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Q71SP7 (FAS_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·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=1.3.1.10
  7. Oleoyl-[acyl-carrier-protein] hydrolase
    EC=3.1.2.14
Gene names
Name:FASN
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length2513 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Acyl-[acyl-carrier-protein] + NADP+ = 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 By similarity.

Subcellular location

Cytoplasm By similarity. Melanosome By similarity.

Sequence similarities

Contains 1 acyl carrier domain.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   LigandNAD
NADP
Phosphopantetheine
Pyridoxal phosphate
   Molecular functionHydrolase
Lyase
Oxidoreductase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmelanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Inferred from electronic annotation. Source: 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: EC

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

Inferred from electronic annotation. Source: EC

[acyl-carrier-protein] S-acetyltransferase activity

Inferred from electronic annotation. Source: EC

[acyl-carrier-protein] S-malonyltransferase activity

Inferred from electronic annotation. Source: EC

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

Inferred from electronic annotation. Source: EC

myristoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: EC

oleoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: EC

palmitoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25132513Fatty acid synthase
PRO_0000180274

Regions

Domain2125 – 218157Acyl carrier
Nucleotide binding1673 – 169018NADP (ER) By similarity
Nucleotide binding1888 – 190316NADP (KR) By similarity
Region1 – 414414Beta-ketoacyl synthase
Region429 – 817389Acyl and malonyl transferases
Region1637 – 1865229Enoyl reductase
Region1866 – 2119254Beta-ketoacyl reductase
Region2209 – 2513305Thioesterase

Sites

Active site1611For beta-ketoacyl synthase activity By similarity
Active site5811For malonyltransferase activity By similarity
Active site8781For beta-hydroxyacyl dehydratase activity By similarity
Active site23101For thioesterase activity By similarity
Active site24831For thioesterase activity By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue701N6-acetyllysine By similarity
Modified residue2071Phosphoserine By similarity
Modified residue2981N6-acetyllysine By similarity
Modified residue5281N6-acetyllysine By similarity
Modified residue6731N6-acetyllysine By similarity
Modified residue17061N6-(pyridoxal phosphate)lysine By similarity
Modified residue17061N6-acetyllysine By similarity
Modified residue17731N6-acetyllysine By similarity
Modified residue18491N6-acetyllysine By similarity
Modified residue19971N6-acetyllysine By similarity
Modified residue21581O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residue22061Phosphothreonine By similarity
Modified residue22381Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q71SP7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D75B09DB855DFDAB

FASTA2,513274,554
        10         20         30         40         50         60 
MEEVVITGMS GKLPESENLE EFWANLIGGV DMVTDDDRRW KAGLYGLPRR SGKLKDLSRF 

        70         80         90        100        110        120 
DASFFGVHPK QAHNMDPQLR LLLEVTYEAI VDAGINPASI RGTNTGVWVG VSGSEASEAL 

       130        140        150        160        170        180 
SRDPETLVGY SMVGCQRAML ANRLSFFFDF KGPSITLDTA CSSSLLALQR AYQAIQRGEC 

       190        200        210        220        230        240 
AMAIVGGVNI RLKPNTSVQF MKLGMLSPEG TCKFFDASGN GYCRAKAVMA ILLTKKSLAR 

       250        260        270        280        290        300 
RVYATILNAG TNTDGCKEKG VTFPSGEAQE QLISSLYKPA GLDPETLEYV EAHGTGTKVG 

       310        320        330        340        350        360 
DPQELNGIVQ ALCGTRQSPL RIGSTKSNMG HPEPASGLAA LAKVLLSLEH GLWAPNLHFH 

       370        380        390        400        410        420 
NPNPKIPALQ DGRLQVVDRP LPVLGGNVGI NSFGFGGSNV HVILQPNSQP LPPPAPHAAL 

       430        440        450        460        470        480 
PRLLRASGRT LEGVQGLLEL GLQHSQNLAF VSMLNDIATP SPAAMPFRGY AVLGSQGGSQ 

