Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P12276

- FAS_CHICK

UniProt

P12276 - FAS_CHICK

Protein

Fatty acid synthase

Gene

FASN

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 activityi

    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 + an [acyl-carrier-protein] = CoA + a 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei161 – 1611For beta-ketoacyl synthase activityPROSITE-ProRule annotation
    Active sitei580 – 5801For acyl/malonyl transferase activityPROSITE-ProRule annotation
    Active sitei878 – 8781For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation
    Active sitei2309 – 23091For thioesterase activityPROSITE-ProRule annotation
    Active sitei2482 – 24821For thioesterase activityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1675 – 169218NADP (ER)Add
    BLAST
    Nucleotide bindingi1889 – 190416NADP (KR)Add
    BLAST

    GO - Molecular functioni

    1. [acyl-carrier-protein] S-acetyltransferase activity Source: UniProtKB-EC
    2. [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB-EC
    3. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
    4. 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Source: InterPro
    5. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
    6. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
    7. enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity Source: UniProtKB-EC
    8. enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Source: InterPro
    9. myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
    10. oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
    11. palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
    12. zinc ion binding Source: InterPro

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Lyase, Oxidoreductase, Transferase

    Keywords - Biological processi

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

    Keywords - Ligandi

    NAD, NADP, Pyridoxal phosphate

    Enzyme and pathway databases

    SABIO-RKP12276.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid synthase (EC:2.3.1.85)
    Including the following 7 domains:
    [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-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59)
    Enoyl-[acyl-carrier-protein] reductase (EC:1.3.1.39)
    Oleoyl-[acyl-carrier-protein] hydrolase (EC:3.1.2.14)
    Gene namesi
    Name:FASN
    Synonyms:FAS
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 25122511Fatty acid synthasePRO_0000180273Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglutamate
    Modified residuei1708 – 17081N6-(pyridoxal phosphate)lysineBy similarity
    Modified residuei2158 – 21581O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

    Keywords - PTMi

    Acetylation, Phosphopantetheine, Phosphoprotein

    Proteomic databases

    PaxDbiP12276.
    PRIDEiP12276.

    Interactioni

    Subunit structurei

    Homodimer which is arranged in a head to tail fashion.

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000038133.

    Structurei

    3D structure databases

    ProteinModelPortaliP12276.
    SMRiP12276. Positions 421-821, 2122-2202, 2222-2508.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2125 – 218157Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – ?412411Beta-ketoacyl synthaseAdd
    BLAST
    Regioni427 – 815389Acyl and malonyl transferasesAdd
    BLAST
    Regioni1638 – 1866229Enoyl reductaseAdd
    BLAST
    Regioni1867 – 2119253Beta-ketoacyl reductaseAdd
    BLAST
    Regioni2209 – 2511303ThioesteraseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3319.
    HOGENOMiHOG000019642.
    HOVERGENiHBG005640.
    PhylomeDBiP12276.

