P19096 (FAS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fatty acid synthase
EC=2.3.1.85

Including the following 7 domains:

1. [Acyl-carrier-protein] S-acetyltransferase
   EC=2.3.1.38
2. [Acyl-carrier-protein] S-malonyltransferase
   EC=2.3.1.39
3. 3-oxoacyl-[acyl-carrier-protein] synthase
   EC=2.3.1.41
4. 3-oxoacyl-[acyl-carrier-protein] reductase
   EC=1.1.1.100
5. 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
   EC=4.2.1.59
6. Enoyl-[acyl-carrier-protein] reductase
   EC=1.3.1.10
7. Oleoyl-[acyl-carrier-protein] hydrolase
   EC=3.1.2.14

Gene names

Name:

Fasn

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2504 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	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 + [acyl-carrier-protein] = CoA + 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. Acyl-[acyl-carrier-protein] + NADP+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH. Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.
Subunit structure	Homodimer which is arranged in a head to tail fashion.
Subcellular location	Cytoplasm By similarity. Melanosome By similarity.
Sequence similarities	Contains 1 acyl carrier domain.
Sequence caution	The sequence CAA31525.1 differs from that shown. Reason: Frameshift at positions 1842, 1855, 1863, 1964 and 1967.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Ligand	NAD NADP Phosphopantetheine Pyridoxal phosphate
Molecular function	Hydrolase Lyase Oxidoreductase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA metabolic process Inferred from electronic annotation. Source: Compara cellular response to interleukin-4 Inferred from direct assay PubMed 9798653. Source: MGI fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara glycogen granule Inferred from direct assay PubMed 15169678. Source: MGI melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Inferred from electronic annotation. Source: EC 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Inferred from electronic annotation. Source: InterPro 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Inferred from electronic annotation. Source: EC 3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: EC NADPH binding Inferred from electronic annotation. Source: Compara [acyl-carrier-protein] S-acetyltransferase activity Inferred from electronic annotation. Source: EC [acyl-carrier-protein] S-malonyltransferase activity Inferred from electronic annotation. Source: EC drug binding Inferred from electronic annotation. Source: Compara enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Inferred from electronic annotation. Source: EC myristoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: EC oleoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: EC palmitoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2504	2504	Fatty acid synthase		PRO_0000180277
Regions
	Domain	2117 – 2173	57	Acyl carrier
	Nucleotide binding	1664 – 1681	18	NADP (ER) By similarity
	Nucleotide binding	1879 – 1894	16	NADP (KR) By similarity
	Region	1 – 414	414	Beta-ketoacyl synthase
	Region	429 – 817	389	Acyl and malonyl transferases
	Region	1628 – 1856	229	Enoyl reductase
	Region	1857 – 2111	255	Beta-ketoacyl reductase
	Region	2201 – 2504	304	Thioesterase
Sites
	Active site	161	1	For beta-ketoacyl synthase activity By similarity
	Active site	581	1	For malonyltransferase activity By similarity
	Active site	878	1	For beta-hydroxyacyl dehydratase activity By similarity
	Active site	2301	1	For thioesterase activity By similarity
	Active site	2474	1	For thioesterase activity By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.4
	Modified residue	70	1	N6-acetyllysine By similarity
	Modified residue	207	1	Phosphoserine By similarity
	Modified residue	298	1	N6-acetyllysine By similarity
	Modified residue	528	1	N6-acetyllysine By similarity
	Modified residue	673	1	N6-acetyllysine By similarity
