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P12276 (FAS_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid synthase

EC=2.3.1.85

Including the following 7 domains:

  1. [Acyl-carrier-protein] S-acetyltransferase
    EC=2.3.1.38
  2. [Acyl-carrier-protein] S-malonyltransferase
    EC=2.3.1.39
  3. 3-oxoacyl-[acyl-carrier-protein] synthase
    EC=2.3.1.41
  4. 3-oxoacyl-[acyl-carrier-protein] reductase
    EC=1.1.1.100
  5. 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
    EC=4.2.1.59
  6. Enoyl-[acyl-carrier-protein] reductase
    EC=1.3.1.39
  7. Oleoyl-[acyl-carrier-protein] hydrolase
    EC=3.1.2.14
Gene names
Name:FASN
Synonyms:FAS
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length2512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 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 CO2 + 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] + CO2 + [acyl-carrier-protein].

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

A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.

An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.

Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.

Subunit structure

Homodimer which is arranged in a head to tail fashion.

Sequence similarities

Contains 1 acyl carrier domain.

Sequence caution

The sequence AAA82106.1 differs from that shown. Reason: Frameshift at position 2352.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Coding sequence diversityAlternative splicing
   LigandNAD
NADP
Pyridoxal phosphate
   Molecular functionHydrolase
Lyase
Oxidoreductase
Transferase
   PTMAcetylation
Phosphopantetheine
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity

Inferred from electronic annotation. Source: InterPro

3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity

Inferred from electronic annotation. Source: UniProtKB-EC

3-oxoacyl-[acyl-carrier-protein] synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

[acyl-carrier-protein] S-acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

[acyl-carrier-protein] S-malonyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity

Inferred from electronic annotation. Source: UniProtKB-EC

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

Inferred from electronic annotation. Source: InterPro

myristoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

oleoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

palmitoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P12276-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: P12276-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2349-2349: T → TQCFSFSLF

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 25122511Fatty acid synthase
PRO_0000180273

Regions

Domain2125 – 218157Acyl carrier
Nucleotide binding1675 – 169218NADP (ER)
Nucleotide binding1889 – 190416NADP (KR)
Region2 – ?412411Beta-ketoacyl synthase
Region427 – 815389Acyl and malonyl transferases
Region1638 – 1866229Enoyl reductase
Region1867 – 2119253Beta-ketoacyl reductase
Region2209 – 2511303Thioesterase

Sites

Active site1611For beta-ketoacyl synthase activity By similarity
Active site5801For acyl/malonyl transferase activity By similarity
Active site8781For beta-hydroxyacyl dehydratase activity By similarity
Active site23091For thioesterase activity By similarity
Active site24821For thioesterase activity By similarity

Amino acid modifications

Modified residue21N-acetylglutamate
Modified residue17081N6-(pyridoxal phosphate)lysine By similarity
Modified residue21581O-(pantetheine 4'-phosphoryl)serine By similarity

Natural variations

Alternative sequence23491T → TQCFSFSLF in isoform 1.
VSP_000149

Experimental info

Sequence conflict78 – 792QL → PV in AAA48767. Ref.2
Sequence conflict1171L → A in AAA48767. Ref.2
Sequence conflict6761R → S in AAA48767. Ref.2
Sequence conflict11701K → N in AAA48767. Ref.2
Sequence conflict11791A → T in AAA48767. Ref.2
Sequence conflict11921R → H in AAA48767. Ref.2
Sequence conflict11991P → L in AAA48767. Ref.2
Sequence conflict1287 – 12882DN → ND in AAA48767. Ref.2
Sequence conflict13731K → E in AAA48767. Ref.2
Sequence conflict15341C → Y in AAA48767. Ref.2
Sequence conflict15781W → R in AAA48767. Ref.2
Sequence conflict1686 – 169712QAAIA…LSMGC → ASSHCHRLEHGLA in AAA48767. Ref.2
Sequence conflict17331Q → E in AAA48767. Ref.2
Sequence conflict17461S → N in AAA48767. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 66FDE22F5CCF603C

