UniProtKB - P12785 (FAS_RAT)
Fatty acid synthase
Fasn
Functioni
Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain.
1 Publication4 PublicationsCatalytic activityi
- acetyl-CoA + 2n H+ + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP+3 PublicationsEC:2.3.1.853 PublicationsThis reaction proceeds in the forward3 Publications direction.
- EC:2.3.1.383 PublicationsThis reaction proceeds in the forward3 Publications direction.
- EC:2.3.1.391 PublicationThis reaction proceeds in the forward1 Publication direction.
- EC:2.3.1.413 PublicationsThis reaction proceeds in the forward3 Publications direction.
- EC:1.1.1.1003 PublicationsThis reaction proceeds in the backward3 Publications direction.
- EC:4.2.1.591 Publication2 Publications
- EC:1.3.1.393 PublicationsThis reaction proceeds in the backward3 Publications direction.
- EC:3.1.2.143 PublicationsThis reaction proceeds in the forward3 Publications direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- EC:3.1.2.14By similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
Activity regulationi
Kineticsi
- Vmax=300 nmol/min/mg enzyme for the overall fatty acid synthase reaction1 Publication
- Vmax=900 nmol/min/mg enzyme for the beta-ketoacyl reductase reaction of acetoacetyl-CoA1 Publication
- Vmax=25 nmol/min/mg enzyme for the enoyl reductase reaction1 Publication
- Vmax=25 nmol/min/mg enzyme for the thioesterase reaction1 Publication
- Vmax=3 nmol/min/mg enzyme for the beta-ketoacyl synthase reaction2 Publications
- Vmax=16 nmol/min/µg enzyme for the transferase reaction using malonyl-CoA as donor1 Publication
- Vmax=1.6 nmol/min/µg enzyme for the beta-ketoacyl reductase reaction of acetoacetyl-CoA1 Publication
- Vmax=2.5 nmol/min/µg enzyme for the fatty acid synthase reaction1 Publication
- Vmax=0.72 nmol/min/µg enzyme for the thioesterase reaction1 Publication
- Vmax=1.9 nmol/min/µg enzyme for the enoyl reductase reaction1 Publication
: fatty acid biosynthesis Pathwayi
This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.3 PublicationsView all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 161 | For beta-ketoacyl synthase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 581 | For malonyltransferase activityPROSITE-ProRule annotation | 1 | |
Binding sitei | 671 | Acyl-CoABy similarity | 1 | |
Binding sitei | 773 | Acyl-CoABy similarity | 1 | |
Active sitei | 878 | For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2302 | For thioesterase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2475 | For thioesterase activityPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1665 – 1682 | NADP; for enoyl reductase activityAdd BLAST | 18 | |
Nucleotide bindingi | 1765 – 1780 | NADP; for ketoreductase activityAdd BLAST | 16 |
GO - Molecular functioni
- (3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- [acyl-carrier-protein] S-acetyltransferase activity Source: UniProtKB-EC
- [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
- 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
- enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity Source: UniProtKB-EC
- fatty acid synthase activity Source: RGD
- identical protein binding Source: IntAct
- myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
- oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
- palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
- phosphopantetheine binding Source: InterPro
GO - Biological processi
- acetyl-CoA metabolic process Source: RGD
- cellular response to interleukin-4 Source: RGD
- establishment of endothelial intestinal barrier Source: RGD
- ether lipid biosynthetic process Source: RGD
- fatty acid biosynthetic process Source: RGD
- glandular epithelial cell development Source: RGD
- inflammatory response Source: RGD
- lipid biosynthetic process Source: RGD
- mammary gland development Source: RGD
- monocyte differentiation Source: RGD
