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Protein

Fatty acid synthase

Gene

Fasn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei161For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei581For malonyltransferase activityPROSITE-ProRule annotation1
Active sitei878For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation1
Active sitei2301For thioesterase activityPROSITE-ProRule annotation1
Active sitei2474For thioesterase activityPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1664 – 1681NADP (ER)By similarityAdd BLAST18
Nucleotide bindingi1879 – 1894NADP (KR)By similarityAdd BLAST16

GO - Molecular functioni

GO - Biological processi

  • acetyl-CoA metabolic process Source: Ensembl
  • cellular response to interleukin-4 Source: MGI
  • fatty acid biosynthetic process Source: MGI
  • mammary gland development Source: CACAO
  • osteoblast differentiation Source: MGI
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

ReactomeiR-MMU-163765. ChREBP activates metabolic gene expression.
R-MMU-199220. Vitamin B5 (pantothenate) metabolism.
R-MMU-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Protein family/group databases

ESTHERimouse-FASN. Thioesterase.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:95485. Fasn.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • glycogen granule Source: MGI
  • Golgi apparatus Source: MGI
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: MGI
  • mitochondrion Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1795189.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001802771 – 2504Fatty acid synthaseAdd BLAST2504

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei59N6-acetyllysineCombined sources1
Modified residuei63PhosphoserineBy similarity1
Modified residuei70N6-acetyllysineBy similarity1
Modified residuei207PhosphoserineBy similarity1
Modified residuei298N6-acetyllysineBy similarity1
Modified residuei528N6-acetyllysineBy similarity1
Modified residuei673N6-acetyllysineBy similarity1
Modified residuei725PhosphoserineCombined sources1
Modified residuei790N6-acetyllysineCombined sources1
Modified residuei993N6-acetyllysineCombined sources1
Modified residuei1071N6-acetyllysineCombined sources1
Modified residuei1276N6-acetyllysineCombined sources1
Modified residuei1577PhosphoserineCombined sources1
Modified residuei1587PhosphoserineCombined sources1
Modified residuei1697N6-(pyridoxal phosphate)lysine; alternateBy similarity1
Modified residuei1697N6-acetyllysine; alternateBy similarity1
Modified residuei1764N6-acetyllysineBy similarity1
Modified residuei1840N6-acetyllysineCombined sources1
Modified residuei1988N6-acetyllysineBy similarity1
Modified residuei2150O-(pantetheine 4'-phosphoryl)serine; alternatePROSITE-ProRule annotation1
Modified residuei2150Phosphoserine; alternateBy similarity1
Modified residuei2190PhosphoserineCombined sources1
Modified residuei2229PhosphoserineBy similarity1
Modified residuei2384N6-acetyllysineCombined sources1
Cross-linki2442Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphopantetheine, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP19096.
MaxQBiP19096.
PaxDbiP19096.
PeptideAtlasiP19096.
PRIDEiP19096.

PTM databases

iPTMnetiP19096.
PhosphoSitePlusiP19096.
SwissPalmiP19096.

Expressioni

Gene expression databases

BgeeiENSMUSG00000025153.
CleanExiMM_FASN.
ExpressionAtlasiP19096. baseline and differential.
GenevisibleiP19096. MM.

Interactioni

Subunit structurei

Homodimer which is arranged in a head to tail fashion (By similarity). Interacts with CEACAM1; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199596. 4 interactors.
IntActiP19096. 8 interactors.
MINTiMINT-2514287.
STRINGi10090.ENSMUSP00000052872.

Chemistry databases

BindingDBiP19096.

