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P12785

- FAS_RAT

UniProt

P12785 - FAS_RAT

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Protein

Fatty acid synthase

Gene
Fasn
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 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 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 activity By similarity
Active sitei581 – 5811For malonyltransferase activity By similarity
Active sitei878 – 8781For beta-hydroxyacyl dehydratase activity By similarity
Active sitei2302 – 23021For thioesterase activity By similarity
Active sitei2475 – 24751For thioesterase activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1665 – 168218NADP (ER)Add
BLAST
Nucleotide bindingi1765 – 178016NADP (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. drug binding Source: RGD
  8. enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity Source: UniProtKB-EC
  9. enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Source: InterPro
  10. fatty acid synthase activity Source: RGD
  11. identical protein binding Source: IntAct
  12. myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  13. NADPH binding Source: RGD
  14. oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  15. palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  16. protein homodimerization activity Source: RGD
  17. zinc ion binding Source: InterPro

GO - Biological processi

  1. acetyl-CoA metabolic process Source: RGD
  2. cellular response to interleukin-4 Source: Ensembl
  3. fatty acid biosynthetic process Source: RGD
  4. lipid biosynthetic process Source: RGD
Complete GO annotation...

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

ReactomeiREACT_198613. Activation of gene expression by SREBF (SREBP).
SABIO-RKP12785.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi620665. Fasn.

Subcellular locationi

Cytoplasm By similarity. Melanosome By similarity

GO - Cellular componenti

  1. glycogen granule Source: Ensembl
  2. Golgi apparatus Source: Ensembl
  3. melanosome Source: UniProtKB-SubCell
  4. mitochondrion Source: Ensembl
  5. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25052505Fatty acid synthasePRO_0000180279Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei59 – 591N6-acetyllysine By similarity
Modified residuei70 – 701N6-acetyllysine By similarity
Modified residuei207 – 2071Phosphoserine By similarity
Modified residuei298 – 2981N6-acetyllysine By similarity
Modified residuei528 – 5281N6-acetyllysine By similarity
Modified residuei673 – 6731N6-acetyllysine By similarity
Modified residuei790 – 7901N6-acetyllysine By similarity
Modified residuei993 – 9931N6-acetyllysine By similarity
Modified residuei1276 – 12761N6-acetyllysine By similarity
Modified residuei1698 – 16981N6-(pyridoxal phosphate)lysine; alternate By similarity
Modified residuei1698 – 16981N6-acetyllysine; alternate By similarity
Modified residuei1765 – 17651N6-acetyllysine By similarity
Modified residuei1841 – 18411N6-acetyllysine By similarity
Modified residuei1989 – 19891N6-acetyllysine By similarity
Modified residuei2151 – 21511O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residuei2230 – 22301Phosphoserine By similarity
Modified residuei2385 – 23851N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphopantetheine, Phosphoprotein

Proteomic databases

PRIDEiP12785.

Expressioni

Inductioni

Up-regulated in livers of rats fed on a high carbohydrate diet.1 Publication

Gene expression databases

GenevestigatoriP12785.

Interactioni

Subunit structurei

Homodimer which is arranged in a head to tail fashion.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself8EBI-493558,EBI-493558

Protein-protein interaction databases

BioGridi248415. 2 interactions.
DIPiDIP-33893N.
MINTiMINT-4564064.

Structurei

Secondary structure

1
2505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2122 – 21243
Helixi2126 – 21305
Beta strandi2140 – 21423
Helixi2144 – 21474
Helixi2152 – 216413
Helixi2171 – 21744
Helixi2180 – 21845
Beta strandi2188 – 21903
Beta strandi2192 – 21943

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PNGNMR-A2114-2202[»]
ProteinModelPortaliP12785.
SMRiP12785. Positions 423-819, 2114-2202, 2216-2501.

Miscellaneous databases

EvolutionaryTraceiP12785.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2118 – 217457Acyl carrierAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 413413Beta-ketoacyl synthaseAdd
BLAST
Regioni429 – 817389Acyl and malonyl transferasesAdd
BLAST
Regioni1629 – 1857229Enoyl reductaseAdd
BLAST
Regioni1858 – 2113256Beta-ketoacyl reductaseAdd
BLAST
Regioni2202 – 2505304ThioesteraseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00530000063309.
HOVERGENiHBG005640.
KOiK00665.
OMAiATGQMAI.
OrthoDBiEOG71K623.
PhylomeDBiP12785.

