ID FAS_MOUSE Reviewed; 2504 AA.
AC P19096; B1ATU8; Q6PB72; Q8C4Z0; Q9EQR0;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 27-NOV-2024, entry version 223.
DE RecName: Full=Fatty acid synthase;
DE EC=2.3.1.85 {ECO:0000269|PubMed:29328619};
DE AltName: Full=Type I Fatty Acid Synthase {ECO:0000303|PubMed:31811668};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] S-acetyltransferase;
DE EC=2.3.1.38 {ECO:0000269|PubMed:29328619};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] S-malonyltransferase;
DE EC=2.3.1.39 {ECO:0000269|PubMed:29328619};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
DE EC=2.3.1.41 {ECO:0000269|PubMed:31811668};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE EC=1.1.1.100 {ECO:0000250|UniProtKB:P49327};
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase;
DE EC=4.2.1.59 {ECO:0000250|UniProtKB:P49327};
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase;
DE EC=1.3.1.39 {ECO:0000250|UniProtKB:P49327};
DE Includes:
DE RecName: Full=Acyl-[acyl-carrier-protein] hydrolase;
DE EC=3.1.2.14 {ECO:0000250|UniProtKB:P49327};
GN Name=Fasn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=11029661; DOI=10.1046/j.1365-2443.2000.00369.x;
RA Ueno K.;
RT "Involvement of fatty acid synthase in axonal development in mouse
RT embryos.";
RL Genes Cells 5:859-869(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 1-12; 225-235; 299-310; 385-409; 469-478; 1252-1270;
RP 1333-1344; 1388-1398; 1501-1508; 1705-1717; 1733-1745; 2124-2132; 2376-2384
RP AND 2476-2498, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1527-2504.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1666-2504.
RC STRAIN=CD-1; TISSUE=Liver;
RX PubMed=2920037; DOI=10.1016/0006-291x(89)92776-9;
RA Paulauskis J.D., Sul H.S.;
RT "Structure of mouse fatty acid synthase mRNA. Identification of the two
RT NADPH binding sites.";
RL Biochem. Biophys. Res. Commun. 158:690-695(1989).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-725; SER-1577; SER-1587 AND
RP SER-2190, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INDUCTION BY ENDOCANNABINOID ANANDAMIDE.
RX PubMed=21987372; DOI=10.1002/hep.24733;
RA Jourdan T., Demizieux L., Gresti J., Djaouti L., Gaba L., Verges B.,
RA Degrace P.;
RT "Antagonism of peripheral hepatic cannabinoid receptor-1 improves liver
RT lipid metabolism in mice: evidence from cultured explants.";
RL Hepatology 55:790-799(2012).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=29328619; DOI=10.1021/acschembio.7b00718;
RA Rittner A., Paithankar K.S., Huu K.V., Grininger M.;
RT "Characterization of the Polyspecific Transferase of Murine Type I Fatty
RT Acid Synthase (FAS) and Implications for Polyketide Synthase (PKS)
RT Engineering.";
RL ACS Chem. Biol. 13:723-732(2018).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-790; LYS-993; LYS-1071;
RP LYS-1276; LYS-1840 AND LYS-2384, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11] {ECO:0007744|PDB:6ROP}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 2-852 IN COMPLEX WITH OCTANOATE
RP AND OCTANOYL-COA, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31811668; DOI=10.1002/pro.3797;
RA Rittner A., Paithankar K.S., Himmler A., Grininger M.;
RT "Type I fatty acid synthase trapped in the octanoyl-bound state.";
RL Protein Sci. 29:589-605(2020).