Structurei

3D structure databases

ProteinModelPortaliP19096.
SMRiP19096.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2117 – 2173Acyl carrierPROSITE-ProRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 414Beta-ketoacyl synthaseAdd BLAST414
Regioni429 – 817Acyl and malonyl transferasesAdd BLAST389
Regioni1628 – 1856Enoyl reductaseAdd BLAST229
Regioni1857 – 2111Beta-ketoacyl reductaseAdd BLAST255
Regioni2201 – 2504ThioesteraseAdd BLAST304

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1202. Eukaryota.
COG3321. LUCA.
GeneTreeiENSGT00530000063309.
HOGENOMiHOG000019642.
HOVERGENiHBG005640.
InParanoidiP19096.
KOiK00665.
OMAiEVARECI.
OrthoDBiEOG091G003K.
PhylomeDBiP19096.
TreeFamiTF300549.

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.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR023102. Fatty_acid_synthase_dom_2.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
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.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR029063. SAM-dependent_MTases.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF16197. KAsynt_C_assoc. 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.
PF14765. PS-DH. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00826. PKS_DH. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 2 hits.
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.

P19096-1 [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 PAALVGGINL LLKPNTSVQF
210 220 230 240 250
MKLGMLSPDG TCRSFDDSGS GYCRSEAVVA VLLTKKSLAR RVYATILNAG
260 270 280 290 300
TNTDGSKEQG VTFPSGEVQE QLICSLYQPA GLAPESLEYI EAHGTGTKVG
310 320 330 340 350
DPQELNGITR SLCAFRQAPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEH
360 370 380 390 400
GVWAPNLHFH NPNPEIPALL DGRLQVVDRP LPVRGGNVGI NSFGFGGSNV
410 420 430 440 450
HVILQPNTRQ APAPTAHAAL PHLLHASGRT LEAVQDLLEQ GRQHSQDLAF
460 470 480 490 500
VSMLNDIAAT PTAAMPFRGY TVLGVEGRVQ EVQQVSTNKR PLWFICSGMG
510 520 530 540 550
TQWRGMGLSL MRLDSFRESI LRSDEAVKPL GVKVSDLLLS TDERTFDDIV
560 570 580 590 600
HAFVSLTAIQ IALIDLLTSV GLKPDGIIGH SLGEVACGYA DGCLSQREAV
610 620 630 640 650
LAAYWRGQCI KDAHLPPGSM AAVGLSWEEC KQRCPAGVVP 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
HIPEHAVVLE IAPHALLQAV LKRGVKSSCT IIPLMKRDHK DNLEFFLTNL
810 820 830 840 850
GKVHLTGINV NPNALFPPVE FPAPRGTPLI SPHIKWDHSQ TWDVPVAEDF
860 870 880 890 900
PNGSSSSSAT VYSIDASPES PDHYLVDHCI DGRVIFPGTG YLCLVWKTLA
910 920 930 940 950
RSLGLSLEET PVVFENVSFH QATILPKTGT VALEVRLLEA SHAFEVSDTG
960 970 980 990 1000
NLIVSGKVYL WEDPNSKLFD HPEVPTPPES ASVSRLTQGE VYKELRLRGY