       490        500        510        520        530        540 
KVQQVLAGKR PLWFICSGMG TQWRGMGLSL MRLSRFRDSI LRSDEAVKPL GLQVSQLLLS 

       550        560        570        580        590        600 
TDEAIFDDMV ISFVSLTAIQ IALIDLLTSM GLQPDGIIGH SLGEVACGYA DGCISQEEAI 

       610        620        630        640        650        660 
LSAYWRGQCI KEANIPPGAM AAVGLTWEEC KQRCPPGIVP ACHNCIDTVT ISGPQASMLE 

       670        680        690        700        710        720 
FVQQLKQEGV FAKEVRTGGM AFHSYFMDAI APMLLQQLKK VIREPQPRSP RWLSTSIPET 

       730        740        750        760        770        780 
QWQESLARTF SAEYNVNNLV SPVLFQEALW RVPEDAVVLE IAPHALLQAV LKRGLKSSCT 

       790        800        810        820        830        840 
IIPLMKKDHR DNLEFFLSNV GQLYLTGIDV NPNGLFPPVE FPAPRGTPLI SPHIKWDHSQ 

       850        860        870        880        890        900 
TWDVPTAEDF PSGSSSSSAT IYKIDINPES PDHYLVDHCI DGRIIFPGTG YLCLVWKTLA 

       910        920        930        940        950        960 
RALDQNMEHT PVVFEDVTLH QAVILPKTGI VLLKVRLLEA SCTFEVSENG NLIASGKVYQ 

       970        980        990       1000       1010       1020 
WEDPNPKLFD NRYGPDPATP VDPTTAIHLS RGDVYKELQL QGFNYGPYFQ GILEASSEGN 

      1030       1040       1050       1060       1070       1080 
TGQLLWKDNW VTFMDTMLQM SILAPSKRSL RLPTRITAIY IHPATHQQKL YTLQDKTQVA 

      1090       1100       1110       1120       1130       1140 
DVVINRCLDT TVAGGIYISR IHTSVAPRHQ QEQLVPILEK FCFTPHVETG CLAGNLALQE 

      1150       1160       1170       1180       1190       1200 
ELQLCVGLAQ ALQTRVAQQG IKMVVPGLDG AQAPQEAPQQ GLPRLLATAC QLQLNGNLQM 

      1210       1220       1230       1240       1250       1260 
EMGQILAQER ALLCDDPLLS GLLNSPALKA CVTLALENMT SLKMKVVLAG DGQLYSRIPT 

      1270       1280       1290       1300       1310       1320 
LLNTQPLLEL DYTATDRHPQ ALEAAQAKLQ QLDITQGQWD PSDPAPSNLG GANLVVCNYA 

      1330       1340       1350       1360       1370       1380 
LASLGDPATA VGNMVAALKE GGFLLLHTLL RGHPLGETVT FLTCPEPQQG QRHLLSQDEW 

      1390       1400       1410       1420       1430       1440 
ERLFAGASLH LVALKKSFYG SVLFLCRRLA PLDSPIFLPV EDTSFQWVDS LKNILADSSS 

      1450       1460       1470       1480       1490       1500 
RAVWLMAVGC TTSGVVGLVN CLRKEPDGHR IRCVLVSNLN STSPIPETDP KSLELQKVLQ 

      1510       1520       1530       1540       1550       1560 
SDLVMNVYRD GAWGAFRHFP LEQDKPEEQT EHAFINVLTR GDLSSIRWVC SPLRHSQPTA 

      1570       1580       1590       1600       1610       1620 
PGFQLCTIYY ASLNFKRNHA GHGQAVPRRH PRNWASRNCL LGMEFSGRDA SGKRVMGLVP 

      1630       1640       1650       1660       1670       1680 
AEGLATSTLV PQSFLWDVPS NWTLEEAASV PVVYSTAYYA LMVRGRMQPG ETVLIHSGSG 

      1690       1700       1710       1720       1730       1740 
GVGQAAIAIA LSLGCRVFPL VGSAEKRAYL QSRFPQLNET SFANSRDTSF EQHVLWHTAG 