CC -!- FUNCTION: Fatty acid synthetase is a multifunctional enzyme that
CC catalyzes the de novo biosynthesis of long-chain saturated fatty acids
CC starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This
CC multifunctional protein contains 7 catalytic activities and a site for
CC the binding of the prosthetic group 4'-phosphopantetheine of the acyl
CC carrier protein ([ACP]) domain. {ECO:0000269|PubMed:29328619,
CC ECO:0000269|PubMed:31811668}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H(+) = a long-chain
CC fatty acid + (n+1) CoA + n CO2 + 2n NADP(+).; EC=2.3.1.85;
CC Evidence={ECO:0000269|PubMed:29328619};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + acetyl-CoA = acetyl-[ACP] + CoA;
CC Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78446; EC=2.3.1.38;
CC Evidence={ECO:0000269|PubMed:29328619};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41789;
CC Evidence={ECO:0000269|PubMed:29328619};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA;
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC Evidence={ECO:0000269|PubMed:29328619};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC Evidence={ECO:0000269|PubMed:29328619};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + malonyl-[ACP] + H(+) = a 3-oxoacyl-[ACP]
CC + holo-[ACP] + CO2; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41; Evidence={ECO:0000269|PubMed:31811668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC Evidence={ECO:0000269|PubMed:31811668};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + NADPH
CC + H(+); Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC NADPH + H(+); Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.39;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-[ACP] + H2O = hexadecanoate + holo-[ACP] + H(+);
CC Xref=Rhea:RHEA:41932, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78483; EC=3.1.2.14;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxobutanoyl-[ACP] +
CC holo-[ACP] + CO2; Xref=Rhea:RHEA:41800, Rhea:RHEA-COMP:9621,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78446, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450;
CC Evidence={ECO:0000305|PubMed:31811668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41801;
CC Evidence={ECO:0000305|PubMed:31811668};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxobutanoyl-[ACP] + NADPH + H(+) = (3R)-hydroxybutanoyl-
CC [ACP] + NADP(+); Xref=Rhea:RHEA:41804, Rhea:RHEA-COMP:9625,
CC Rhea:RHEA-COMP:9626, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78450, ChEBI:CHEBI:78451;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-[ACP] + NADPH + H(+) = butanoyl-[ACP] + NADP(+);
CC Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78453, ChEBI:CHEBI:78454;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxohexanoyl-[ACP] +
CC holo-[ACP] + CO2; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456;
CC Evidence={ECO:0000305|PubMed:31811668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821;
CC Evidence={ECO:0000305|PubMed:31811668};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxohexanoyl-[ACP] + NADPH + H(+) = (3R)-hydroxyhexanoyl-
CC [ACP] + NADP(+); Xref=Rhea:RHEA:41824, Rhea:RHEA-COMP:9629,
CC Rhea:RHEA-COMP:9630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78456, ChEBI:CHEBI:78457;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexenoyl-[ACP] + NADPH + H(+) = hexanoyl-[ACP] + NADP(+);
CC Xref=Rhea:RHEA:41832, Rhea:RHEA-COMP:9631, Rhea:RHEA-COMP:9632,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78458, ChEBI:CHEBI:78459;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxooctanoyl-[ACP] +
CC holo-[ACP] + CO2; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460;
CC Evidence={ECO:0000269|PubMed:31811668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837;
CC Evidence={ECO:0000269|PubMed:31811668};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxooctanoyl-[ACP] + NADPH + H(+) = (3R)-hydroxyoctanoyl-
CC [ACP] + NADP(+); Xref=Rhea:RHEA:41840, Rhea:RHEA-COMP:9633,
CC Rhea:RHEA-COMP:9634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78460, ChEBI:CHEBI:78461;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octenoyl-[ACP] + NADPH + H(+) = octanoyl-[ACP] + NADP(+);
CC Xref=Rhea:RHEA:41848, Rhea:RHEA-COMP:9635, Rhea:RHEA-COMP:9636,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78462, ChEBI:CHEBI:78463;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxodecanoyl-[ACP] +
CC holo-[ACP] + CO2; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464;
CC Evidence={ECO:0000269|PubMed:31811668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853;
CC Evidence={ECO:0000269|PubMed:31811668};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxodecanoyl-[ACP] + NADPH + H(+) = (3R)-hydroxydecanoyl-
CC [ACP] + NADP(+); Xref=Rhea:RHEA:41856, Rhea:RHEA-COMP:9637,
