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P36189 (FAS_ANSAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid synthase

EC=2.3.1.85
Gene names
Name:FASN
Synonyms:FAS
OrganismAnser anser anser (Western graylag goose)
Taxonomic identifier8844 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnser

Protein attributes

Sequence length352 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

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 seven 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 CO2 + 2n NADP+.

Subunit structure

Homodimer which monomers are arranged in a head to tail fashion.

Induction

By triiodothyronine.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›352›352Fatty acid synthase
PRO_0000180272

Regions

Region1 – ›352›352Beta-ketoacyl synthase

Sites

Active site1611For beta-ketoacyl synthase activity By similarity

Experimental info

Non-terminal residue3521

Sequences

Sequence LengthMass (Da)Tools
P36189 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 908530BF76762335

FASTA35237,912
        10         20         30         40         50         60 
MEDVVIAGIA GKLPESENLQ EFWEKLLNGV DMVTEDDRRW KPGMYGLPKR NGKLKDISKF 

        70         80         90        100        110        120 
DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPATL RGTDTGVWVG ASGSEAGEAF 

       130        140        150        160        170        180 
SQDPEQLLGY SMIGCQRAMF ANRISYFYDF KGPSLSIDTA CSSSLMALEN AYKAIRNGRC 

       190        200        210        220        230        240 
SAAVVGGVNL LLKPNTSVQF MKLGMLSPDG ACKVFDASGD GYCRSEAVVV VLLTKKSMAK 

       250        260        270        280        290        300 
RIYATIVNAG SNTDGFKEQG VTFPSGDMQR QLVSSLHREC GIKPGDIEYV ETHGTGTKVG 

       310        320        330        340        350 
DPQEVNGLAD LFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVVLSLEH GL 

« Hide

References

[1]"Isolation and partial characterization of the gene for goose fatty acid synthase."
Kameda K., Goodridge A.G.
J. Biol. Chem. 266:419-426(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Specific modification of the condensation domain of fatty acid synthase and the determination of the primary structure of the modified active site peptides."
Pouloe A.J., Bonsall R.F., Kolattukudy P.E.
Arch. Biochem. Biophys. 230:117-128(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 152-173.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60622 mRNA. Translation: AAA49316.1.
PIRA39042.

3D structure databases

ProteinModelPortalP36189.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP36189.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.47.10. 2 hits.
InterProIPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. SSF53901. 1 hit.
PROSITEPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFAS_ANSAN
AccessionPrimary (citable) accession number: P36189
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program