- neutrophil differentiation Source: RGD
- tissue development Source: RGD
Keywordsi
Molecular function | Hydrolase, Lyase, Multifunctional enzyme, Oxidoreductase, Transferase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Ligand | NAD, NADP, Pyridoxal phosphate |
Enzyme and pathway databases
Reactomei | R-RNO-163765, ChREBP activates metabolic gene expression R-RNO-199220, Vitamin B5 (pantothenate) metabolism R-RNO-75105, Fatty acyl-CoA biosynthesis |
SABIO-RKi | P12785 |
UniPathwayi | UPA00094 |
Protein family/group databases
ESTHERi | ratno-fas, Thioesterase |
Chemistry databases
SwissLipidsi | SLP:000001864 |
Names & Taxonomyi
Protein namesi | Recommended name: Fatty acid synthase (EC:2.3.1.853 Publications)Alternative name(s): Type I FAS1 Publication Including the following 7 domains: [Acyl-carrier-protein] S-acetyltransferase (EC:2.3.1.383 Publications) [Acyl-carrier-protein] S-malonyltransferase (EC:2.3.1.391 Publication) 3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.413 Publications) 3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.1003 Publications) 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.592 Publications) Enoyl-[acyl-carrier-protein] reductase (EC:1.3.1.393 Publications) Acyl-[acyl-carrier-protein] hydrolase (EC:3.1.2.14) |
Gene namesi | Name:Fasn |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 620665, Fasn |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Other locations
- Melanosome By similarity
Cytosol
- cytosol Source: Reactome
Other locations
- cytoplasm Source: UniProtKB
- glycogen granule Source: RGD
- melanosome Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000180279 | 1 – 2505 | Fatty acid synthaseAdd BLAST | 2505 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineBy similarity | 1 | |
Modified residuei | 59 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 63 | PhosphoserineBy similarity | 1 | |
Modified residuei | 70 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 207 | PhosphoserineBy similarity | 1 | |
Modified residuei | 298 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 528 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 673 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 725 | PhosphoserineCombined sources | 1 | |
Modified residuei | 790 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 993 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1276 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1464 | S-nitrosocysteineBy similarity | 1 | |
Modified residuei | 1578 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1588 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1698 | N6-(pyridoxal phosphate)lysine; alternateBy similarity | 1 | |
Modified residuei | 1698 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 1765 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1841 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1989 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 2085 | S-nitrosocysteineBy similarity | 1 | |
Modified residuei | 2151 | O-(pantetheine 4'-phosphoryl)serine; alternatePROSITE-ProRule annotation | 1 | |
Modified residuei | 2151 | Phosphoserine; alternateCombined sources | 1 | |
Modified residuei | 2191 | PhosphoserineCombined sources | 1 | |
Modified residuei | 2230 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2385 | N6-acetyllysineBy similarity | 1 | |
Cross-linki | 2443 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphopantetheine, Phosphoprotein, S-nitrosylation, Ubl conjugationProteomic databases
jPOSTi | P12785 |
PaxDbi | P12785 |
PRIDEi | P12785 |
PTM databases
CarbonylDBi | P12785 |
iPTMneti | P12785 |
PhosphoSitePlusi | P12785 |
Expressioni
Inductioni
Gene expression databases
Bgeei | ENSRNOG00000045636, Expressed in liver and 21 other tissues |
Genevisiblei | P12785, RN |
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 (PubMed:16054098).
