ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P12276


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name FAS_CHICK
Primary accession number P12276
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on January 23, 2007 (Sequence version 5)
Annotations were last modified on    July 22, 2008 (Entry version 91)
Name and origin of the protein
Protein name Fatty acid synthase
Synonym EC 2.3.1.85
Includes [Acyl-carrier-protein] S-acetyltransferase
     (EC 2.3.1.38)
[Acyl-carrier-protein] S-malonyltransferase
     (EC 2.3.1.39)
3-oxoacyl-[acyl-carrier-protein] synthase
     (EC 2.3.1.41)
3-oxoacyl-[acyl-carrier-protein] reductase
     (EC 1.1.1.100)
3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
     (EC 4.2.1.61)
Enoyl-[acyl-carrier-protein] reductase
     (EC 1.3.1.10)
Oleoyl-[acyl-carrier-protein] hydrolase
     (EC 3.1.2.14)
Gene name
Name: FASN
Synonyms: FAS
From
Gallus gallus (Chicken) [TaxID: 9031] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-12.
STRAIN=White leghorn;
TISSUE=Liver;
DOI=10.1006/abbi.1994.1410; PubMed=7944406 [NCBI, ExPASy, EBI, Israel, Japan]
Huang W.-Y., Chirala S.S., Wakil S.J.;
"Amino-terminal blocking group and sequence of the animal fatty acid synthase.";
Arch. Biochem. Biophys. 314:45-49(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 75-1775.
TISSUE=Liver;
PubMed=2734291 [NCBI, ExPASy, EBI, Israel, Japan]
Holzer K.P., Liu W., Hammes G.G.;
"Molecular cloning and sequencing of chicken liver fatty acid synthase cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 86:4387-4391(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1568-2512, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2917973 [NCBI, ExPASy, EBI, Israel, Japan]
Chirala S.S., Kasturi R., Pazirandeh M., Stolow D.T., Huang W.-Y., Wakil S.J.;
"A novel cDNA extension procedure. Isolation of chicken fatty acid synthase cDNA clones.";
J. Biol. Chem. 264:3750-3757(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1752-2512.
PubMed=2842766 [NCBI, ExPASy, EBI, Israel, Japan]
Yuan Z., Liu W., Hammes G.G.;
"Molecular cloning and sequencing of DNA complementary to chicken liver fatty acid synthase mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 85:6328-6331(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2202-2512.
DOI=10.1021/bi00420a029; PubMed=3207710 [NCBI, ExPASy, EBI, Israel, Japan]
Kasturi R., Chirala S.S., Pazirandeh M., Wakil S.J.;
"Characterization of a genomic and cDNA clone coding for the thioesterase domain and 3' noncoding region of the chicken liver fatty acid synthase gene.";
Biochemistry 27:7778-7785(1988).
[6]
PROTEIN SEQUENCE OF 2122-2210.
DOI=10.1016/0003-9861(89)90011-8; PubMed=2648999 [NCBI, ExPASy, EBI, Israel, Japan]
Huang W.-Y., Stoops J.K., Wakil S.J.;
"Complete amino acid sequence of chicken liver acyl carrier protein derived from the fatty acid synthase.";
Arch. Biochem. Biophys. 270:92-98(1989).
[7]
PROTEIN SEQUENCE OF 2210-2509.
STRAIN=White leghorn;
DOI=10.1021/bi00420a028; PubMed=3207709 [NCBI, ExPASy, EBI, Israel, Japan]
Yang C.-Y., Huang W.-Y., Chirala S.S., Wakil S.J.;
"Complete amino acid sequence of the thioesterase domain of chicken liver fatty acid synthase.";
Biochemistry 27:7773-7777(1988).
[8]
PROTEIN SEQUENCE OF 668-675 AND 1699-1710.
DOI=10.1021/bi00435a023; PubMed=2751995 [NCBI, ExPASy, EBI, Israel, Japan]
Chang S.I., Hammes G.G.;
"Amino acid sequences of pyridoxal 5'-phosphate binding sites and fluorescence resonance energy transfer in chicken liver fatty acid synthase.";
Biochemistry 28:3781-3788(1989).
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+.
  • CATALYTIC ACTIVITY: Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].
  • CATALYTIC ACTIVITY: Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].
  • CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
  • CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
  • CATALYTIC ACTIVITY: (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H2O.
  • CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + NADP+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH.
  • CATALYTIC ACTIVITY: Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.
  • SUBUNIT: Homodimer which is arranged in a head to tail fashion.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name2
    Isoform IDP12276-1
    This is the isoform sequence displayed in this entry.
    Name1
    Isoform IDP12276-2
    Features which should be applied to build the isoform sequence: VSP_000149.
  • SIMILARITY: Contains 1 acyl carrier domain.
  • SEQUENCE CAUTION:
    • Sequence=AAA82106.1; Type=Frameshift; Positions=2352;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J03860; AAA48767.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04485; AAB46389.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02839; AAA82106.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S57248; XYCHFA.
RefSeq NP_990486.1; -.
UniGene Gga.33829
3D structure databases
HSSP P12785; 1N8L. [HSSP ENTRY / PDB]
SMR P12276; 2218-2503.
ModBase P12276.
Ontologies
GO
GO:0004317; Molecular function: 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity (inferred from electronic annotation from EC).
GO:0004316; Molecular function: 3-oxoacyl-[acyl-carrier-protein] reductase activity (inferred from electronic annotation from EC).