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.
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.
IPR013217. Methyltransf_12.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
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.
PF00107. ADH_zinc_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF08242. Methyltransf_12. 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]

Sequencei

Sequence statusi: Complete.

P12785-1 [UniParc]FASTAAdd to Basket

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MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR     50
SGKLKDLSKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL 100
RGTNTGVWVG VSGSEASEAL SRDPETLLGY SMVGCQRAMM ANRLSFFFDF 150
KGPSIALDTA CSSSLLALQN AYQAIRSGEC PAAIVGGINL LLKPNTSVQF 200
MKLGMLSPDG TCRSFDDSGN GYCRAEAVVA VLLTKKSLAR RVYATILNAG 250
TNTDGCKEQG VTFPSGEAQE QLIRSLYQPG GVAPESLEYI EAHGTGTKVG 300
DPQELNGITR SLCAFRQSPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEN 350
GVWAPNLHFH NPNPEIPALL DGRLQVVDRP LPVRGGIVGI NSFGFGGANV 400
HVILQPNTQQ APAPAPHAAL PHLLHASGRT MEAVQGLLEQ GRQHSQDLAF 450
VSMLNDIAAT PTAAMPFRGY TVLGVEGHVQ EVQQVPASQR PLWFICSGMG 500
TQWRGMGLSL MRLDSFRESI LRSDEALKPL GVKVSDLLLS TDEHTFDDIV 550
HSFVSLTAIQ IALIDLLTSM GLKPDGIIGH SLGEVACGYA DGCLSQREAV 600
LAAYWRGQCI KDANLPAGSM AAVGLSWEEC KQRCPPGVVP ACHNSEDTVT 650
ISGPQAAVNE FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK 700
VIREPRPRSA RWLSTSIPEA QWQSSLARTS SAEYNVNNLV SPVLFQEALW 750
HVPEHAVVLE IAPHALLQAV LKRGVKPSCT IIPLMKRDHK DNLEFFLTNL 800
GKVHLTGIDI NPNALFPPVE FPVPRGTPLI SPHIKWDHSQ TWDIPVAEDF 850
PNGSSSSSAT VYNIDASSES SDHYLVDHCI DGRVLFPGTG YLYLVWKTLA 900
RSLSLSLEET PVVFENVTFH QATILPRTGT VPLEVRLLEA SHAFEVSDSG 950
NLIVSGKVYQ WEDPDSKLFD HPEVPIPAES ESVSRLTQGE VYKELRLRGY 1000
DYGPHFQGVY EATLEGEQGK LLWKDNWVTF MDTMLQISIL GFSKQSLQLP 1050
TRVTAIYIDP ATHLQKVYML EGDTQVADVT TSRCLGVTVS GGVYISRLQT 1100
TATSRRQQEQ LVPTLEKFVF TPHVEPECLS ESAILQKELQ LCKGLAKALQ 1150
TKATQQGLKM TVPGLEDLPQ HGLPRLLAAA CQLQLNGNLQ LELGEVLARE 1200
RLLLPEDPLI SGLLNSQALK ACIDTALENL STLKMKVVEV LAGEGHLYSH 1250
ISALLNTQPM LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWDPSGPAPT 1300
NLGALDLVVC NCALATLGDP ALALDNMVAA LKDGGFLLMH TVLKGHALGE 1350
TLACLPSEVQ PGPSFLSQEE WESLFSRKAL HLVGLKKSFY GTALFLCRRL 1400
SPQDKPIFLP VEDTSFQWVD SLKSILATSS SQPVWLTAMN CPTSGVVGLV 1450
