RAT:FAS

Species (Taxon ID)	Rattus norvegicus (Rat). (10116)
Gene Name(s)	Fasn
Protein Name(s)	Fatty acid synthase [Acyl-carrier-protein] S-acetyltransferase [Acyl-carrier-protein] S-malonyltransferase 3-oxoacyl-[acyl-carrier-protein] synthase 3-oxoacyl-[acyl-carrier-protein] reductase 3-hydroxyacyl-[acyl-carrier-protein] dehydratase Enoyl-[acyl-carrier-protein] reductase Oleoyl-[acyl-carrier-protein] hydrolase
External Links
UniProt	P12785
EMBL	M76767 X62888 X62889 M84761 X13415 X13527 J03514
PIR	A30313
RefSeq	NP_059028.1
UniGene	Rn.9486
PDB	2PNG
PDBsum	2PNG
ProteinModelPortal	P12785
SMR	P12785
BioGrid	248415
DIP	DIP-33893N
MINT	MINT-4564064
BindingDB	P12785
ChEMBL	CHEMBL3783
PRIDE	P12785
Ensembl	ENSRNOT00000073321
GeneID	50671
KEGG	rno:50671
CTD	2194
RGD	620665
GeneTree	ENSGT00530000063309
HOVERGEN	HBG005640
InParanoid	P12785
KO	K00665
OMA	GRELMKY
OrthoDB	EOG71K623
PhylomeDB	P12785
Reactome	REACT_198613 REACT_233245 REACT_251333 REACT_260003
SABIO-RK	P12785
EvolutionaryTrace	P12785
NextBio	610498
PRO	PR:P12785
Proteomes	UP000002494
Genevestigator	P12785
GO	GO:0070062 GO:0042587 GO:0005794 GO:0042470 GO:0005739 GO:0005886 GO:0047451 GO:0004317 GO:0004316 GO:0004315 GO:0004313 GO:0004314 GO:0008144 GO:0047117 GO:0004319 GO:0004312 GO:0042802 GO:0016295 GO:0070402 GO:0004320 GO:0016296 GO:0044822 GO:0042803 GO:0008270 GO:0006084 GO:0071353 GO:0006633 GO:0008610 GO:0001649
Gene3D	1.10.1200.10 1.10.1470.20 3.40.366.10 3.40.47.10 3.40.50.150 3.40.50.1820 3.40.50.720
InterPro	IPR029058 IPR001227 IPR009081 IPR014043 IPR016035 IPR013149 IPR023102 IPR011032 IPR018201 IPR014031 IPR014030 IPR016036 IPR013217 IPR016040 IPR020843 IPR013968 IPR006162 IPR029063 IPR001031 IPR016039 IPR016038
Pfam	PF00698 PF00107 PF00109 PF02801 PF08659 PF08242 PF00550 PF00975
SMART	SM00829 SM00822
SUPFAM	SSF47336 SSF50129 SSF52151 SSF53335 SSF53474 SSF53901 SSF55048
PROSITE	PS50075 PS00606 PS00012