    Family and domain databases

    Gene3Di1.10.1200.10. 1 hit.
    1.10.1470.20. 1 hit.
    3.40.366.10. 2 hits.
    3.40.47.10. 2 hits.
    3.40.50.150. 1 hit.
    3.40.50.1820. 2 hits.
    3.40.50.720. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR001227. 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.
    IPR029063. SAM-dependent_MTases-like.
    IPR001031. Thioesterase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view]
    PfamiPF00698. 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]
    SMARTiSM00829. PKS_ER. 1 hit.
    SM00822. PKS_KR. 1 hit.
    [Graphical view]
    SUPFAMiSSF47336. SSF47336. 1 hit.
    SSF50129. SSF50129. 1 hit.
    SSF52151. SSF52151. 2 hits.
    SSF53335. SSF53335. 1 hit.
    SSF53474. SSF53474. 1 hit.
    SSF53901. SSF53901. 2 hits.
    SSF55048. SSF55048. 1 hit.
    PROSITEiPS50075. ACP_DOMAIN. 1 hit.
    PS00606. B_KETOACYL_SYNTHASE. 1 hit.
    PS00012. PHOSPHOPANTETHEINE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: P12276-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEDVVIAGIA GKLPESENLQ EFWENLLNGV DMVTEDDRRW KPGIYGLPKR     50
    NGKLKDIKKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPTAL 100
    RGTDTGVWVG ASGSEALEAL SQDPEELLGY SMTGCQRAML ANRISYFYDF 150
    TGPSLTIDTA CSSSLMALEN AYKAIRHGQC SAALVGGVNI LLKPNTSVQF 200
    MKLGMLSPDG ACKAFDVSGN GYCRSEAVVV VLLTKKSMAK RVYATIVNAG 250
    SNTDGFKEQG VTFPSGEMQQ QLVGSLYREC GIKPGDVEYV EAHGTGTKVG 300
    DPQEVNGIVN VFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVILSLEH 350
    GLWAPNLHFN DPNPDIPALH DGSLKVVCKP TPVKGGLVSI NSFGFGGSNA 400
    HVILRPNEKK CQPQETCNLP RLVQVCGRTQ EAVEILIEES RKHGGCSPFL 450
    SLLSDISAVP VSSMPYRGYT LVGTESDITE IQQVQASGRP LWYICSGMGT 500
    QWKGMGLSLM KLDLFRQSIL RSDEALKSTG LKVSDLLLNA DENTFDDTVH 550
    AFVGLAAIQI AQIDVLKAAG LQPDGILGHS VGELACGYAD NSLSHEEAVL 600
    AAYWRGRCVK EAKLPPGGMA AVGLTWEECK QRCPPNVVPA CHNSEDTVTV 650
    SGPLDSVSEF VTKLKKDGVF AKEVRRAGVA FHSYYMASIA PALLSALKKV 700
    IPHPKPRSAR WISTSIPESQ WQSDLARNSS AEYHVNNLVN PVLFHEGLKH 750
    IPENAVVVEI APHALLQAIL RRTLKPTCTI LPLMKKDHKN NLEFFLTQTG 800
    KIHLTGINVL GNNLFPPVEY PVPVGTPLIS PYIKWDHSQD WDVPKAEDFP 850
    SGSKGSASAS VYNIDVSPDS PDHYLVGHCI DGRVLYPATG YLVLAWRTLA 900
    RSLGMVMEQT AVMFEEVTIH QATILPKKGS TQLEVRIMPA SHSFEVSGNG 950
    NLAVSGKISL LENDALKNFH NQLADFQSQA NVTAKSGLLM EDVYQELHLR 1000
    GYNYGPTFQG VLECNSEGSA GKILWNGNWV TFLDTLLHLI VLAETGRSLR 1050
    LPTRIRSVYI DPVLHQEQVY QYQDNVEAFD VVVDRCLDSL KAGGVQINGL 1100
    HASVAPRRQQ ERISPTLEKF SFVPYIESDC LSSSTQLHAY LEHCKGLIQK 1150
    LQAKMALHGV KLVIHGLETK GAAAGSPPAQ KGLQHILTEI CRLELNGNPH 1200
    SELEQIVTQE KMHLQDDPLL NGLLDSSELK TCLDVAKENT TSHRMKIVEA 1250
    LAGSGRLFSR VQSILNTQPL LQLDYIATDC TPETLSDNET ELHDAGISFS 1300
    QWDPSSLPSG NLTNADLAVC NCSTSVLGNT AEIISNLAAA VKEGGFVLLH 1350
    TLLKEETLGE IVSFLTSPDL QQKHSFLSQA QWEELFSKAS LNLVAMKRSF 1400
    FGSVIFLCRR QSPAKAPILL PVDDTHYKWV DSLKEILADS SEQPLWLTAT 1450
    NCGNSGILGM VNCLRLEAEG HRIRCVFVSN LSPSSTVPAT SLSSLEMQKI 1500
    IERDLVMNVY RDGKWGSFRH LPLQQAQPQE LTECAYVNVL TRGDLSSLRW 1550
    IVSPLRHFQT TNPNVQLCKV YYASLNFWDI MLATGKLSPD AIPGNWTLQQ 1600
    CMLGMEFSGR DLAGRRVMGL LPAKGLATVV DCDKRFLWEV PENWTLEEAA 1650
    SVPVVYATAY YALVVRGGMK KGESVLIHSG SGGVGQAAIA IALSMGCRVF 1700
    ATVGSAEKRE YLQARFPQLD ANSFASSRNT TFQQHILRVT NGKGVSLVLN 1750
    SLAEEKLQAS LRCLAQHGRF LEIGKFDLSN NSQLGMALFL KNVAFHGILL 1800
    DSIFEEGNQE WEVVSELLTK GIKDGVVKPL RTTVFGKEEV EAAFRFMAQG 1850
    KHIGKVMIKI QEEEKQYPLR SEPVKLSAIS RTSCPPTKSY IITGGLGGFG 1900
    LELAQWLIER GAQKLVLTSR SGIRTGYQAK CVREWKALGI QVLVSTSDVG 1950
    TLEGTQLLIE EALKLGPVGG IFNLAVVLKD AMIENQTPEL FWEVNKPKYS 2000
    GTLHLDWVTR KKCPDLDYFV VFSSVSCGRG NAGQSNYGFA NSAMERICEQ 2050
    RHHDGLPGLA VQWGAIGDVG ILKAMGNREV VIGGTVLQQI SSCLEVLDMF 2100
    LNQPHPVMSS FVLAEKVSVK SEGGSQRDLV EAVAHILGVR DVSSLNAESS 2150
    LADLGLDSLM GVEVRQTLER DYDIVMTMRE IRLLTINKLR ELSSKTGTAE 2200
    ELKPSQVLKT GPGEPPKLDL NNLLVNPEGP TITRLNEVQS TERPLFLVHP 2250
    IEGSIAVFYT LASKLHMPCY GLQCTKAAPL DSIQSLASYY IDCMKQIQPE 2300
    GPYRIAGYSF GACVAFEMCS QLQAQQNASH ALNSLFLFDG SHSFVAAYTQ 2350
    SYRAKLTQGN EAALETEALC AFVQQFTGIE YNKLLEILLP LEDLEARVNA 2400
    AADLITQIHK NINREALSFA AASFYHKLKA ADKYIPESKY HGNVTLMRAK 2450
    THNEYEEGLG GDYRLSEVCD GKVSVHIIEG DHRTLLEGDG VESIIGIIHG 2500
    SLAEPRVSVR EG 2512
    Length:2,512
    Mass (Da):274,782
    Last modified:January 23, 2007 - v5
    Checksum:i66FDE22F5CCF603C
    GO
    Isoform 1 (identifier: P12276-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,520
    Mass (Da):275,742
    Checksum:iCA1DA253E4BD0956
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti78 – 792QL → PV in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti117 – 1171L → A in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti676 – 6761R → S in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti1170 – 11701K → N in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti1179 – 11791A → T in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti1192 – 11921R → H in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti1199 – 11991P → L in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti1287 – 12882DN → ND in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti1373 – 13731K → E in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti1534 – 15341C → Y in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti1578 – 15781W → R in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti1686 – 169712QAAIA…LSMGC → ASSHCHRLEHGLA in AAA48767. (PubMed:2734291)CuratedAdd
    BLAST
    Sequence conflicti1733 – 17331Q → E in AAA48767. (PubMed:2734291)Curated
    Sequence conflicti1746 – 17461S → N in AAA48767. (PubMed:2734291)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2349 – 23491T → TQCFSFSLF in isoform 1. CuratedVSP_000149