1010 1020 1030 1040 1050
DYGPQFQGIC EATLEGEQGK LLWKDNWVTF MDTMLQVSIL GSSQQSLQLP
1060 1070 1080 1090 1100
TRVTAIYIDP ATHRQKVYRL KEDTQVADVT TSRCLGITVS GGIHISRLQT
1110 1120 1130 1140 1150
TATSRRQQEQ LVPTLEKFVF TPHMEAECLS ESTALQKELQ LCKGLARALQ
1160 1170 1180 1190 1200
TKATQQGLKA AMLGQEDPPQ HGLPRLLAAA CQLQLNGNLQ LELGEALAQE
1210 1220 1230 1240 1250
RLLLPEDPLI SGLLNSQALK ACVDTALENL STLKMKVAEV LAGEGHLYSR
1260 1270 1280 1290 1300
IPALLNTQPM LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWNPSDPAPS
1310 1320 1330 1340 1350
SLGALDLLVC NCALATLGDP ALALDNMVAA LKEGGFLLVH TVLKGHALGE
1360 1370 1380 1390 1400
TLACLPSEVQ PAPSLLSQEE WESLFSRKAL HLVGLKRSFY GTALFLCRRA
1410 1420 1430 1440 1450
IPQEKPIFLS VEDTSFQWVD SLKSTLATSS SQPVWLTAMD CPTSGVVGLV
1460 1470 1480 1490 1500
NCLRKEPGGH RIRCILLSNL SNTSHAPKLD PGSPELQQVL KHDLVMNVYR
1510 1520 1530 1540 1550
DGAWGAFRHF QLEQDKPKEQ TAHAFVNVLT RGDLASIRWV SSPLKHTQPS
1560 1570 1580 1590 1600
SSGAQLCTVY YASLNFRDIM LATGKLSPDA IPGKWASRDC MLGMEFSGRD
1610 1620 1630 1640 1650
RCGRRVMGLV PAEGLATSVL LSSDFLWDVP SSWTLEEAAS VPVVYTTAYY
1660 1670 1680 1690 1700
SLVVRGRIQR GETVLIHSGS GGVGQAAISI ALSLGCRVFT TVGSAEKRAY
1710 1720 1730 1740 1750
LQARFPQLDD TSFANSRDTS FEQHVLLHTG GKGVDLVLNS LAEEKLQASV
1760 1770 1780 1790 1800
RCLAQHGRFL EIGKFDLSNN HPLGMAIFLK NVTFHGILLD ALFEEANDSW
1810 1820 1830 1840 1850
REVAALLKAG IRDGVVKPLK CTVFPKAQVE DAFRYMAQGK HIGKVLVQVR
1860 1870 1880 1890 1900
EEEPEAVLPG AQPTLISAIS KTFCPAHKSY IITGGLGGFG LELARWLVLR
1910 1920 1930 1940 1950
GAQRLVLTSR SGIRTGYQAK HIREWRRQGI QVLVSTSNVS SLEGARALIA
1960 1970 1980 1990 2000
EATKLGPVGG VFNLAMVLRD AMLENQTPEL FQDVNKPKYN GTLNLDRATR
2010 2020 2030 2040 2050
EACPELDYFV AFSSVSCGRG NAGQTNYGFA NSTMERICEQ RRHDGLPGLA
2060 2070 2080 2090 2100
VQWGAIGDVG IVLEAMGTND TVIGGTLPQR ISSCMEVLDL FLNQPHAVLS
2110 2120 2130 2140 2150
SFVLAEKKAV AHGDGDTQRD LVKAVAHILG IRDLAGINLD STLADLGLDS
2160 2170 2180 2190 2200
LMGVEVRQIL EREHDLVLPM REVRQLTLRK LQEMSSKTDS ATDTTAPKSR
2210 2220 2230 2240 2250
SDTSLKQNQL NLSTLLVNPE GPTLTQLNSV QSSERPLFLV HPIEGSTTVF
2260 2270 2280 2290 2300
HSLAAKLSVP TYGLQCTQAA PLDSIPNLAA YYIDCIKQVQ PEGPYRIAGY
2310 2320 2330 2340 2350
SFGACVAFEM CSQLQAQQGP APTHNNLFLF DGSHTYVLAY TQSYRAKMTP
2360 2370 2380 2390 2400
GCEAEAEAEA LCFFIKQFLD VEHSKVLEAL LPLKSLEDRV AASVDLITKS
2410 2420 2430 2440 2450
HHSLDRRELS FAAVSFYHKL RAADQYKPKA KYHGNVTLLR AKTGGTYGED
2460 2470 2480 2490 2500
LGADYNLSQV CDGKVSVHII EGDHRTLLEG SGLESIINII HSSLAEPRVS

VREG
Length:2,504
Mass (Da):272,428
Last modified:October 11, 2004 - v2
Checksum:i2B48068B9D370C6F
GO