FASTA2,512274,782
        10         20         30         40         50         60 
MEDVVIAGIA GKLPESENLQ EFWENLLNGV DMVTEDDRRW KPGIYGLPKR NGKLKDIKKF 

        70         80         90        100        110        120 
DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPTAL RGTDTGVWVG ASGSEALEAL 

       130        140        150        160        170        180 
SQDPEELLGY SMTGCQRAML ANRISYFYDF TGPSLTIDTA CSSSLMALEN AYKAIRHGQC 

       190        200        210        220        230        240 
SAALVGGVNI LLKPNTSVQF MKLGMLSPDG ACKAFDVSGN GYCRSEAVVV VLLTKKSMAK 

       250        260        270        280        290        300 
RVYATIVNAG SNTDGFKEQG VTFPSGEMQQ QLVGSLYREC GIKPGDVEYV EAHGTGTKVG 

       310        320        330        340        350        360 
DPQEVNGIVN VFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVILSLEH GLWAPNLHFN 

       370        380        390        400        410        420 
DPNPDIPALH DGSLKVVCKP TPVKGGLVSI NSFGFGGSNA HVILRPNEKK CQPQETCNLP 

       430        440        450        460        470        480 
RLVQVCGRTQ EAVEILIEES RKHGGCSPFL SLLSDISAVP VSSMPYRGYT LVGTESDITE 

       490        500        510        520        530        540 
IQQVQASGRP LWYICSGMGT QWKGMGLSLM KLDLFRQSIL RSDEALKSTG LKVSDLLLNA 

       550        560        570        580        590        600 
DENTFDDTVH AFVGLAAIQI AQIDVLKAAG LQPDGILGHS VGELACGYAD NSLSHEEAVL 

       610        620        630        640        650        660 
AAYWRGRCVK EAKLPPGGMA AVGLTWEECK QRCPPNVVPA CHNSEDTVTV SGPLDSVSEF 

       670        680        690        700        710        720 
VTKLKKDGVF AKEVRRAGVA FHSYYMASIA PALLSALKKV IPHPKPRSAR WISTSIPESQ 

       730        740        750        760        770        780 
WQSDLARNSS AEYHVNNLVN PVLFHEGLKH IPENAVVVEI APHALLQAIL RRTLKPTCTI 

       790        800        810        820        830        840 
LPLMKKDHKN NLEFFLTQTG KIHLTGINVL GNNLFPPVEY PVPVGTPLIS PYIKWDHSQD 

       850        860        870        880        890        900 
WDVPKAEDFP SGSKGSASAS VYNIDVSPDS PDHYLVGHCI DGRVLYPATG YLVLAWRTLA 

       910        920        930        940        950        960 
RSLGMVMEQT AVMFEEVTIH QATILPKKGS TQLEVRIMPA SHSFEVSGNG NLAVSGKISL 

       970        980        990       1000       1010       1020 
LENDALKNFH NQLADFQSQA NVTAKSGLLM EDVYQELHLR GYNYGPTFQG VLECNSEGSA 

      1030       1040       1050       1060       1070       1080 
GKILWNGNWV TFLDTLLHLI VLAETGRSLR LPTRIRSVYI DPVLHQEQVY QYQDNVEAFD 

      1090       1100       1110       1120       1130       1140 
VVVDRCLDSL KAGGVQINGL HASVAPRRQQ ERISPTLEKF SFVPYIESDC LSSSTQLHAY 

      1150       1160       1170       1180       1190       1200 
LEHCKGLIQK LQAKMALHGV KLVIHGLETK GAAAGSPPAQ KGLQHILTEI CRLELNGNPH 

      1210       1220       1230       1240       1250       1260 
SELEQIVTQE KMHLQDDPLL NGLLDSSELK TCLDVAKENT TSHRMKIVEA LAGSGRLFSR 