GO:0004315; Molecular function: 3-oxoacyl-[acyl-carrier-protein] synthase activity (inferred from electronic annotation from EC).
GO:0004313; Molecular function: [acyl-carrier-protein] S-acetyltransferase activity (inferred from electronic annotation from EC).
GO:0004314; Molecular function: [acyl-carrier-protein] S-malonyltransferase activity (inferred from electronic annotation from EC).
GO:0004319; Molecular function: enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity (inferred from electronic annotation from EC).
GO:0004320; Molecular function: oleoyl-[acyl-carrier-protein] hydrolase activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR001227; Ac_transferase_reg.
IPR009081; ACP_like.
IPR014043; Acyl_transferase.
IPR013149; AlcDHase_Zn-bd.
IPR002198; DHase_sc/Rdtase_SDR.
IPR000794; Ketoacyl_synth.
IPR014031; Ketoacyl_synth_C.
IPR014030; Ketoacyl_synth_N.
IPR016040; NAD(P)-bd.
IPR006163; Phsphopanteth_bd.
IPR006162; Ppantne_S.
IPR001031; Thioesterase.
IPR016038; Thiolase-like_subgr.
Graphical view of domain structure.
Gene3D G3DSA:3.40.366.10; Ac_transferase_reg; 1.
G3DSA:1.10.1200.10; ACP_like; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 2.
G3DSA:3.40.47.10; Thiolase-like_subgr; 2.
PANTHER PTHR11712; Ketoacyl_synth; 1.
Pfam PF00698; Acyl_transf_1; 1.
PF00106; adh_short; 1.
PF00107; ADH_zinc_N; 1.
PF00109; ketoacyl-synt; 1.
PF02801; Ketoacyl-synt_C; 1.
PF00550; PP-binding; 1.
PF00975; Thioesterase; 1.
Pfam graphical view of domain structure.
PROSITE PS50075; ACP_DOMAIN; 1.
PS00606; B_KETOACYL_SYNTHASE; 1.
PS00012; PHOSPHOPANTETHEINE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P12276.
Genome annotation databases
Ensembl ENSGALG00000002747; Gallus gallus. [Contig view]
GeneID 396061; -.
KEGG gga:396061; -.
Phylogenomic databases
HOGENOM P12276; -.
HOVERGEN P12276; -.
Other
ProtoNet P12276.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Alternative splicing; Direct protein sequencing; Fatty acid biosynthesis; Hydrolase; Lipid synthesis; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphopantetheine; Pyridoxal phosphate; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
INIT_MET   1      1        Removed. 
CHAIN   2   2512  2511     Fatty acid synthase. PRO_0000180273
DOMAIN   2125   2181  57     Acyl carrier. 
NP_BIND   1675   1692  18     NADP (ER). 
NP_BIND   1889   1904  16     NADP (KR). 
REGION   2   ?412        Beta-ketoacyl synthase. 
REGION   427    815  389     Acyl and malonyl transferases. 
REGION   1638   1866  229     Enoyl reductase. 
REGION   1867   2119  253     Beta-ketoacyl reductase. 
REGION   2209   2511  303     Thioesterase. 
ACT_SITE   161    161        For beta-ketoacyl synthase activity (By similarity). 
ACT_SITE   580    580        For acyl/malonyl transferase activity (By similarity). 
ACT_SITE   878    878        For beta-hydroxyacyl dehydratase activity (By similarity). 
ACT_SITE   2309   2309        For thioesterase activity (By similarity). 
ACT_SITE   2482   2482        For thioesterase activity (By similarity). 
BINDING   1708   1708        Pyridoxal phosphate (covalent) (By similarity). 
BINDING   2158   2158        Phosphopantetheine (covalent) (By similarity). 
MOD_RES   2      2        N-acetylglutamate. 
VAR_SEQ   2349   2349        T -> TQCFSFSLF (in isoform 1). VSP_000149
CONFLICT   78     79        QL -> PV (in Ref. 2; AAA48767). 
CONFLICT   117    117        L -> A (in Ref. 2; AAA48767). 
CONFLICT   676    676        R -> S (in Ref. 2; AAA48767). 
CONFLICT   1170   1170        K -> N (in Ref. 2; AAA48767). 
CONFLICT   1179   1179        A -> T (in Ref. 2; AAA48767). 
CONFLICT   1192   1192        R -> H (in Ref. 2; AAA48767). 
CONFLICT   1199   1199        P -> L (in Ref. 2; AAA48767). 
CONFLICT   1287   1288        DN -> ND (in Ref. 2; AAA48767). 
CONFLICT   1373   1373        K -> E (in Ref. 2; AAA48767). 
CONFLICT   1534   1534        C -> Y (in Ref. 2; AAA48767). 
CONFLICT   1578   1578        W -> R (in Ref. 2; AAA48767). 
CONFLICT   1686   1697        QAAIAIALSMGC -> ASSHCHRLEHGLA (in Ref. 2; AAA48767). 
CONFLICT   1733   1733        Q -> E (in Ref. 2; AAA48767). 
CONFLICT   1746   1746        S -> N (in Ref. 2; AAA48767). 
Sequence information
Length: 2512 AA [This is the length of the unprocessed precursor] Molecular weight: 274782 Da [This is the MW of the unprocessed precursor] CRC64: 66FDE22F5CCF603C [This is a checksum on the sequence]
        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 

P12276 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!