CC Rhea:RHEA-COMP:9638, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78464, ChEBI:CHEBI:78466;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-decenoyl-[ACP] + NADPH + H(+) = decanoyl-[ACP] + NADP(+);
CC Xref=Rhea:RHEA:41864, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78467, ChEBI:CHEBI:78468;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxododecanoyl-[ACP]
CC + holo-[ACP] + CO2; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469;
CC Evidence={ECO:0000269|PubMed:31811668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869;
CC Evidence={ECO:0000269|PubMed:31811668};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxododecanoyl-[ACP] + NADPH + H(+) = (3R)-hydroxydodecanoyl-
CC [ACP] + NADP(+); Xref=Rhea:RHEA:41872, Rhea:RHEA-COMP:9641,
CC Rhea:RHEA-COMP:9642, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78469, ChEBI:CHEBI:78470;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41873;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-dodecenoyl-[ACP] + NADPH + H(+) = dodecanoyl-[ACP] +
CC NADP(+); Xref=Rhea:RHEA:41880, Rhea:RHEA-COMP:9643, Rhea:RHEA-
CC COMP:9644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65264, ChEBI:CHEBI:78472;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxotetradecanoyl-
CC [ACP] + holo-[ACP] + CO2; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473;
CC Evidence={ECO:0000269|PubMed:31811668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885;
CC Evidence={ECO:0000269|PubMed:31811668};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxotetradecanoyl-[ACP] + NADPH + H(+) = (3R)-
CC hydroxytetradecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41888,
CC Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9646, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78473,
CC ChEBI:CHEBI:78474; Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41889;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] +
CC H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-tetradecenoyl-[ACP] + NADPH + H(+) = tetradecanoyl-[ACP]
CC + NADP(+); Xref=Rhea:RHEA:41896, Rhea:RHEA-COMP:9647, Rhea:RHEA-
CC COMP:9648, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78475, ChEBI:CHEBI:78477;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tetradecanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-
CC oxohexadecanoyl-[ACP] + holo-[ACP] + CO2; Xref=Rhea:RHEA:41900,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649,
CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477,
CC ChEBI:CHEBI:78478; Evidence={ECO:0000269|PubMed:31811668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901;
CC Evidence={ECO:0000269|PubMed:31811668};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxohexadecanoyl-[ACP] + NADPH + H(+) = (3R)-
CC hydroxyhexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41904, Rhea:RHEA-
CC COMP:9649, Rhea:RHEA-COMP:9650, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78478, ChEBI:CHEBI:78480;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] +
CC H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexadecenoyl-[ACP] + NADPH + H(+) = hexadecanoyl-[ACP] +
CC NADP(+); Xref=Rhea:RHEA:41912, Rhea:RHEA-COMP:9651, Rhea:RHEA-
CC COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78481, ChEBI:CHEBI:78483;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxooctadecanoyl-
CC [ACP] + holo-[ACP] + CO2; Xref=Rhea:RHEA:41916, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78483, ChEBI:CHEBI:78487;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxooctadecanoyl-[ACP] + NADPH + H(+) = (3R)-
CC hydroxyoctadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41920, Rhea:RHEA-
CC COMP:9653, Rhea:RHEA-COMP:9654, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78487, ChEBI:CHEBI:78488;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41921;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] +
CC H2O; Xref=Rhea:RHEA:41924, Rhea:RHEA-COMP:9654, Rhea:RHEA-COMP:9655,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78488, ChEBI:CHEBI:78489;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41925;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octadecenoyl-[ACP] + NADPH + H(+) = octadecanoyl-[ACP] +
CC NADP(+); Xref=Rhea:RHEA:41928, Rhea:RHEA-COMP:9655, Rhea:RHEA-
CC COMP:9656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78489, ChEBI:CHEBI:78495;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41929;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tetradecanoyl-[ACP] + H2O = tetradecanoate + holo-[ACP] +
CC H(+); Xref=Rhea:RHEA:30123, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78477; EC=3.1.2.14;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.28 uM for malonyl-CoA {ECO:0000269|PubMed:29328619};
CC KM=1.63 uM for acetyl-CoA {ECO:0000269|PubMed:29328619};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:29328619}.