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0004312	fatty acid synthase activity	PMID:21569266^[1]	ECO:0000314			F	Figure 4	complete CACAO 3559
	GO:0004312	fatty acid synthase activity	PMID:21389266^[2]	ECO:0000314			F	Figure 1	complete CACAO 4315
part_of	GO:0005737	cytoplasm	PMID:16054098^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004312	fatty acid synthase activity	PMID:21389266^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004312	fatty acid synthase activity	PMID:21569266^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070402	NADPH binding	PMID:15715522^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:19151726^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008144	drug binding	PMID:15715522^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006633	fatty acid biosynthetic process	PMID:15715522^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006084	acetyl-CoA metabolic process	PMID:18062843^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004312	fatty acid synthase activity	PMID:15715522^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004312	fatty acid synthase activity	PMID:18062843^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:9047334^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P12785	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19151726^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P12785	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15711565^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P12785	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11248039^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P12785	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:10206962^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P12785	F	Seeded From UniProt	complete
involved_in	GO:0090557	establishment of endothelial intestinal barrier	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	P	Seeded From UniProt	complete
involved_in	GO:0071353	cellular response to interleukin-4	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	P	Seeded From UniProt	complete
involved_in	GO:0048468	cell development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	P	Seeded From UniProt	complete
involved_in	GO:0043170	macromolecule metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	P	Seeded From UniProt	complete
part_of	GO:0042587	glycogen granule	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	C	Seeded From UniProt	complete
involved_in	GO:0030879	mammary gland development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	P	Seeded From UniProt	complete
involved_in	GO:0030224	monocyte differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	P	Seeded From UniProt	complete
involved_in	GO:0030223	neutrophil differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	P	Seeded From UniProt	complete
involved_in	GO:0009888	tissue development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	P	Seeded From UniProt	complete
involved_in	GO:0008611	ether lipid biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	P	Seeded From UniProt	complete
involved_in	GO:0006633	fatty acid biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	P	Seeded From UniProt	complete
enables	GO:0004312	fatty acid synthase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P19096 ensembl:ENSMUSP00000052872	F	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P49327 ensembl:ENSP00000304592	C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P49327 ensembl:ENSP00000304592	C	Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P49327 ensembl:ENSP00000304592	C	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016039	F	Seeded From UniProt	complete
enables	GO:0004312	fatty acid synthase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023102	F	Seeded From UniProt	complete
involved_in	GO:0009058	biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001031	P	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020843	F	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001227	F	Seeded From UniProt	complete
enables	GO:0016788	hydrolase activity, acting on ester bonds	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001031	F	Seeded From UniProt	complete
enables	GO:0031177	phosphopantetheine binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020806	F	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013149	P	Seeded From UniProt	complete
enables	GO:0102132	3-oxo-pimeloyl-[acp] methyl ester reductase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.1.1.100	F	Seeded From UniProt	complete
enables	GO:0004313	[acyl-carrier-protein] S-acetyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.1.38	F	Seeded From UniProt	complete
enables	GO:0004314	[acyl-carrier-protein] S-malonyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.1.39	F	Seeded From UniProt	complete
enables	GO:0004315	3-oxoacyl-[acyl-carrier-protein] synthase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.1.41	F	Seeded From UniProt	complete
enables	GO:0004312	fatty acid synthase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.1.85	F	Seeded From UniProt	complete
enables	GO:0008659	(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:4.2.1.59	F	Seeded From UniProt	complete
enables	GO:0004320	oleoyl-[acyl-carrier-protein] hydrolase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.2.14	F	Seeded From UniProt	complete
enables	GO:0016297	acyl-[acyl-carrier-protein] hydrolase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.2.14	F	Seeded From UniProt	complete
enables	GO:0016295	myristoyl-[acyl-carrier-protein] hydrolase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.2.14	F	Seeded From UniProt	complete
enables	GO:0016296	palmitoyl-[acyl-carrier-protein] hydrolase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.2.14	F	Seeded From UniProt	complete
enables	GO:0047451	3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:4.2.1.59	F	Seeded From UniProt	complete
enables	GO:0004316	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.1.1.100	F	Seeded From UniProt	complete
enables	GO:0102131	3-oxo-glutaryl-[acp] methyl ester reductase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.1.1.100	F	Seeded From UniProt	complete
enables	GO:0016419	S-malonyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.1.39	F	Seeded From UniProt	complete
enables	GO:0047117	enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.3.1.39	F	Seeded From UniProt	complete
enables	GO:0016418	S-acetyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.1.38	F	Seeded From UniProt	complete
enables	GO:0019171	3-hydroxyacyl-[acyl-carrier-protein] dehydratase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:4.2.1.59	F	Seeded From UniProt	complete
involved_in	GO:0008610	lipid biosynthetic process	PMID:11971939^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-RNO-5655945	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0443	P	Seeded From UniProt	complete
involved_in	GO:0006631	fatty acid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0276	P	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	P	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F	Seeded From UniProt	complete
involved_in	GO:0006633	fatty acid biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0275	P	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P	Seeded From UniProt	complete
enables	GO:0016829	lyase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0456	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	F	Seeded From UniProt	complete
part_of	GO:0042470	melanosome	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0161	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Alberdi, G et al. (2011) Changes in white adipose tissue metabolism induced by resveratrol in rats. Nutr Metab (Lond) 8 29 PubMed GONUTS page
↑ ^2.0 ^2.1 Wu, M et al. (2011) Antidiabetic and antisteatotic effects of the selective fatty acid synthase (FAS) inhibitor platensimycin in mouse models of diabetes. Proc. Natl. Acad. Sci. U.S.A. 108 5378-83 PubMed GONUTS page
↑ Najjar, SM et al. (2005) Insulin acutely decreases hepatic fatty acid synthase activity. Cell Metab. 2 43-53 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Rendina, AR & Cheng, D (2005) Characterization of the inactivation of rat fatty acid synthase by C75: inhibition of partial reactions and protection by substrates. Biochem. J. 388 895-903 PubMed GONUTS page
↑ ^5.0 ^5.1 Brignole, EJ et al. (2009) Conformational flexibility of metazoan fatty acid synthase enables catalysis. Nat. Struct. Mol. Biol. 16 190-7 PubMed GONUTS page
↑ ^6.0 ^6.1 Huong, DT & Ide, T (2008) Dietary lipoic acid-dependent changes in the activity and mRNA levels of hepatic lipogenic enzymes in rats. Br. J. Nutr. 100 79-87 PubMed GONUTS page
↑ Joshi, AK et al. (1997) Mapping of functional interactions between domains of the animal fatty acid synthase by mutant complementation in vitro. Biochemistry 36 2316-22 PubMed GONUTS page
↑ Asturias, FJ et al. (2005) Structure and molecular organization of mammalian fatty acid synthase. Nat. Struct. Mol. Biol. 12 225-32 PubMed GONUTS page
↑ Chirala, SS et al. (2001) Human fatty acid synthase: role of interdomain in the formation of catalytically active synthase dimer. Proc. Natl. Acad. Sci. U.S.A. 98 3104-8 PubMed GONUTS page
↑ Witkowski, A et al. (1999) Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit. Reevaluation of the side-by-side, antiparallel subunit model. J. Biol. Chem. 274 11557-63 PubMed GONUTS page
↑ Moon, YS et al. (2002) Suppression of fatty acid synthase promoter by polyunsaturated fatty acids. J. Lipid Res. 43 691-8 PubMed GONUTS page