      1750       1760       1770       1780       1790       1800 
KGADLVLNSL AEEKLQASVR CLAQHGRFLE IGKFDLSKNH PLGMAIFLKN VTFHGILLDS 

      1810       1820       1830       1840       1850       1860 
LFEENNTMWQ EVSTLLKAGI RKGVVQPLKR TVFPRTQAED AFRYMAQGKH IGKVVIQVRE 

      1870       1880       1890       1900       1910       1920 
EEQEAVLHGT KPTQMVALCK TFCPAHKSYI ITGGLGGFGL ELAHWLVERG AQKLVLTSRS 

      1930       1940       1950       1960       1970       1980 
GIRTGYQARQ VHEWRRQGVQ VLVSTSDVST LDGTRSLITE AAQLGPVGGI FNLAVVLRDA 

      1990       2000       2010       2020       2030       2040 
MLDNQTPEFF QDVNKPKYNG TLNLDRVTRE ACPELDYFEV FSSVSCGRGN AGQTNYGFAN 

      2050       2060       2070       2080       2090       2100 
STMERICEKR RHDGLPGLAV QWGAIADVGL LMELKGTKDK AIGGTLPQRI TSCMEVLDLF 

      2110       2120       2130       2140       2150       2160 
LNQPHPVLSS FVLAEKATSR GPSGSHQDLV KAVTHILGIR DLATVNLDSS LSDLGLDSLM 

      2170       2180       2190       2200       2210       2220 
GVEVRQMLER EHNLLLSMRE IRQLTIHKLQ EISAQAGTAD ELTDSTPKFG SPAQSHTQLN 

      2230       2240       2250       2260       2270       2280 
LSTLLVNPEG PTLTRLNSVQ SSERPLFLVH PIEGSTTVFH SLATKLSIPT YGLQCTGAAP 

      2290       2300       2310       2320       2330       2340 
LDSIQSLATY YIECIRQVQP EGNYRIAGYS YGACVAFEMC SQLQAQQNAG PTNNSLFLFD 

      2350       2360       2370       2380       2390       2400 
GSHTFVMAYT QSYRAKLNPG CEAEAEAEAM CFFMQQFTEA EHSRVLEALL PLGDLEARVA 

      2410       2420       2430       2440       2450       2460 
ATVELIVQSH AGLDRHALSF AARSFYHKLR AAEEYTPRAT YHGNVTLLRA KMGSAYQEGL 

      2470       2480       2490       2500       2510 
GADYNLSQVC DGKVSVHIIE GDHRTLLEGS GLESILSIIH SSLAEPRVSV REG

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References

[1]"Cloning, genomic organization and expression analysis of bovine FASN gene."
Roy R., Eggen A., Rodellar C.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF285607 Genomic DNA. Translation: AAR19788.1.
AY343889 mRNA. Translation: AAR17600.1.
IPIIPI00712133.
RefSeqNP_001012687.1. NM_001012669.1.
UniGeneBt.30099.

3D structure databases

ProteinModelPortalQ71SP7.
SMRQ71SP7. Positions 422-822, 2121-2208, 2223-2509.
ModBaseSearch...

Proteomic databases

PaxDbQ71SP7.
PRIDEQ71SP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281152.
KEGGbta:281152.

Organism-specific databases

CTD2194.

Phylogenomic databases

eggNOGCOG3319.
HOVERGENHBG005640.
KOK00665.

Enzyme and pathway databases

BioCycCATTLE:281152-MONOMER.

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.
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.
IPR013968. PKS_KR.
IPR006162. PPantetheine_attach_site.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF00698. Acyl_transf_1. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 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. ACP_like. 1 hit.
SSF52151. Acyl_Trfase/lysoPlipase. 1 hit.
SSF50129. GroES_like. 1 hit.
SSF55048. Malonyl_transacylase_ACP-bd. 1 hit.
SSF53901. Thiolase-like. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805215.

Entry information

Entry nameFAS_BOVIN
AccessionPrimary (citable) accession number: Q71SP7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 5, 2004
Last modified: May 29, 2013
This is version 77 of the entry and version 1 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

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