Sequence cautioni

The sequence CAA31525 differs from that shown. Reason: Frameshift at positions 1842, 1855, 1863, 1964 and 1967.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1992T → N in CAA31525 (PubMed:2920037).Curated1
Sequence conflicti2028G → C in CAA31525 (PubMed:2920037).Curated1
Sequence conflicti2045G → V in CAA31525 (PubMed:2920037).Curated1
Sequence conflicti2117T → N in CAA31525 (PubMed:2920037).Curated1
Sequence conflicti2175Q → R in CAA31525 (PubMed:2920037).Curated1
Sequence conflicti2295Y → H in CAA31525 (PubMed:2920037).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF127033 mRNA. Translation: AAG02285.1.
AL663090 Genomic DNA. Translation: CAM27545.1.
BC046513 mRNA. Translation: AAH46513.1.
BC059850 mRNA. Translation: AAH59850.1.
AK080374 mRNA. Translation: BAC37895.1.
X13135 mRNA. Translation: CAA31525.1. Frameshift.
CCDSiCCDS25759.1.
PIRiA32262.
RefSeqiNP_032014.3. NM_007988.3.
UniGeneiMm.236443.

Genome annotation databases

EnsembliENSMUST00000055655; ENSMUSP00000052872; ENSMUSG00000025153.
GeneIDi14104.
KEGGimmu:14104.
UCSCiuc007mut.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF127033 mRNA. Translation: AAG02285.1.
AL663090 Genomic DNA. Translation: CAM27545.1.
BC046513 mRNA. Translation: AAH46513.1.
BC059850 mRNA. Translation: AAH59850.1.
AK080374 mRNA. Translation: BAC37895.1.
X13135 mRNA. Translation: CAA31525.1. Frameshift.
CCDSiCCDS25759.1.
PIRiA32262.
RefSeqiNP_032014.3. NM_007988.3.
UniGeneiMm.236443.

3D structure databases

ProteinModelPortaliP19096.
SMRiP19096.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199596. 4 interactors.
IntActiP19096. 8 interactors.
MINTiMINT-2514287.
STRINGi10090.ENSMUSP00000052872.

Chemistry databases

BindingDBiP19096.
ChEMBLiCHEMBL1795189.

Protein family/group databases

ESTHERimouse-FASN. Thioesterase.

PTM databases

iPTMnetiP19096.
PhosphoSitePlusiP19096.
SwissPalmiP19096.

Proteomic databases

EPDiP19096.
MaxQBiP19096.
PaxDbiP19096.
PeptideAtlasiP19096.
PRIDEiP19096.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055655; ENSMUSP00000052872; ENSMUSG00000025153.
GeneIDi14104.
KEGGimmu:14104.
UCSCiuc007mut.1. mouse.

Organism-specific databases

CTDi2194.
MGIiMGI:95485. Fasn.

Phylogenomic databases

eggNOGiKOG1202. Eukaryota.
COG3321. LUCA.
GeneTreeiENSGT00530000063309.
HOGENOMiHOG000019642.
HOVERGENiHBG005640.
InParanoidiP19096.
KOiK00665.
OMAiEVARECI.
OrthoDBiEOG091G003K.
PhylomeDBiP19096.
TreeFamiTF300549.

Enzyme and pathway databases

ReactomeiR-MMU-163765. ChREBP activates metabolic gene expression.
R-MMU-199220. Vitamin B5 (pantothenate) metabolism.
R-MMU-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

PROiP19096.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025153.
CleanExiMM_FASN.
ExpressionAtlasiP19096. baseline and differential.
GenevisibleiP19096. MM.

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.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR023102. Fatty_acid_synthase_dom_2.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
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.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR029063. SAM-dependent_MTases.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF16197. KAsynt_C_assoc. 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.
PF14765. PS-DH. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00826. PKS_DH. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 2 hits.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiFAS_MOUSE
AccessioniPrimary (citable) accession number: P19096
Secondary accession number(s): B1ATU8
, Q6PB72, Q8C4Z0, Q9EQR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 11, 2004
Last modified: November 30, 2016
This is version 171 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.