NCLRKEPGGH RIRCILLSNL SSTSHVPKLD PGSSELQKVL ESDLVMNVYR 1500
DGAWGAFRHF QLEQDKPEEQ TAHAFVNVLT RGDLASIRWV SSPLKHMQPP 1550
SSSGAQLCTV YYASLNFRDI MLATGKLSPD AIPGKWASRD CMLGMEFSGR 1600
DKCGRRVMGL VPAEGLATSV LLSPDFLWDV PSSWTLEEAA SVPVVYTTAY 1650
YSLVVRGRIQ HGETVLIHSG SGGVGQAAIS IALSLGCRVF TTVGSAEKRA 1700
YLQARFPQLD DTSFANSRDT SFEQHVLLHT GGKGVDLVLN SLAEEKLQAS 1750
VRCLAQHGRF LEIGKFDLSN NHPLGMAIFL KNVTFHGILL DALFEGANDS 1800
WREVAELLKA GIRDGVVKPL KCTVFPKAQV EDAFRYMAQG KHIGKVLVQV 1850
REEEPEAMLP GAQPTLISAI SKTFCPEHKS YIITGGLGGF GLELARWLVL 1900
RGAQRLVLTS RSGIRTGYQA KHVREWRRQG IHVLVSTSNV SSLEGARALI 1950
AEATKLGPVG GVFNLAMVLR DAMLENQTPE LFQDVNKPKY NGTLNLDRAT 2000
REACPELDYF VAFSSVSCGR GNAGQSNYGF ANSTMERICE QRRHDGLPGL 2050
AVQWGAIGDV GIILEAMGTN DTVVGGTLPQ RISSCMEVLD LFLNQPHAVL 2100
SSFVLAEKKA VAHGDGEAQR DLVKAVAHIL GIRDLAGINL DSSLADLGLD 2150
SLMGVEVRQI LEREHDLVLP IREVRQLTLR KLQEMSSKAG SDTELAAPKS 2200
KNDTSLKQAQ LNLSILLVNP EGPTLTRLNS VQSSERPLFL VHPIEGSITV 2250
FHSLAAKLSV PTYGLQCTQA APLDSIPNLA AYYIDCIKQV QPEGPYRVAG 2300
YSFGACVAFE MCSQLQAQQG PAPAHNNLFL FDGSHTYVLA YTQSYRAKLT 2350
PGCEAEAEAE AICFFIKQFV DAEHSKVLEA LLPLKSLEDR VAAAVDLITR 2400
SHQSLDRRDL SFAAVSFYYK LRAADQYKPK AKYHGNVILL RAKTGGTYGE 2450
DLGADYNLSQ VCDGKVSVHI IEGDHRTLLE GRGLESIINI IHSSLAEPRV 2500
SVREG 2505
Length:2,505
Mass (Da):272,650
Last modified:November 1, 1997 - v3
Checksum:i5810EC13D37F3114
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841I → T in AAA41145. 1 Publication
Sequence conflicti871 – 8711S → P in CAA31780. 1 Publication
Sequence conflicti2085 – 20851C → P in AAA41144. 1 Publication
Sequence conflicti2106 – 21061A → V in AAA57219. 1 Publication
Sequence conflicti2106 – 21061A → V in AAA41145. 1 Publication
Sequence conflicti2106 – 21061A → V in CAA31882. 1 Publication
Sequence conflicti2296 – 22961Y → H in AAA57219. 1 Publication
Sequence conflicti2296 – 22961Y → H in CAA31882. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M76767 mRNA. Translation: AAA57219.1.
X62888 mRNA. Translation: CAA44679.1.
X62889 Genomic DNA. Translation: CAA44680.1.
M84761 Genomic DNA. Translation: AAA41145.1.
X13415 mRNA. Translation: CAA31780.1.
X13527 mRNA. Translation: CAA31882.1.
J03514 mRNA. Translation: AAA41144.1.
PIRiA30313. XYRTFA.
RefSeqiNP_059028.1. NM_017332.1.
UniGeneiRn.9486.