By similarity1 PublicationBinary interactionsi
P12785
With | #Exp. | IntAct |
---|---|---|
itself | 9 | EBI-493558,EBI-493558 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 248415, 5 interactors |
DIPi | DIP-33893N |
IntActi | P12785, 2 interactors |
MINTi | P12785 |
STRINGi | 10116.ENSRNOP00000064445 |
Chemistry databases
BindingDBi | P12785 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P12785 |
BMRBi | P12785 |
SMRi | P12785 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P12785 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2113 – 2193 | CarrierPROSITE-ProRule annotationAdd BLAST | 81 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 413 | Beta-ketoacyl synthaseAdd BLAST | 413 | |
Regioni | 429 – 817 | Acyl and malonyl transferasesAdd BLAST | 389 | |
Regioni | 647 – 648 | Acyl-CoA bindingBy similarity | 2 | |
Regioni | 1629 – 1857 | Enoyl reductaseAdd BLAST | 229 | |
Regioni | 1858 – 2113 | Beta-ketoacyl reductaseAdd BLAST | 256 | |
Regioni | 2202 – 2505 | ThioesteraseAdd BLAST | 304 |
Phylogenomic databases
eggNOGi | KOG1202, Eukaryota |
GeneTreei | ENSGT00940000157276 |
HOGENOMi | CLU_000022_31_7_1 |
InParanoidi | P12785 |
OMAi | KMRGGEF |
OrthoDBi | 19161at2759 |
PhylomeDBi | P12785 |
Family and domain databases
Gene3Di | 1.10.1200.10, 1 hit 3.10.129.110, 1 hit 3.40.366.10, 1 hit 3.40.47.10, 1 hit 3.40.50.150, 1 hit 3.40.50.1820, 2 hits |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR001227, Ac_transferase_dom_sf IPR036736, ACP-like_sf IPR014043, Acyl_transferase IPR016035, Acyl_Trfase/lysoPLipase IPR013149, ADH-like_C IPR011032, GroES-like_sf IPR018201, Ketoacyl_synth_AS IPR014031, Ketoacyl_synth_C IPR014030, Ketoacyl_synth_N IPR016036, Malonyl_transacylase_ACP-bd IPR013217, Methyltransf_12 IPR036291, NAD(P)-bd_dom_sf IPR032821, PKS_assoc IPR020841, PKS_Beta-ketoAc_synthase_dom IPR020807, PKS_dehydratase IPR042104, PKS_dehydratase_sf 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 |
Pfami | View protein in Pfam PF00698, 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 |
SMARTi | View protein in SMART SM00827, PKS_AT, 1 hit SM00826, PKS_DH, 1 hit SM00829, PKS_ER, 1 hit SM00825, PKS_KS, 1 hit SM00823, PKS_PP, 1 hit |
SUPFAMi | SSF47336, SSF47336, 1 hit SSF50129, SSF50129, 1 hit SSF51735, SSF51735, 2 hits SSF52151, SSF52151, 1 hit SSF53335, SSF53335, 1 hit SSF53474, SSF53474, 1 hit SSF53901, SSF53901, 1 hit SSF55048, SSF55048, 1 hit |
PROSITEi | View protein in PROSITE PS00606, B_KETOACYL_SYNTHASE, 1 hit PS50075, CARRIER, 1 hit PS00012, PHOSPHOPANTETHEINE, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A8I6A2Z2 | A0A8I6A2Z2_RAT | Fatty acid synthase | Fasn | 2,521 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 184 | I → T in AAA41145 (PubMed:1736293).Curated | 1 | |
Sequence conflicti | 871 | S → P in CAA31780 (PubMed:2915923).Curated | 1 | |
Sequence conflicti | 2085 | C → P in AAA41144 (PubMed:2891707).Curated | 1 | |
Sequence conflicti | 2106 | A → V in AAA57219 (PubMed:2717611).Curated | 1 | |
Sequence conflicti | 2106 | A → V in AAA41145 (PubMed:1736293).Curated | 1 | |
Sequence conflicti | 2106 | A → V in CAA31882 (PubMed:3109907).Curated | 1 | |
Sequence conflicti | 2296 | Y → H in AAA57219 (PubMed:2717611).Curated | 1 | |
Sequence conflicti | 2296 | Y → H in CAA31882 (PubMed:3109907).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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 |