CC -!- SUBUNIT: Homodimer which is arranged in a head to tail fashion (By
CC similarity). Interacts with CEACAM1; this interaction is insulin and
CC phosphorylation-dependent; reduces fatty-acid synthase activity (By
CC similarity). {ECO:0000250|UniProtKB:P12785,
CC ECO:0000250|UniProtKB:P49327}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
CC {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by endocannabinoid anandamide/AEA.
CC {ECO:0000269|PubMed:21987372}.
CC -!- PTM: S-nitrosylation of Fatty acid synthase at cysteine residues Cys-
CC 1464 or Cys-2084 is important for the enzyme dimerization. In
CC adipocytes, S-nitrosylation of Fatty acid synthase occurs under
CC physiological conditions and gradually increases during adipogenesis.
CC {ECO:0000250|UniProtKB:P49327}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA31525.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF127033; AAG02285.1; -; mRNA.
DR EMBL; AL663090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046513; AAH46513.1; -; mRNA.
DR EMBL; BC059850; AAH59850.1; -; mRNA.
DR EMBL; AK080374; BAC37895.1; -; mRNA.
DR EMBL; X13135; CAA31525.1; ALT_FRAME; mRNA.
DR CCDS; CCDS25759.1; -.
DR PIR; A32262; A32262.
DR RefSeq; NP_032014.3; NM_007988.3.
DR PDB; 5MY0; X-ray; 2.94 A; A/B/C/D=2-852.
DR PDB; 5MY2; X-ray; 2.70 A; A/B/C/D=2-852.
DR PDB; 6ROP; X-ray; 2.70 A; A/B/C/D=2-852.
DR PDBsum; 5MY0; -.
DR PDBsum; 5MY2; -.
DR PDBsum; 6ROP; -.
DR AlphaFoldDB; P19096; -.
DR SMR; P19096; -.
DR BioGRID; 199596; 29.
DR IntAct; P19096; 6.
DR MINT; P19096; -.
DR STRING; 10090.ENSMUSP00000052872; -.
DR BindingDB; P19096; -.
DR ChEMBL; CHEMBL1795189; -.
DR ESTHER; mouse-FASN; Thioesterase.
DR GlyGen; P19096; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P19096; -.
DR MetOSite; P19096; -.
DR PhosphoSitePlus; P19096; -.
DR SwissPalm; P19096; -.
DR CPTAC; non-CPTAC-3808; -.
DR jPOST; P19096; -.
DR PaxDb; 10090-ENSMUSP00000052872; -.
DR PeptideAtlas; P19096; -.
DR ProteomicsDB; 275589; -.
DR Pumba; P19096; -.
DR Antibodypedia; 1650; 755 antibodies from 40 providers.
DR DNASU; 14104; -.
DR Ensembl; ENSMUST00000055655.9; ENSMUSP00000052872.8; ENSMUSG00000025153.10.
DR GeneID; 14104; -.
DR KEGG; mmu:14104; -.
DR UCSC; uc007mut.1; mouse.
DR AGR; MGI:95485; -.
DR CTD; 2194; -.
DR MGI; MGI:95485; Fasn.
DR VEuPathDB; HostDB:ENSMUSG00000025153; -.
DR eggNOG; KOG1202; Eukaryota.
DR GeneTree; ENSGT00940000157276; -.
DR HOGENOM; CLU_000022_31_7_1; -.
DR InParanoid; P19096; -.
DR OMA; KMRGGEF; -.
DR OrthoDB; 3378513at2759; -.
DR PhylomeDB; P19096; -.
DR TreeFam; TF300549; -.
DR BRENDA; 2.3.1.85; 3474.
DR Reactome; R-MMU-199220; Vitamin B5 (pantothenate) metabolism.
