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Reviewed, UniProtKB/Swiss-Prot P49327 (FAS_HUMAN)

Last modified November 25, 2008. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Fatty acid synthase
    EC=2.3.1.85
Including the following 7 domains:
    1- Recommended name:
            [Acyl-carrier-protein] S-acetyltransferase
              EC=2.3.1.38
    2- Recommended name:
            [Acyl-carrier-protein] S-malonyltransferase
              EC=2.3.1.39
    3- Recommended name:
            3-oxoacyl-[acyl-carrier-protein] synthase
              EC=2.3.1.41
    4- Recommended name:
            3-oxoacyl-[acyl-carrier-protein] reductase
              EC=1.1.1.100
    5- Recommended name:
            3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
              EC=4.2.1.61
    6- Recommended name:
            Enoyl-[acyl-carrier-protein] reductase
              EC=1.3.1.10
    7- Recommended name:
            Oleoyl-[acyl-carrier-protein] hydrolase
              EC=3.1.2.14
Gene names
Name: FASN
Synonyms: FAS
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length2511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.

Catalytic activity

Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO(2) + 2n NADP(+).

Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].

Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H(2)O.

Acyl-[acyl-carrier-protein] + NADP(+) = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH.

Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate.

Subunit structure

Homodimer which is arranged in a head to tail fashion.

Subcellular location

Cytoplasm. Melanosome. Note= Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Tissue specificity

Ubiquitous. Prominent expression in brain, lung, and liver.

Miscellaneous

The relatively low beta-ketoacyl synthase activity may be attributable to the low 4'-phosphopantetheine content of the protein.

Sequence similarities

Contains 1 acyl carrier domain.

Sequence caution

The sequence AAC50259.1 differs from that shown. Reason: Miscellaneous discrepancy. Several sequencing errors.

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Ontologies

Keywords

   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentCytoplasm
   LigandNAD
NADP
Phosphopantetheine
Pyridoxal phosphate
   Molecular functionHydrolase
Lyase
Oxidoreductase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing
Multifunctional enzyme

Gene Ontology (GO)

   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytosol Ref.1

Inferred from Experiment. Source: Reactome

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity

Inferred from electronic annotation. Source: EC

3-oxoacyl-[acyl-carrier-protein] reductase activity Ref.1

Inferred from electronic annotation. Source: EC

3-oxoacyl-[acyl-carrier-protein] synthase activity Ref.1

Inferred from electronic annotation. Source: EC

[acyl-carrier-protein] S-acetyltransferase activity Ref.1

Inferred from electronic annotation. Source: EC

[acyl-carrier-protein] S-malonyltransferase activity Ref.1

Inferred from electronic annotation. Source: EC

acyl carrier activity

Inferred from electronic annotation. Source: InterPro

cofactor binding

Inferred from electronic annotation. Source: InterPro

enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Ref.1

Inferred from electronic annotation. Source: EC

oleoyl-[acyl-carrier-protein] hydrolase activity Ref.1

Inferred from electronic annotation. Source: EC

phosphopantetheine binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

NDRG1Q925971EBI-356658,EBI-716486

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25112511Fatty acid synthase
PRO_0000180276

Regions

Domain2123 – 217957Acyl carrier
Nucleotide binding1671 – 168818NADP (ER) By similarity
Nucleotide binding1886 – 190116NADP (KR) By similarity
Region1 – 414414Beta-ketoacyl synthase By similarity
Region429 – 817389Acyl and malonyl transferases By similarity
Region1635 – 1863229Enoyl reductase By similarity
Region1864 – 2118255Beta-ketoacyl reductase By similarity
Region2207 – 2511305Thioesterase By similarity

Sites

Active site1611For beta-ketoacyl synthase activity By similarity
Active site5811For malonyltransferase activity By similarity
Active site8781For beta-hydroxyacyl dehydratase activity By similarity
Active site23081For thioesterase activity By similarity
Active site24811For thioesterase activity By similarity
Binding site17041Pyridoxal phosphate (covalent) By similarity
Binding site21561Phosphopantetheine (covalent) By similarity

Amino acid modifications

Modified residue11N-acetylmethionine
Modified residue2071Phosphoserine
Modified residue21981Phosphoserine
Modified residue22041Phosphothreonine
Modified residue22361Phosphoserine

Experimental info

Sequence conflict459 – 4624AVPA → LSPT in AAA73576. Ref.2
Sequence conflict528 – 5292KP → NR in AAA73576. Ref.2
Sequence conflict6371G → A in AAA73576. Ref.2
Sequence conflict8011G → R in AAA73576. Ref.2
Sequence conflict9021A → P in AAA73576. Ref.2
Sequence conflict9581V → M in AAS09886. Ref.3
Sequence conflict11211P → S Ref.2 Ref.3
Sequence conflict11511T → K Ref.2 Ref.3
Sequence conflict1353 – 13564LGDI → SGH in AAA73576. Ref.2
Sequence conflict13861L → V in AAA73576. Ref.2
Sequence conflict1467 – 14682NR → T in AAA73576. Ref.2
Sequence conflict18271K → E in AAS09886. Ref.3
Sequence conflict19341R → A in AAA73576. Ref.2
Sequence conflict20651D → H Ref.7
Sequence conflict20871R → A in AAA73576. Ref.2
Sequence conflict23631A → P Ref.7
Sequence conflict24281R → G in AAA73576. Ref.2
Sequence conflict24531A → T Ref.7
Sequence conflict24561E → Q Ref.7

Secondary structure

1 ...................................................................................................................... 2511
Helix Strand Turn

Details...