      1270       1280       1290       1300       1310       1320 
VQSILNTQPL LQLDYIATDC TPETLSDNET ELHDAGISFS QWDPSSLPSG NLTNADLAVC 

      1330       1340       1350       1360       1370       1380 
NCSTSVLGNT AEIISNLAAA VKEGGFVLLH TLLKEETLGE IVSFLTSPDL QQKHSFLSQA 

      1390       1400       1410       1420       1430       1440 
QWEELFSKAS LNLVAMKRSF FGSVIFLCRR QSPAKAPILL PVDDTHYKWV DSLKEILADS 

      1450       1460       1470       1480       1490       1500 
SEQPLWLTAT NCGNSGILGM VNCLRLEAEG HRIRCVFVSN LSPSSTVPAT SLSSLEMQKI 

      1510       1520       1530       1540       1550       1560 
IERDLVMNVY RDGKWGSFRH LPLQQAQPQE LTECAYVNVL TRGDLSSLRW IVSPLRHFQT 

      1570       1580       1590       1600       1610       1620 
TNPNVQLCKV YYASLNFWDI MLATGKLSPD AIPGNWTLQQ CMLGMEFSGR DLAGRRVMGL 

      1630       1640       1650       1660       1670       1680 
LPAKGLATVV DCDKRFLWEV PENWTLEEAA SVPVVYATAY YALVVRGGMK KGESVLIHSG 

      1690       1700       1710       1720       1730       1740 
SGGVGQAAIA IALSMGCRVF ATVGSAEKRE YLQARFPQLD ANSFASSRNT TFQQHILRVT 

      1750       1760       1770       1780       1790       1800 
NGKGVSLVLN SLAEEKLQAS LRCLAQHGRF LEIGKFDLSN NSQLGMALFL KNVAFHGILL 

      1810       1820       1830       1840       1850       1860 
DSIFEEGNQE WEVVSELLTK GIKDGVVKPL RTTVFGKEEV EAAFRFMAQG KHIGKVMIKI 

      1870       1880       1890       1900       1910       1920 
QEEEKQYPLR SEPVKLSAIS RTSCPPTKSY IITGGLGGFG LELAQWLIER GAQKLVLTSR 

      1930       1940       1950       1960       1970       1980 
SGIRTGYQAK CVREWKALGI QVLVSTSDVG TLEGTQLLIE EALKLGPVGG IFNLAVVLKD 

      1990       2000       2010       2020       2030       2040 
AMIENQTPEL FWEVNKPKYS GTLHLDWVTR KKCPDLDYFV VFSSVSCGRG NAGQSNYGFA 

      2050       2060       2070       2080       2090       2100 
NSAMERICEQ RHHDGLPGLA VQWGAIGDVG ILKAMGNREV VIGGTVLQQI SSCLEVLDMF 

      2110       2120       2130       2140       2150       2160 
LNQPHPVMSS FVLAEKVSVK SEGGSQRDLV EAVAHILGVR DVSSLNAESS LADLGLDSLM 

      2170       2180       2190       2200       2210       2220 
GVEVRQTLER DYDIVMTMRE IRLLTINKLR ELSSKTGTAE ELKPSQVLKT GPGEPPKLDL 

      2230       2240       2250       2260       2270       2280 
NNLLVNPEGP TITRLNEVQS TERPLFLVHP IEGSIAVFYT LASKLHMPCY GLQCTKAAPL 

      2290       2300       2310       2320       2330       2340 
DSIQSLASYY IDCMKQIQPE GPYRIAGYSF GACVAFEMCS QLQAQQNASH ALNSLFLFDG 

      2350       2360       2370       2380       2390       2400 
SHSFVAAYTQ SYRAKLTQGN EAALETEALC AFVQQFTGIE YNKLLEILLP LEDLEARVNA 

      2410       2420       2430       2440       2450       2460 
AADLITQIHK NINREALSFA AASFYHKLKA ADKYIPESKY HGNVTLMRAK THNEYEEGLG 

      2470       2480       2490       2500       2510 
GDYRLSEVCD GKVSVHIIEG DHRTLLEGDG VESIIGIIHG SLAEPRVSVR EG 

« Hide

Isoform 1 [UniParc].