DR Reactome; R-MMU-75105; Fatty acyl-CoA biosynthesis.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 14104; 23 hits in 80 CRISPR screens.
DR ChiTaRS; Fasn; mouse.
DR PRO; PR:P19096; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P19096; protein.
DR Bgee; ENSMUSG00000025153; Expressed in aorta tunica adventitia and 296 other cell types or tissues.
DR ExpressionAtlas; P19096; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042587; C:glycogen granule; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0019171; F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0141148; F:enoyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IDA:MGI.
DR GO; GO:0016297; F:fatty acyl-[ACP] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:MGI.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IMP:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:MGI.
DR GO; GO:0002068; P:glandular epithelial cell development; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0008610; P:lipid biosynthetic process; IDA:MGI.
DR GO; GO:0030879; P:mammary gland development; IMP:CACAO.
DR GO; GO:0044788; P:modulation by host of viral process; IEA:Ensembl.
DR GO; GO:0030224; P:monocyte differentiation; IMP:MGI.
DR GO; GO:0030223; P:neutrophil differentiation; IMP:MGI.
DR GO; GO:0009888; P:tissue development; IMP:MGI.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08954; KR_1_FAS_SDR_x; 2.
DR CDD; cd00833; PKS; 1.
DR FunFam; 1.10.1200.10:FF:000013; Fatty acid synthase; 1.
DR FunFam; 3.10.129.110:FF:000002; Fatty acid synthase; 1.
DR FunFam; 3.40.366.10:FF:000005; Fatty acid synthase; 1.
DR FunFam; 3.40.47.10:FF:000033; Fatty acid synthase; 1.
DR FunFam; 3.40.50.150:FF:000186; Fatty acid synthase; 1.
DR FunFam; 3.40.50.1820:FF:000059; Fatty acid synthase; 1.
DR FunFam; 3.40.50.1820:FF:000105; Fatty acid synthase; 1.
DR FunFam; 3.40.50.720:FF:000249; Fatty acid synthase; 1.
DR FunFam; 3.90.180.10:FF:000015; Fatty acid synthase; 1.
DR FunFam; 3.40.50.720:FF:000209; Polyketide synthase Pks12; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029058; AB_hydrolase_fold.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase_dom.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR049391; FAS_pseudo-KR.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR049900; PKS_mFAS_DH.
DR InterPro; IPR050091; PKS_NRPS_Biosynth_Enz.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF7; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF21149; FAS_pseudo-KR; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS52019; PKS_MFAS_DH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase; Isopeptide bond;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Multifunctional enzyme; NAD;
KW NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; S-nitrosylation; Transferase;
KW Ubl conjugation.
FT CHAIN 1..2504
FT /note="Fatty acid synthase"
FT /id="PRO_0000180277"
FT DOMAIN 1..406
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT DOMAIN 844..1104
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2112..2192
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 429..817
FT /note="Acyl and malonyl transferases"
FT REGION 844..967
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 982..1104
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1628..1856
FT /note="Enoyl reductase"
FT REGION 1857..2111
FT /note="Beta-ketoacyl reductase"
FT REGION 2181..2205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2201..2504
FT /note="Thioesterase"
FT ACT_SITE 161
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 293
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 331
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 581
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 878
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1032
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 2301
FT /note="For thioesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2474