	Modified residue	1697	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	1697	1	N6-acetyllysine By similarity
	Modified residue	1764	1	N6-acetyllysine By similarity
	Modified residue	1840	1	N6-acetyllysine By similarity
	Modified residue	1988	1	N6-acetyllysine By similarity
	Modified residue	2150	1	O-(pantetheine 4'-phosphoryl)serine By similarity
	Modified residue	2229	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	1992	1	T → N in CAA31525. Ref.6
	Sequence conflict	2028	1	G → C in CAA31525. Ref.6
	Sequence conflict	2045	1	G → V in CAA31525. Ref.6
	Sequence conflict	2117	1	T → N in CAA31525. Ref.6
	Sequence conflict	2175	1	Q → R in CAA31525. Ref.6
	Sequence conflict	2295	1	Y → H in CAA31525. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P19096 [UniParc]. Last modified October 11, 2004. Version 2. Checksum: 2B48068B9D370C6F	FASTA	2,504	272,428
	10 20 30 40 50 60 MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR SGKLKDLSKF 70 80 90 100 110 120 DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL RGTNTGVWVG VSGSEASEAL 130 140 150 160 170 180 SRDPETLLGY SMVGCQRAMM ANRLSFFFDF KGPSIALDTA CSSSLLALQN AYQAIRSGEC 190 200 210 220 230 240 PAALVGGINL LLKPNTSVQF MKLGMLSPDG TCRSFDDSGS GYCRSEAVVA VLLTKKSLAR 250 260 270 280 290 300 RVYATILNAG TNTDGSKEQG VTFPSGEVQE QLICSLYQPA GLAPESLEYI EAHGTGTKVG 310 320 330 340 350 360 DPQELNGITR SLCAFRQAPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEH GVWAPNLHFH 370 380 390 400 410 420 NPNPEIPALL DGRLQVVDRP LPVRGGNVGI NSFGFGGSNV HVILQPNTRQ APAPTAHAAL 430 440 450 460 470 480 PHLLHASGRT LEAVQDLLEQ GRQHSQDLAF VSMLNDIAAT PTAAMPFRGY TVLGVEGRVQ 490 500 510 520 530 540 EVQQVSTNKR PLWFICSGMG TQWRGMGLSL MRLDSFRESI LRSDEAVKPL GVKVSDLLLS 550 560 570 580 590 600 TDERTFDDIV HAFVSLTAIQ IALIDLLTSV GLKPDGIIGH SLGEVACGYA DGCLSQREAV 610 620 630 640 650 660 LAAYWRGQCI KDAHLPPGSM AAVGLSWEEC KQRCPAGVVP ACHNSEDTVT ISGPQAAVNE 670 680 690 700 710 720 FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK VIREPRPRSA RWLSTSIPEA 730 740 750 760 770 780 QWQSSLARTS SAEYNVNNLV SPVLFQEALW HIPEHAVVLE IAPHALLQAV LKRGVKSSCT 790 800 810 820 830 840 IIPLMKRDHK DNLEFFLTNL GKVHLTGINV NPNALFPPVE FPAPRGTPLI SPHIKWDHSQ 850 860 870 880 890 900 TWDVPVAEDF PNGSSSSSAT VYSIDASPES PDHYLVDHCI DGRVIFPGTG YLCLVWKTLA 910 920 930 940 950 960 RSLGLSLEET PVVFENVSFH QATILPKTGT VALEVRLLEA SHAFEVSDTG NLIVSGKVYL 970 980 990 1000 1010 1020 WEDPNSKLFD HPEVPTPPES ASVSRLTQGE VYKELRLRGY DYGPQFQGIC EATLEGEQGK 1030 1040 1050 1060 1070 1080 LLWKDNWVTF MDTMLQVSIL GSSQQSLQLP TRVTAIYIDP ATHRQKVYRL KEDTQVADVT 1090 1100 1110 1120 1130 1140 TSRCLGITVS GGIHISRLQT TATSRRQQEQ LVPTLEKFVF TPHMEAECLS ESTALQKELQ 1150 1160 1170 1180 1190 1200 LCKGLARALQ TKATQQGLKA AMLGQEDPPQ HGLPRLLAAA CQLQLNGNLQ LELGEALAQE 1210 1220 1230 1240 1250 1260 RLLLPEDPLI SGLLNSQALK ACVDTALENL STLKMKVAEV LAGEGHLYSR IPALLNTQPM 1270 1280 1290 1300 1310 1320 LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWNPSDPAPS SLGALDLLVC NCALATLGDP 1330 1340 1350 1360 1370 1380 ALALDNMVAA LKEGGFLLVH TVLKGHALGE TLACLPSEVQ PAPSLLSQEE WESLFSRKAL 1390 1400 1410 1420 1430 1440 HLVGLKRSFY GTALFLCRRA IPQEKPIFLS VEDTSFQWVD SLKSTLATSS SQPVWLTAMD 1450 1460 1470 1480 1490 1500 CPTSGVVGLV NCLRKEPGGH RIRCILLSNL SNTSHAPKLD PGSPELQQVL KHDLVMNVYR 1510 1520 1530 1540 1550 1560 DGAWGAFRHF QLEQDKPKEQ TAHAFVNVLT RGDLASIRWV SSPLKHTQPS SSGAQLCTVY 1570 1580 1590 1600 1610 1620 YASLNFRDIM LATGKLSPDA IPGKWASRDC MLGMEFSGRD RCGRRVMGLV PAEGLATSVL 1630 1640 1650 1660 1670 1680 LSSDFLWDVP SSWTLEEAAS VPVVYTTAYY SLVVRGRIQR GETVLIHSGS GGVGQAAISI 1690 1700 1710 1720 1730 1740 ALSLGCRVFT TVGSAEKRAY LQARFPQLDD TSFANSRDTS FEQHVLLHTG GKGVDLVLNS 1750 1760 1770 1780 1790 1800 LAEEKLQASV RCLAQHGRFL EIGKFDLSNN HPLGMAIFLK NVTFHGILLD ALFEEANDSW 1810 1820 1830 1840 1850 1860 REVAALLKAG IRDGVVKPLK CTVFPKAQVE DAFRYMAQGK HIGKVLVQVR EEEPEAVLPG 1870 1880 1890 1900 1910 1920 AQPTLISAIS KTFCPAHKSY IITGGLGGFG