Checksum: CA1DA253E4BD0956
Show »

FASTA2,520275,742

References

[1]"Amino-terminal blocking group and sequence of the animal fatty acid synthase."
Huang W.-Y., Chirala S.S., Wakil S.J.
Arch. Biochem. Biophys. 314:45-49(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-12.
Strain: White leghorn.
Tissue: Liver.
[2]"Molecular cloning and sequencing of chicken liver fatty acid synthase cDNA."
Holzer K.P., Liu W., Hammes G.G.
Proc. Natl. Acad. Sci. U.S.A. 86:4387-4391(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-1775.
Tissue: Liver.
[3]"A novel cDNA extension procedure. Isolation of chicken fatty acid synthase cDNA clones."
Chirala S.S., Kasturi R., Pazirandeh M., Stolow D.T., Huang W.-Y., Wakil S.J.
J. Biol. Chem. 264:3750-3757(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1568-2512, PARTIAL PROTEIN SEQUENCE.
[4]"Molecular cloning and sequencing of DNA complementary to chicken liver fatty acid synthase mRNA."
Yuan Z., Liu W., Hammes G.G.
Proc. Natl. Acad. Sci. U.S.A. 85:6328-6331(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1752-2512.
[5]"Characterization of a genomic and cDNA clone coding for the thioesterase domain and 3' noncoding region of the chicken liver fatty acid synthase gene."
Kasturi R., Chirala S.S., Pazirandeh M., Wakil S.J.
Biochemistry 27:7778-7785(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2202-2512.
[6]"Complete amino acid sequence of chicken liver acyl carrier protein derived from the fatty acid synthase."
Huang W.-Y., Stoops J.K., Wakil S.J.
Arch. Biochem. Biophys. 270:92-98(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2122-2210.
[7]"Complete amino acid sequence of the thioesterase domain of chicken liver fatty acid synthase."
Yang C.-Y., Huang W.-Y., Chirala S.S., Wakil S.J.
Biochemistry 27:7773-7777(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2210-2509.
Strain: White leghorn.
[8]"Amino acid sequences of pyridoxal 5'-phosphate binding sites and fluorescence resonance energy transfer in chicken liver fatty acid synthase."
Chang S.I., Hammes G.G.
Biochemistry 28:3781-3788(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 668-675 AND 1699-1710.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03860 mRNA. Translation: AAA48767.1.
J04485 mRNA. Translation: AAB46389.1.
J02839 Genomic DNA. Translation: AAA82106.1. Frameshift.
PIRXYCHFA. S57248.
UniGeneGga.8951.

3D structure databases

ProteinModelPortalP12276.
SMRP12276. Positions 421-821, 2122-2202, 2222-2508.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000038133.

Chemistry

BindingDBP12276.
ChEMBLCHEMBL1795136.

Proteomic databases

PaxDbP12276.
PRIDEP12276.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3319.
HOGENOMHOG000019642.
HOVERGENHBG005640.
PhylomeDBP12276.

Enzyme and pathway databases

SABIO-RKP12276.

Family and domain databases

Gene3D1.10.1200.10. 1 hit.
1.10.1470.20. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.720. 2 hits.
InterProIPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR002198. DH_sc/Rdtase_SDR.
IPR023102. Fatty_acid_synthase_dom_2.
IPR011032. GroES-like.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020843. PKS_ER.
IPR006162. PPantetheine_attach_site.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF00698. Acyl_transf_1. 1 hit.
PF00106. adh_short. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTSM00829. PKS_ER. 1 hit.
SM00822. PKS_KR. 1 hit.
[Graphical view]
SUPFAMSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816121.
PROP12276.

Entry information

Entry nameFAS_CHICK
AccessionPrimary (citable) accession number: P12276
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 140 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families