Genome annotation databases
Ensembli | ENSRNOT00000073321; ENSRNOP00000064445; ENSRNOG00000045636 |
GeneIDi | 50671 |
KEGGi | rno:50671 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2PNG | NMR | - | A | 2114-2202 | [»] | |
AlphaFoldDBi | P12785 | |||||
BMRBi | P12785 | |||||
SMRi | P12785 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 248415, 5 interactors |
DIPi | DIP-33893N |
IntActi | P12785, 2 interactors |
MINTi | P12785 |
STRINGi | 10116.ENSRNOP00000064445 |
Chemistry databases
BindingDBi | P12785 |
ChEMBLi | CHEMBL3783 |
SwissLipidsi | SLP:000001864 |
Protein family/group databases
ESTHERi | ratno-fas, Thioesterase |
PTM databases
CarbonylDBi | P12785 |
iPTMneti | P12785 |
PhosphoSitePlusi | P12785 |
Proteomic databases
jPOSTi | P12785 |
PaxDbi | P12785 |
PRIDEi | P12785 |
Genome annotation databases
Ensembli | ENSRNOT00000073321; ENSRNOP00000064445; ENSRNOG00000045636 |
GeneIDi | 50671 |
KEGGi | rno:50671 |
Organism-specific databases
CTDi | 2194 |
RGDi | 620665, Fasn |
Phylogenomic databases
eggNOGi | KOG1202, Eukaryota |
GeneTreei | ENSGT00940000157276 |
HOGENOMi | CLU_000022_31_7_1 |
InParanoidi | P12785 |
OMAi | KMRGGEF |
OrthoDBi | 19161at2759 |
PhylomeDBi | P12785 |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
Reactomei | R-RNO-163765, ChREBP activates metabolic gene expression R-RNO-199220, Vitamin B5 (pantothenate) metabolism R-RNO-75105, Fatty acyl-CoA biosynthesis |
SABIO-RKi | P12785 |
Miscellaneous databases
EvolutionaryTracei | P12785 |
PROi | PR:P12785 |
Gene expression databases
Bgeei | ENSRNOG00000045636, Expressed in liver and 21 other tissues |
Genevisiblei | P12785, RN |
Family and domain databases
Gene3Di | 1.10.1200.10, 1 hit 3.10.129.110, 1 hit 3.40.366.10, 1 hit 3.40.47.10, 1 hit 3.40.50.150, 1 hit 3.40.50.1820, 2 hits |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR001227, Ac_transferase_dom_sf IPR036736, ACP-like_sf IPR014043, Acyl_transferase IPR016035, Acyl_Trfase/lysoPLipase IPR013149, ADH-like_C IPR011032, GroES-like_sf IPR018201, Ketoacyl_synth_AS IPR014031, Ketoacyl_synth_C IPR014030, Ketoacyl_synth_N IPR016036, Malonyl_transacylase_ACP-bd IPR013217, Methyltransf_12 IPR036291, NAD(P)-bd_dom_sf IPR032821, PKS_assoc IPR020841, PKS_Beta-ketoAc_synthase_dom IPR020807, PKS_dehydratase IPR042104, PKS_dehydratase_sf 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 |
Pfami | View protein in Pfam PF00698, 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 |
SMARTi | View protein in SMART SM00827, PKS_AT, 1 hit SM00826, PKS_DH, 1 hit SM00829, PKS_ER, 1 hit SM00825, PKS_KS, 1 hit SM00823, PKS_PP, 1 hit |
SUPFAMi | SSF47336, SSF47336, 1 hit SSF50129, SSF50129, 1 hit SSF51735, SSF51735, 2 hits SSF52151, SSF52151, 1 hit SSF53335, SSF53335, 1 hit SSF53474, SSF53474, 1 hit SSF53901, SSF53901, 1 hit SSF55048, SSF55048, 1 hit |
PROSITEi | View protein in PROSITE PS00606, B_KETOACYL_SYNTHASE, 1 hit PS50075, CARRIER, 1 hit PS00012, PHOSPHOPANTETHEINE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | FAS_RAT | |
Accessioni | P12785Primary (citable) accession number: P12785 Secondary accession number(s): O09187 Q64717 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1989 |
Last sequence update: | November 1, 1997 | |
Last modified: | May 25, 2022 | |
This is version 202 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references