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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 activityPROSITE-ProRule annotation
Active sitei581 – 5811For malonyltransferase activityPROSITE-ProRule annotation
Active sitei878 – 8781For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation
Active sitei2302 – 23021For thioesterase activityPROSITE-ProRule annotation
Active sitei2475 – 24751For thioesterase activityPROSITE-ProRule annotation

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. poly(A) RNA binding Source: Ensembl
  17. protein homodimerization activity Source: RGD
  18. 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
  5. osteoblast differentiation Source: Ensembl
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. extracellular vesicular exosome Source: Ensembl
  2. glycogen granule Source: Ensembl
  3. Golgi apparatus Source: Ensembl
  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-acetylmethionineBy similarity
Modified residuei59 – 591N6-acetyllysineBy similarity
Modified residuei70 – 701N6-acetyllysineBy similarity
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei298 – 2981N6-acetyllysineBy similarity
Modified residuei528 – 5281N6-acetyllysineBy similarity
Modified residuei673 – 6731N6-acetyllysineBy similarity
Modified residuei790 – 7901N6-acetyllysineBy similarity
Modified residuei993 – 9931N6-acetyllysineBy similarity
Modified residuei1276 – 12761N6-acetyllysineBy similarity
Modified residuei1698 – 16981N6-(pyridoxal phosphate)lysine; alternateBy similarity
Modified residuei1698 – 16981N6-acetyllysine; alternateBy similarity
Modified residuei1765 – 17651N6-acetyllysineBy similarity
Modified residuei1841 – 18411N6-acetyllysineBy similarity
Modified residuei1989 – 19891N6-acetyllysineBy similarity
Modified residuei2151 – 21511O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei2230 – 22301PhosphoserineBy similarity
Modified residuei2385 – 23851N6-acetyllysineBy 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12785.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2118 – 217457Acyl carrierPROSITE-ProRule annotationAdd
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

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063309.
HOVERGENiHBG005640.
InParanoidiP12785.
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