Genome annotation databases

EnsembliENSRNOT00000073321; ENSRNOP00000064445; ENSRNOG00000045636.
GeneIDi50671.
KEGGirno:50671.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M76767 mRNA. Translation: AAA57219.1 .
X62888 mRNA. Translation: CAA44679.1 .
X62889 Genomic DNA. Translation: CAA44680.1 .
M84761 Genomic DNA. Translation: AAA41145.1 .
X13415 mRNA. Translation: CAA31780.1 .
X13527 mRNA. Translation: CAA31882.1 .
J03514 mRNA. Translation: AAA41144.1 .
PIRi A30313. XYRTFA.
RefSeqi NP_059028.1. NM_017332.1.
UniGenei Rn.9486.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2PNG NMR - A 2114-2202 [» ]
ProteinModelPortali P12785.
SMRi P12785. Positions 423-819, 2114-2202, 2216-2501.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248415. 2 interactions.
DIPi DIP-33893N.
MINTi MINT-4564064.

Chemistry

BindingDBi P12785.
ChEMBLi CHEMBL3783.

Proteomic databases

PRIDEi P12785.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000073321 ; ENSRNOP00000064445 ; ENSRNOG00000045636 .
GeneIDi 50671.
KEGGi rno:50671.

Organism-specific databases

CTDi 2194.
RGDi 620665. Fasn.

Phylogenomic databases

GeneTreei ENSGT00530000063309.
HOVERGENi HBG005640.
KOi K00665.
OMAi ATGQMAI.
OrthoDBi EOG71K623.
PhylomeDBi P12785.

Enzyme and pathway databases

Reactomei REACT_198613. Activation of gene expression by SREBF (SREBP).
SABIO-RK P12785.

Miscellaneous databases

EvolutionaryTracei P12785.
NextBioi 610498.
PROi P12785.

Gene expression databases

Genevestigatori P12785.

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.
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.
IPR013217. Methyltransf_12.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
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.
PF00107. ADH_zinc_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF08242. Methyltransf_12. 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. "Molecular cloning and sequencing of cDNAs encoding the entire rat fatty acid synthase."
    Amy C.M., Witkowski A., Naggert J., Williams B., Randhawa Z., Smith S.
    Proc. Natl. Acad. Sci. U.S.A. 86:3114-3118(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The fatty acid synthase (FAS) gene and its promoter in Rattus norvegicus."
    Beck K.F., Schreglmann R., Stathopulos I., Klein H., Hoch J., Schweizer M.
    DNA Seq. 2:359-386(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  3. "Intron-exon organization of the gene for the multifunctional animal fatty acid synthase."
    Amy C.M., Williams-Ahlf B., Naggert J., Smith S.
    Proc. Natl. Acad. Sci. U.S.A. 89:1105-1108(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Rat mammary gland fatty acid synthase: localization of the constituent domains and two functional polyadenylation/termination signals in the cDNA."
    Schweizer M., Takabeyashi K., Beck K.F., Schreglmann R.
    Nucleic Acids Res. 17:567-586(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-2505.
    Strain: Sprague-Dawley.
    Tissue: Mammary gland.
  5. "Molecular cloning and sequencing of a cDNA encoding the acyl carrier protein and its flanking domains in the mammalian fatty acid synthetase."
    Witlowski A., Naggert J., Mikkelsen J., Smith S.
    Eur. J. Biochem. 165:601-606(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1921-2324.
    Tissue: Mammary gland.
  6. "Molecular cloning and sequencing of a cDNA encoding the thioesterase domain of the rat fatty acid synthetase."
    Naggert J., Witkowski A., Mikkelsen J., Smith S.
    J. Biol. Chem. 263:1146-1150(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2085-2505.
    Tissue: Mammary gland.
  7. "Nutritional control of rat liver fatty acid synthase and S14 mRNA abundance."
    Clarke S.D., Armstrong M.K., Jump D.B.
    J. Nutr. 120:218-224(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 2377-2413, INDUCTION.
  8. "The type I rat fatty acid synthase ACP shows structural homology and analogous biochemical properties to type II ACPs."
    Reed M.A.C., Schweizer M., Szafranska A.E., Arthur C., Nicholson T.P., Cox R.J., Crosby J., Crump M.P., Simpson T.J.
    Org. Biomol. Chem. 1:463-471(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2114-2202.

Entry informationi

Entry nameiFAS_RAT
AccessioniPrimary (citable) accession number: P12785
Secondary accession number(s): O09187
, O09190, Q63577, Q64717
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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