LELARWLVLR GAQRLVLTSR SGIRTGYQAK 1930 1940 1950 1960 1970 1980 HIREWRRQGI QVLVSTSNVS SLEGARALIA EATKLGPVGG VFNLAMVLRD AMLENQTPEL 1990 2000 2010 2020 2030 2040 FQDVNKPKYN GTLNLDRATR EACPELDYFV AFSSVSCGRG NAGQTNYGFA NSTMERICEQ 2050 2060 2070 2080 2090 2100 RRHDGLPGLA VQWGAIGDVG IVLEAMGTND TVIGGTLPQR ISSCMEVLDL FLNQPHAVLS 2110 2120 2130 2140 2150 2160 SFVLAEKKAV AHGDGDTQRD LVKAVAHILG IRDLAGINLD STLADLGLDS LMGVEVRQIL 2170 2180 2190 2200 2210 2220 EREHDLVLPM REVRQLTLRK LQEMSSKTDS ATDTTAPKSR SDTSLKQNQL NLSTLLVNPE 2230 2240 2250 2260 2270 2280 GPTLTQLNSV QSSERPLFLV HPIEGSTTVF HSLAAKLSVP TYGLQCTQAA PLDSIPNLAA 2290 2300 2310 2320 2330 2340 YYIDCIKQVQ PEGPYRIAGY SFGACVAFEM CSQLQAQQGP APTHNNLFLF DGSHTYVLAY 2350 2360 2370 2380 2390 2400 TQSYRAKMTP GCEAEAEAEA LCFFIKQFLD VEHSKVLEAL LPLKSLEDRV AASVDLITKS 2410 2420 2430 2440 2450 2460 HHSLDRRELS FAAVSFYHKL RAADQYKPKA KYHGNVTLLR AKTGGTYGED LGADYNLSQV 2470 2480 2490 2500 CDGKVSVHII EGDHRTLLEG SGLESIINII HSSLAEPRVS VREG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Involvement of fatty acid synthase in axonal development in mouse embryos." Ueno K. Genes Cells 5:859-869(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Brain and Liver.
[4]	Bienvenut W.V. Submitted (JUL-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-12; 225-235; 299-310; 385-409; 469-478; 1252-1270; 1333-1344; 1388-1398; 1501-1508; 1705-1717; 1733-1745; 2124-2132; 2376-2384 AND 2476-2498, ACETYLATION AT MET-1, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Liver.
[5]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1527-2504. Strain: C57BL/6J. Tissue: Thymus.
[6]	"Structure of mouse fatty acid synthase mRNA. Identification of the two NADPH binding sites." Paulauskis J.D., Sul H.S. Biochem. Biophys. Res. Commun. 158:690-695(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1666-2504. Strain: CD-1. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00113223.
PIR	A32262.
RefSeq	NP_032014.3. NM_007988.3.
UniGene	Mm.236443.
3D structure databases
ProteinModelPortal	P19096.
SMR	P19096. Positions 2-853, 1215-2107, 2113-2201, 2211-2484.
ModBase	Search...
Protein-protein interaction databases
IntAct	P19096. 2 interactions.
MINT	MINT-2514287.
PTM databases
PhosphoSite	P19096.
Proteomic databases
PaxDb	P19096.
PRIDE	P19096.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000055655; ENSMUSP00000052872; ENSMUSG00000025153.
GeneID	14104.
KEGG	mmu:14104.
UCSC	uc007mut.1. mouse.
Organism-specific databases
CTD	2194.
MGI	MGI:95485. Fasn.
Phylogenomic databases
eggNOG	COG3319.
GeneTree	ENSGT00530000063309.
HOGENOM	HOG000019642.
HOVERGEN	HBG005640.
InParanoid	B1ATU8.
KO	K00665.
OMA	ITSCMEV.
OrthoDB	EOG4KH2T3.
Gene expression databases
Bgee	P19096.
CleanEx	MM_FASN.
Genevestigator	P19096.
GermOnline	ENSMUSG00000025153. Mus musculus.
Family and domain databases
Gene3D	1.10.1200.10. 1 hit. 1.10.1470.20. 1 hit. 3.40.366.10. 2 hits. 3.40.47.10. 2 hits. 3.40.50.720. 2 hits.
InterPro	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. IPR001031. Thioesterase. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
Pfam	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]
SMART	SM00829. PKS_ER. 1 hit. SM00822. PKS_KR. 1 hit. [Graphical view]
SUPFAM	SSF47336. ACP_like. 1 hit. SSF52151. Acyl_Trfase/lysoPlipase. 1 hit. SSF50129. GroES_like. 1 hit. SSF55048. Malonyl_transacylase_ACP-bd. 1 hit. SSF53901. Thiolase-like. 1 hit.
PROSITE	PS50075. ACP_DOMAIN. 1 hit. PS00606. B_KETOACYL_SYNTHASE. 1 hit. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P19096.
ChEMBL	CHEMBL1795189.
NextBio	285138.
SOURCE	Search...

Entry information

Entry name

FAS_MOUSE

Accession

Primary (citable) accession number: P19096
Secondary accession number(s): B1ATU8 , Q6PB72, Q8C4Z0, Q9EQR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	October 11, 2004
Last modified:	May 29, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program