FT /note="For thioesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT BINDING 647..648
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:31811668,
FT ECO:0007744|PDB:6ROP"
FT BINDING 671
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:31811668,
FT ECO:0007744|PDB:6ROP"
FT BINDING 773
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:31811668,
FT ECO:0007744|PDB:6ROP"
FT BINDING 1664..1681
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /ligand_note="for enoyl reductase activity"
FT /evidence="ECO:0000250"
FT BINDING 1879..1894
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /ligand_note="for ketoreductase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 298
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 528
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 673
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 790
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 993
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1071
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1276
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1464
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 1577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1697
FT /note="N6-(pyridoxal phosphate)lysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 1697
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 1764
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 1840
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1988
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 2084
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 2150
FT /note="O-(pantetheine 4'-phosphoryl)serine; alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2150
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P12785"
FT MOD_RES 2190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 2384
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 2442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT CONFLICT 1992
FT /note="T -> N (in Ref. 6; CAA31525)"
FT /evidence="ECO:0000305"
FT CONFLICT 2028
FT /note="G -> C (in Ref. 6; CAA31525)"
FT /evidence="ECO:0000305"
FT CONFLICT 2045
FT /note="G -> V (in Ref. 6; CAA31525)"
FT /evidence="ECO:0000305"
FT CONFLICT 2117
FT /note="T -> N (in Ref. 6; CAA31525)"
FT /evidence="ECO:0000305"
FT CONFLICT 2175
FT /note="Q -> R (in Ref. 6; CAA31525)"
FT /evidence="ECO:0000305"
FT CONFLICT 2295
FT /note="Y -> H (in Ref. 6; CAA31525)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 77..92
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:5MY2"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 336..349
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 397..406
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 431..443
FT /evidence="ECO:0007829|PDB:5MY2"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 448..456
FT /evidence="ECO:0007829|PDB:5MY2"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 467..477
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:5MY2"
FT TURN 504..507
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 509..512
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 514..527
FT /evidence="ECO:0007829|PDB:5MY2"
FT TURN 528..531
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 534..539
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 549..569
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 575..579
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 583..590
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 596..611
FT /evidence="ECO:0007829|PDB:5MY2"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:5MY0"
FT STRAND 618..625
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 627..633
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 639..643
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 645..654
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 660..666