« Hide

        10         20         30         40         50
MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR
60 70 80 90 100
SGKLKDLSKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL
110 120 130 140 150
RGTNTGVWVG VSGSEASEAL SRDPETLLGY SMVGCQRAMM ANRLSFFFDF
160 170 180 190 200
KGPSIALDTA CSSSLLALQN AYQAIRSGEC PAAIVGGINL LLKPNTSVQF
210 220 230 240 250
MKLGMLSPDG TCRSFDDSGN GYCRAEAVVA VLLTKKSLAR RVYATILNAG
260 270 280 290 300
TNTDGCKEQG VTFPSGEAQE QLIRSLYQPG GVAPESLEYI EAHGTGTKVG
310 320 330 340 350
DPQELNGITR SLCAFRQSPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEN
360 370 380 390 400
GVWAPNLHFH NPNPEIPALL DGRLQVVDRP LPVRGGIVGI NSFGFGGANV
410 420 430 440 450
HVILQPNTQQ APAPAPHAAL PHLLHASGRT MEAVQGLLEQ GRQHSQDLAF
460 470 480 490 500
VSMLNDIAAT PTAAMPFRGY TVLGVEGHVQ EVQQVPASQR PLWFICSGMG
510 520 530 540 550
TQWRGMGLSL MRLDSFRESI LRSDEALKPL GVKVSDLLLS TDEHTFDDIV
560 570 580 590 600
HSFVSLTAIQ IALIDLLTSM GLKPDGIIGH SLGEVACGYA DGCLSQREAV
610 620 630 640 650
LAAYWRGQCI KDANLPAGSM AAVGLSWEEC KQRCPPGVVP ACHNSEDTVT
660 670 680 690 700
ISGPQAAVNE FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK
710 720 730 740 750
VIREPRPRSA RWLSTSIPEA QWQSSLARTS SAEYNVNNLV SPVLFQEALW
760 770 780 790 800
HVPEHAVVLE IAPHALLQAV LKRGVKPSCT IIPLMKRDHK DNLEFFLTNL
810 820 830 840 850
GKVHLTGIDI NPNALFPPVE FPVPRGTPLI SPHIKWDHSQ TWDIPVAEDF
860 870 880 890 900
PNGSSSSSAT VYNIDASSES SDHYLVDHCI DGRVLFPGTG YLYLVWKTLA
910 920 930 940 950
RSLSLSLEET PVVFENVTFH QATILPRTGT VPLEVRLLEA SHAFEVSDSG
960 970 980 990 1000
NLIVSGKVYQ WEDPDSKLFD HPEVPIPAES ESVSRLTQGE VYKELRLRGY
1010 1020 1030 1040 1050
DYGPHFQGVY EATLEGEQGK LLWKDNWVTF MDTMLQISIL GFSKQSLQLP
1060 1070 1080 1090 1100
TRVTAIYIDP ATHLQKVYML EGDTQVADVT TSRCLGVTVS GGVYISRLQT
1110 1120 1130 1140 1150
TATSRRQQEQ LVPTLEKFVF TPHVEPECLS ESAILQKELQ LCKGLAKALQ
1160 1170 1180 1190 1200
TKATQQGLKM TVPGLEDLPQ HGLPRLLAAA CQLQLNGNLQ LELGEVLARE
1210 1220 1230 1240 1250
RLLLPEDPLI SGLLNSQALK ACIDTALENL STLKMKVVEV LAGEGHLYSH
1260 1270 1280 1290 1300
ISALLNTQPM LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWDPSGPAPT
1310 1320 1330 1340 1350
NLGALDLVVC NCALATLGDP ALALDNMVAA LKDGGFLLMH TVLKGHALGE
1360 1370 1380 1390 1400
TLACLPSEVQ PGPSFLSQEE WESLFSRKAL HLVGLKKSFY GTALFLCRRL
1410 1420 1430 1440 1450
SPQDKPIFLP VEDTSFQWVD SLKSILATSS SQPVWLTAMN CPTSGVVGLV
1460 1470 1480 1490 1500
NCLRKEPGGH RIRCILLSNL SSTSHVPKLD PGSSELQKVL ESDLVMNVYR
1510 1520 1530 1540 1550
DGAWGAFRHF QLEQDKPEEQ TAHAFVNVLT RGDLASIRWV SSPLKHMQPP
1560 1570 1580 1590 1600
SSSGAQLCTV YYASLNFRDI MLATGKLSPD AIPGKWASRD CMLGMEFSGR
1610 1620 1630 1640 1650
DKCGRRVMGL VPAEGLATSV LLSPDFLWDV PSSWTLEEAA SVPVVYTTAY
1660 1670 1680 1690 1700
YSLVVRGRIQ HGETVLIHSG SGGVGQAAIS IALSLGCRVF TTVGSAEKRA
1710 1720 1730 1740 1750
YLQARFPQLD DTSFANSRDT SFEQHVLLHT GGKGVDLVLN SLAEEKLQAS
1760 1770 1780 1790 1800
VRCLAQHGRF LEIGKFDLSN NHPLGMAIFL KNVTFHGILL DALFEGANDS
1810 1820 1830 1840 1850
WREVAELLKA GIRDGVVKPL KCTVFPKAQV EDAFRYMAQG KHIGKVLVQV
1860 1870 1880 1890 1900
REEEPEAMLP GAQPTLISAI SKTFCPEHKS YIITGGLGGF GLELARWLVL
1910 1920 1930 1940 1950
RGAQRLVLTS RSGIRTGYQA KHVREWRRQG IHVLVSTSNV SSLEGARALI
1960 1970 1980 1990 2000
AEATKLGPVG GVFNLAMVLR DAMLENQTPE LFQDVNKPKY NGTLNLDRAT
2010 2020 2030 2040 2050
REACPELDYF VAFSSVSCGR GNAGQSNYGF ANSTMERICE QRRHDGLPGL
2060 2070 2080 2090 2100
AVQWGAIGDV GIILEAMGTN DTVVGGTLPQ RISSCMEVLD LFLNQPHAVL
2110 2120 2130 2140 2150
SSFVLAEKKA VAHGDGEAQR DLVKAVAHIL GIRDLAGINL DSSLADLGLD
2160 2170 2180 2190 2200
SLMGVEVRQI LEREHDLVLP IREVRQLTLR KLQEMSSKAG SDTELAAPKS
2210 2220 2230 2240 2250
KNDTSLKQAQ LNLSILLVNP EGPTLTRLNS VQSSERPLFL VHPIEGSITV
2260 2270 2280 2290 2300
FHSLAAKLSV PTYGLQCTQA APLDSIPNLA AYYIDCIKQV QPEGPYRVAG
2310 2320 2330 2340 2350
YSFGACVAFE MCSQLQAQQG PAPAHNNLFL FDGSHTYVLA YTQSYRAKLT
2360 2370 2380 2390 2400
PGCEAEAEAE AICFFIKQFV DAEHSKVLEA LLPLKSLEDR VAAAVDLITR
2410 2420 2430 2440 2450
SHQSLDRRDL SFAAVSFYYK LRAADQYKPK AKYHGNVILL RAKTGGTYGE
2460 2470 2480 2490 2500
DLGADYNLSQ VCDGKVSVHI IEGDHRTLLE GRGLESIINI IHSSLAEPRV

SVREG
Length:2,505
Mass (Da):272,650
Last modified:November 1, 1997 - v3
Checksum:i5810EC13D37F3114
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841I → T in AAA41145. (PubMed:1736293)Curated
Sequence conflicti871 – 8711S → P in CAA31780. (PubMed:2915923)Curated
Sequence conflicti2085 – 20851C → P in AAA41144. (PubMed:2891707)Curated
Sequence conflicti2106 – 21061A → V in AAA57219. (PubMed:2717611)Curated
Sequence conflicti2106 – 21061A → V in AAA41145. (PubMed:1736293)Curated
Sequence conflicti2106 – 21061A → V in CAA31882. (PubMed:3109907)Curated
Sequence conflicti2296 – 22961Y → H in AAA57219. (PubMed:2717611)Curated
Sequence conflicti2296 – 22961Y → H in CAA31882. (PubMed:3109907)Curated

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.
InParanoidi P12785.
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: October 29, 2014
This is version 148 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