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P36189

- FAS_ANSAN

UniProt

P36189 - FAS_ANSAN

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Protein

Fatty acid synthase

Gene

FASN

Organism
Anser anser anser (Western graylag goose)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO2 + 2n NADP+.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611For beta-ketoacyl synthase activityPROSITE-ProRule annotation

GO - Molecular functioni

  1. fatty acid synthase activity Source: UniProtKB-EC
  2. hydrolase activity Source: UniProtKB-KW
  3. ligase activity Source: UniProtKB-KW
  4. oxidoreductase activity Source: UniProtKB-KW

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Oxidoreductase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase (EC:2.3.1.85)
Gene namesi
Name:FASN
Synonyms:FAS
OrganismiAnser anser anser (Western graylag goose)
Taxonomic identifieri8844 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnser

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›352›352Fatty acid synthasePRO_0000180272Add
BLAST

Keywords - PTMi

Phosphopantetheine

Proteomic databases

PRIDEiP36189.

Expressioni

Inductioni

By triiodothyronine.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP36189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – ›352›352Beta-ketoacyl synthaseAdd
BLAST

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 1 hit.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P36189-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEDVVIAGIA GKLPESENLQ EFWEKLLNGV DMVTEDDRRW KPGMYGLPKR
60 70 80 90 100
NGKLKDISKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPATL
110 120 130 140 150
RGTDTGVWVG ASGSEAGEAF SQDPEQLLGY SMIGCQRAMF ANRISYFYDF
160 170 180 190 200
KGPSLSIDTA CSSSLMALEN AYKAIRNGRC SAAVVGGVNL LLKPNTSVQF
210 220 230 240 250
MKLGMLSPDG ACKVFDASGD GYCRSEAVVV VLLTKKSMAK RIYATIVNAG
260 270 280 290 300
SNTDGFKEQG VTFPSGDMQR QLVSSLHREC GIKPGDIEYV ETHGTGTKVG
310 320 330 340 350
DPQEVNGLAD LFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVVLSLEH

GL
Length:352
Mass (Da):37,912
Last modified:June 1, 1994 - v1
Checksum:i908530BF76762335
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei352 – 3521

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60622 mRNA. Translation: AAA49316.1.
PIRiA39042.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60622 mRNA. Translation: AAA49316.1 .
PIRi A39042.

3D structure databases

ProteinModelPortali P36189.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P36189.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.47.10. 2 hits.
InterProi IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view ]
SUPFAMi SSF53901. SSF53901. 1 hit.
PROSITEi PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiFAS_ANSAN
AccessioniPrimary (citable) accession number: P36189
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 1, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Multifunctional enzyme

External Data

Dasty 3