FT /evidence="ECO:0007829|PDB:5MY2"
FT TURN 667..669
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:5MY2"
FT TURN 688..690
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 691..701
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 715..717
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 719..721
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 725..728
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 732..740
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 745..749
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 757..764
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 768..774
FT /evidence="ECO:0007829|PDB:5MY2"
FT STRAND 779..782
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 792..804
FT /evidence="ECO:0007829|PDB:5MY2"
FT TURN 805..807
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 812..815
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 831..833
FT /evidence="ECO:0007829|PDB:5MY2"
FT HELIX 847..849
FT /evidence="ECO:0007829|PDB:5MY2"
SQ SEQUENCE 2504 AA; 272428 MW; 2B48068B9D370C6F CRC64;
MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR SGKLKDLSKF
DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL RGTNTGVWVG VSGSEASEAL
SRDPETLLGY SMVGCQRAMM ANRLSFFFDF KGPSIALDTA CSSSLLALQN AYQAIRSGEC
PAALVGGINL LLKPNTSVQF MKLGMLSPDG TCRSFDDSGS GYCRSEAVVA VLLTKKSLAR
RVYATILNAG TNTDGSKEQG VTFPSGEVQE QLICSLYQPA GLAPESLEYI EAHGTGTKVG
DPQELNGITR SLCAFRQAPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEH GVWAPNLHFH
NPNPEIPALL DGRLQVVDRP LPVRGGNVGI NSFGFGGSNV HVILQPNTRQ APAPTAHAAL
PHLLHASGRT LEAVQDLLEQ GRQHSQDLAF VSMLNDIAAT PTAAMPFRGY TVLGVEGRVQ
EVQQVSTNKR PLWFICSGMG TQWRGMGLSL MRLDSFRESI LRSDEAVKPL GVKVSDLLLS
TDERTFDDIV HAFVSLTAIQ IALIDLLTSV GLKPDGIIGH SLGEVACGYA DGCLSQREAV
LAAYWRGQCI KDAHLPPGSM AAVGLSWEEC KQRCPAGVVP ACHNSEDTVT ISGPQAAVNE
FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK VIREPRPRSA RWLSTSIPEA
QWQSSLARTS SAEYNVNNLV SPVLFQEALW HIPEHAVVLE IAPHALLQAV LKRGVKSSCT
IIPLMKRDHK DNLEFFLTNL GKVHLTGINV NPNALFPPVE FPAPRGTPLI SPHIKWDHSQ
TWDVPVAEDF PNGSSSSSAT VYSIDASPES PDHYLVDHCI DGRVIFPGTG YLCLVWKTLA
RSLGLSLEET PVVFENVSFH QATILPKTGT VALEVRLLEA SHAFEVSDTG NLIVSGKVYL
WEDPNSKLFD HPEVPTPPES ASVSRLTQGE VYKELRLRGY DYGPQFQGIC EATLEGEQGK
LLWKDNWVTF MDTMLQVSIL GSSQQSLQLP TRVTAIYIDP ATHRQKVYRL KEDTQVADVT
TSRCLGITVS GGIHISRLQT TATSRRQQEQ LVPTLEKFVF TPHMEAECLS ESTALQKELQ
LCKGLARALQ TKATQQGLKA AMLGQEDPPQ HGLPRLLAAA CQLQLNGNLQ LELGEALAQE
RLLLPEDPLI SGLLNSQALK ACVDTALENL STLKMKVAEV LAGEGHLYSR IPALLNTQPM
LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWNPSDPAPS SLGALDLLVC NCALATLGDP
ALALDNMVAA LKEGGFLLVH TVLKGHALGE TLACLPSEVQ PAPSLLSQEE WESLFSRKAL
HLVGLKRSFY GTALFLCRRA IPQEKPIFLS VEDTSFQWVD SLKSTLATSS SQPVWLTAMD
CPTSGVVGLV NCLRKEPGGH RIRCILLSNL SNTSHAPKLD PGSPELQQVL KHDLVMNVYR
DGAWGAFRHF QLEQDKPKEQ TAHAFVNVLT RGDLASIRWV SSPLKHTQPS SSGAQLCTVY
YASLNFRDIM LATGKLSPDA IPGKWASRDC MLGMEFSGRD RCGRRVMGLV PAEGLATSVL
LSSDFLWDVP SSWTLEEAAS VPVVYTTAYY SLVVRGRIQR GETVLIHSGS GGVGQAAISI
ALSLGCRVFT TVGSAEKRAY LQARFPQLDD TSFANSRDTS FEQHVLLHTG GKGVDLVLNS
LAEEKLQASV RCLAQHGRFL EIGKFDLSNN HPLGMAIFLK NVTFHGILLD ALFEEANDSW
REVAALLKAG IRDGVVKPLK CTVFPKAQVE DAFRYMAQGK HIGKVLVQVR EEEPEAVLPG
AQPTLISAIS KTFCPAHKSY IITGGLGGFG LELARWLVLR GAQRLVLTSR SGIRTGYQAK
HIREWRRQGI QVLVSTSNVS SLEGARALIA EATKLGPVGG VFNLAMVLRD AMLENQTPEL
FQDVNKPKYN GTLNLDRATR EACPELDYFV AFSSVSCGRG NAGQTNYGFA NSTMERICEQ
RRHDGLPGLA VQWGAIGDVG IVLEAMGTND TVIGGTLPQR ISSCMEVLDL FLNQPHAVLS
SFVLAEKKAV AHGDGDTQRD LVKAVAHILG IRDLAGINLD STLADLGLDS LMGVEVRQIL
EREHDLVLPM REVRQLTLRK LQEMSSKTDS ATDTTAPKSR SDTSLKQNQL NLSTLLVNPE
GPTLTQLNSV QSSERPLFLV HPIEGSTTVF HSLAAKLSVP TYGLQCTQAA PLDSIPNLAA
YYIDCIKQVQ PEGPYRIAGY SFGACVAFEM CSQLQAQQGP APTHNNLFLF DGSHTYVLAY
TQSYRAKMTP GCEAEAEAEA LCFFIKQFLD VEHSKVLEAL LPLKSLEDRV AASVDLITKS
HHSLDRRELS FAAVSFYHKL RAADQYKPKA KYHGNVTLLR AKTGGTYGED LGADYNLSQV
CDGKVSVHII EGDHRTLLEG SGLESIINII HSSLAEPRVS VREG
//
