyme that involvedin the biosynthesis of patulin and conidial green pigment synthase ().
  IPR001227:Acyl transferase region
Acyl carrier protein (ACP) is an essential cofactor in the synthesis of fatty acids by the fatty acid synthetases systems in bacteria and plants. In addition to fatty acid synthesis.CP is also involved in many other reactions that require acyl transfer steps.uch as the synthesis of polyketide antibiotics.iotin precursor.embrane-derived oligosaccharides.nd activation of toxins.nd functions as an essential cofactor in lipoylation of pyruvate and alpha-ketoglutarate dehydrogenase complexes . The core structure of ACP consists of a four-helical bundle.here helix three is shorter than the others.Several other proteins share structural homology with ACP.uch as the bacterial apo-D-alanyl carrier protein.hich facilitates the incorporation of D-alanine into lipoteichoic acid by a ligase.ecessary for the growth and development of Gram-positive organisms ; and the thioester domain of the bacterial peptide carrier protein found within large modular non-ribosomal peptide synthetases.hich are responsible for the synthesis of a variety of microbial bioactive peptides .
  IPR009081:Acyl carrier protein-like
GroES (chaperonin 10) is an oligomeric molecular chaperone.hich functions in protein folding and possibly in intercellular signalling.eing found on the surface of various prokaryotic and eukaryotic cells.s well as being released from cells. Secreted chaperonins are thought to act as intercellular signals.nteracting with a variety of cell types.ncluding leukocytes.ascular endothelial cells and epithelial cells.s well as activating key cellular activities such as the synthesis of cytokines and adhesion proteins . GroES works as a co-chaperone with GroEL (chaperonin 60) during protein folding. The polypeptide substrate is captured by GroEL.hich bind the co-chaperone GroES and ATP.nd discharges the substrate into a unique microenvironment inside of the chaperone.hich promotes productive folding. After hydrolysis of ATP.he polypeptide is released into solution . GP31 from bacteriophage T4 is functionally equivalent to GroES. GroES folds as a partly opened beta-barrel.The N-terminal domain of alcohol dehydrogenase-like proteins have a GroES-like fold.he C-terminal domain having a classical Rossman-fold . These proteins include.lcohol dehydrogenase.hich contains a zinc-finger subdomain within the GroES-like domain.etose reductase (sorbitol dehydrogenase).ormaldehyde dehydrogenase.uinone oxidoreductase and 2.-dienoyl-CoA reductase.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011032:GroES-like
IPR001227:Acyl_transf_1 
Evalue:-160.53759765625 
Location:493-810IPR000794:ketoacyl-synt 
Evalue:-96.408935546875 
Location:2-239IPR001031:Thioesterase 
Evalue:-70.3187561035156 
Location:2242-2501IPR002198:adh_short 
Evalue:-63.6382713317871 
Location:1885-2053IPR000794:Ketoacyl-synt_C 
Evalue:-51.5086364746094 
Location:243-360IPR013149:ADH_zinc_N 
Evalue:-23.8538722991943 
Location:1667-1816IPR006163:PP-binding 
Evalue:-13.2146701812744 
Location:2125-2191IPR013217:Methyltransf_12 
Evalue:-11.5376024246216 
Location:1243-1342IPR011032:GroES_like 
Evalue:0 
Location:1559-1665
SequencesProtein: FAS_HUMAN (2511 aa)
mRNA: NM_004104
Local Annotation
Synapse Ontology
Microglias, one kind of glias in CNS, are responsible for removing most of the waste and cellular debris from the CNS
sdb:0267 removing metabolic mass  (Evidence:keywords)
KO assignmentK00059
  Level 3 annotation:
    3-oxoacyl-[acyl-carrier protein] reductase
  Level 2 annotation:
    Fatty acid biosynthesis
K00209
  Level 3 annotation:
    enoyl-[acyl-carrier-protein] reductase (NADPH2, B-specific)
  Level 2 annotation:
    Fatty acid biosynthesis
K00644
  Level 3 annotation:
    [acyl-carrier-protein] S-acetyltransferase
  Level 2 annotation:
    Fatty acid biosynthesis
K00645
  Level 3 annotation:
    [acyl-carrier-protein] S-malonyltransferase
  Level 2 annotation:
    Fatty acid biosynthesis
K00646
  Level 3 annotation:
    3-oxoacyl-[acyl-carrier-protein] synthase
  Level 2 annotation:
    Fatty acid biosynthesis
K00665
  Level 3 annotation:
    fatty-acid synthase
  Level 2 annotation:
    Fatty acid biosynthesis
    Insulin signaling pathway
K01071
  Level 3 annotation:
    oleoyl-[acyl-carrier-protein] hydrolase
  Level 2 annotation:
    Fatty acid biosynthesis
K01717
  Level 3 annotation:
    3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
  Level 2 annotation:
    Fatty acid biosynthesis
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 315 residues, 77629503-77630445Exon2: 86 residues, 77630521-77630773Exon3: 35 residues, 77631304-77631403Exon4: 75 residues, 77631534-77631755Exon5: 79 residues, 77631856-77632087Exon6: 65 residues, 77632328-77632517Exon7: 83 residues, 77632765-77633008Exon8: 52 residues, 77633173-77633325Exon9: 32 residues, 77633487-77633579Exon10: 52 residues, 77633691-77633843Exon11: 69 residues, 77634078-77634280Exon12: 76 residues, 77634366-77634590Exon13: 43 residues, 77634681-77634804Exon14: 42 residues, 77634936-77635056Exon15: 61 residues, 77635139-77635318Exon16: 52 residues, 77635398-77635549Exon17: 70 residues, 77635677-77635881Exon18: 53 residues, 77635963-77636118Exon19: 42 residues, 77636199-77636321Exon20: 57 residues, 77636402-77636567Exon21: 132 residues, 77636646-77637036Exon22: 103 residues, 77637418-77637723Exon23: 70 residues, 77638214-77638418Exon24: 62 residues, 77638489-77638669Exon25: 61 residues, 77638849-77639026Exon26: 29 residues, 77639118-77639199Exon27: 66 residues, 77639280-77639472Exon28: 59 residues, 77639554-77639727Exon29: 40 residues, 77639925-77640041Exon30: 70 residues, 77640133-77640337Exon31: 47 residues, 77640414-77640549Exon32: 33 residues, 77640796-77640891Exon33: 65 residues, 77641539-77641729Exon34: 64 residues, 77642046-77642234Exon35: 156 residues, 77642386-77642849Exon36: 47 residues, 77643619-77643754Exon37: 40 residues, 77643861-77643977Exon38: 43 residues, 77644061-77644184Exon39: 69 residues, 77644383-77644584Exon40: 60 residues, 77644762-77644936Exon41: 53 residues, 77646484-77646637Exon42: 46 residues, 77647483-77647617Exon43: 38 residues, 77649285-77649395Exon44: 2 residues, -Jump to FAS_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4323 76816673-76827450 ~-11K 16811(-)Loci: 4324 77091593-77094422 ~-3K 16823(ACTG1)(-)Loci: 3047 77261424-77279550 ~-18K 16838(HGS)(+)Loci: 3048 77451912-77454066 ~-2K 16852(NPB)(+)Loci: 3049 77603051-77608635 ~-6K 16881(GPS1)(+)Loci: 4325 77629503-77649395 ~-20K 16888(FASN)(-)Loci: 4326 77795530-77824862 ~-29K 16893(CSNK1D)(-)Loci: 4327 78208237-78249802 ~-42K 16919(RAB40B)(-)Loci: 3046 76623556-76705827 ~-82K 16801(BAIAP2)(+)Link out to UCSC