[PMID:21569266-1] 1.0 ^1.1 Alberdi, G et al. (2011) Changes in white adipose tissue metabolism induced by resveratrol in rats. Nutr Metab (Lond) 8 29 PubMed GONUTS page

[PMID:21389266-2] 2.0 ^2.1 Wu, M et al. (2011) Antidiabetic and antisteatotic effects of the selective fatty acid synthase (FAS) inhibitor platensimycin in mouse models of diabetes. Proc. Natl. Acad. Sci. U.S.A. 108 5378-83 PubMed GONUTS page

[PMID:16054098-3] Najjar, SM et al. (2005) Insulin acutely decreases hepatic fatty acid synthase activity. Cell Metab. 2 43-53 PubMed GONUTS page

[PMID:15715522-4] 4.0 ^4.1 ^4.2 ^4.3 Rendina, AR & Cheng, D (2005) Characterization of the inactivation of rat fatty acid synthase by C75: inhibition of partial reactions and protection by substrates. Biochem. J. 388 895-903 PubMed GONUTS page

[PMID:19151726-5] 5.0 ^5.1 Brignole, EJ et al. (2009) Conformational flexibility of metazoan fatty acid synthase enables catalysis. Nat. Struct. Mol. Biol. 16 190-7 PubMed GONUTS page

[PMID:18062843-6] 6.0 ^6.1 Huong, DT & Ide, T (2008) Dietary lipoic acid-dependent changes in the activity and mRNA levels of hepatic lipogenic enzymes in rats. Br. J. Nutr. 100 79-87 PubMed GONUTS page

[PMID:9047334-7] Joshi, AK et al. (1997) Mapping of functional interactions between domains of the animal fatty acid synthase by mutant complementation in vitro. Biochemistry 36 2316-22 PubMed GONUTS page

[PMID:15711565-8] Asturias, FJ et al. (2005) Structure and molecular organization of mammalian fatty acid synthase. Nat. Struct. Mol. Biol. 12 225-32 PubMed GONUTS page

[PMID:11248039-9] Chirala, SS et al. (2001) Human fatty acid synthase: role of interdomain in the formation of catalytically active synthase dimer. Proc. Natl. Acad. Sci. U.S.A. 98 3104-8 PubMed GONUTS page

[PMID:10206962-10] Witkowski, A et al. (1999) Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit. Reevaluation of the side-by-side, antiparallel subunit model. J. Biol. Chem. 274 11557-63 PubMed GONUTS page

[PMID:11971939-11] Moon, YS et al. (2002) Suppression of fatty acid synthase promoter by polyunsaturated fatty acids. J. Lipid Res. 43 691-8 PubMed GONUTS page

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RAT:FAS

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