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03860 mRNA. Translation: AAA48767.1.
    J04485 mRNA. Translation: AAB46389.1.
    J02839 Genomic DNA. Translation: AAA82106.1. Frameshift.
    PIRiS57248. XYCHFA.
    UniGeneiGga.8951.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03860 mRNA. Translation: AAA48767.1 .
    J04485 mRNA. Translation: AAB46389.1 .
    J02839 Genomic DNA. Translation: AAA82106.1 . Frameshift.
    PIRi S57248. XYCHFA.
    UniGenei Gga.8951.

    3D structure databases

    ProteinModelPortali P12276.
    SMRi P12276. Positions 421-821, 2122-2202, 2222-2508.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000038133.

    Chemistry

    BindingDBi P12276.
    ChEMBLi CHEMBL1795136.

    Proteomic databases

    PaxDbi P12276.
    PRIDEi P12276.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG3319.
    HOGENOMi HOG000019642.
    HOVERGENi HBG005640.
    PhylomeDBi P12276.

    Enzyme and pathway databases

    SABIO-RK P12276.

    Miscellaneous databases

    NextBioi 20816121.
    PROi P12276.

    Family and domain databases

    Gene3Di 1.10.1200.10. 1 hit.
    1.10.1470.20. 1 hit.
    3.40.366.10. 2 hits.
    3.40.47.10. 2 hits.
    3.40.50.150. 1 hit.
    3.40.50.1820. 2 hits.
    3.40.50.720. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR001227. 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.
    IPR029063. SAM-dependent_MTases-like.
    IPR001031. Thioesterase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view ]
    Pfami PF00698. 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 ]
    SMARTi SM00829. PKS_ER. 1 hit.
    SM00822. PKS_KR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47336. SSF47336. 1 hit.
    SSF50129. SSF50129. 1 hit.
    SSF52151. SSF52151. 2 hits.
    SSF53335. SSF53335. 1 hit.
    SSF53474. SSF53474. 1 hit.
    SSF53901. SSF53901. 2 hits.
    SSF55048. SSF55048. 1 hit.
    PROSITEi PS50075. ACP_DOMAIN. 1 hit.
    PS00606. B_KETOACYL_SYNTHASE. 1 hit.
    PS00012. PHOSPHOPANTETHEINE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiFAS_CHICK
    AccessioniPrimary (citable) accession number: P12276
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 143 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3