ID FAS2_YEAST Reviewed; 1887 AA. AC P19097; D6W3D9; Q12533; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2002, sequence version 2. DT 27-MAR-2024, entry version 232. DE RecName: Full=Fatty acid synthase subunit alpha; DE EC=2.3.1.86; DE Includes: DE RecName: Full=Acyl carrier; DE Includes: DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase; DE EC=1.1.1.100; DE AltName: Full=Beta-ketoacyl reductase; DE Includes: DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase; DE EC=2.3.1.41; DE AltName: Full=Beta-ketoacyl synthase; GN Name=FAS2; OrderedLocusNames=YPL231W; ORFNames=P1409; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2900835; DOI=10.1016/s0021-9258(18)37757-3; RA Mohamed A.H., Chirala S.S., Mody N.H., Huang W.Y., Wakil S.J.; RT "Primary structure of the multifunctional alpha subunit protein of yeast RT fatty acid synthase derived from FAS2 gene sequence."; RL J. Biol. Chem. 263:12315-12325(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 26786 / X2180-1A; RA Schueller H.-J.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., RA Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP MUTAGENESIS OF GLY-1250. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8041367; DOI=10.1007/bf00280191; RA Inokoshi J., Tomoda H., Hashimoto H., Watanabe A., Takeshima H., Omura S.; RT "Cerulenin-resistant mutants of Saccharomyces cerevisiae with an altered RT fatty acid synthase gene."; RL Mol. Gen. Genet. 244:90-96(1994). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=YAL6B; RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., RA Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling RT pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-958 AND SER-1440, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 76625 / YPH499; RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200; RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; RT "Profiling phosphoproteins of yeast mitochondria reveals a role of RT phosphorylation in assembly of the ATP synthase."; RL Mol. Cell. Proteomics 6:1896-1906(2007). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [12] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-37, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). RN [13] RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 671-1744 IN COMPLEX WITH FAS1, AND RP SUBUNIT. RX PubMed=17448991; DOI=10.1016/j.cell.2007.03.013; RA Lomakin I.B., Xiong Y., Steitz T.A.; RT "The crystal structure of yeast fatty acid synthase, a cellular machine RT with eight active sites working together."; RL Cell 129:319-332(2007). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAS1, SUBUNIT, AND RP PHOSPHOPANTETHEINYLATION AT SER-180. RX PubMed=17431182; DOI=10.1126/science.1138249; RA Leibundgut M., Jenni S., Frick C., Ban N.; RT "Structural basis for substrate delivery by acyl carrier protein in the RT yeast fatty acid synthase."; RL Science 316:288-290(2007). RN [15] RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH FAS1 AND THE RP INHIBITOR CERULENIN, AND ACTIVITY REGULATION. RX PubMed=18725634; DOI=10.1073/pnas.0805827105; RA Johansson P., Wiltschi B., Kumari P., Kessler B., Vonrhein C., Vonck J., RA Oesterhelt D., Grininger M.; RT "Inhibition of the fungal fatty acid synthase type I multienzyme complex."; RL Proc. Natl. Acad. Sci. U.S.A. 105:12803-12808(2008). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1766-1887 IN COMPLEX WITH FAS1 AND RP ACETYL-COA, MUTAGENESIS OF VAL-1769; GLY-1770; VAL-1771; ASP-1772; RP VAL-1773; GLU-1774; ARG-1841; VAL-1879 AND VAL-1881, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=19679086; DOI=10.1016/j.str.2009.06.014; RA Johansson P., Mulinacci B., Koestler C., Vollrath R., Oesterhelt D., RA Grininger M.; RT "Multimeric options for the auto-activation of the Saccharomyces cerevisiae RT FAS type I megasynthase."; RL Structure 17:1063-1074(2009). CC -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain CC fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit CC contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier- CC protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This CC subunit coordinates the binding of the six beta subunits to the enzyme CC complex. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:83139; EC=2.3.1.86; CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] CC + CO2 + holo-[ACP]; 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; CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) CC + NADPH; 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 -!- ACTIVITY REGULATION: Inhibited by cerulenin by covalent binding to CC active site of the ketoacyl synthase (KS) region. CC {ECO:0000269|PubMed:18725634}. CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits CC (alpha and beta). {ECO:0000269|PubMed:17431182, CC ECO:0000269|PubMed:17448991, ECO:0000269|PubMed:18725634, CC ECO:0000269|PubMed:19679086}. CC -!- INTERACTION: CC P19097; P07149: FAS1; NbExp=9; IntAct=EBI-6806, EBI-6795; CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine CC of the Acyl carrier domain by the C-terminal PPT domain. This CC modification is essential for activity because fatty acids are bound in CC thioester linkage to the sulfhydryl of the prosthetic group. CC -!- MISCELLANEOUS: Present with 17000 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid CC synthetase subunit alpha family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J03936; AAA34601.1; -; Genomic_DNA. DR EMBL; X76890; CAA54218.1; -; Genomic_DNA. DR EMBL; X94561; CAA64256.1; -; Genomic_DNA. DR EMBL; Z73586; CAA97947.1; -; Genomic_DNA. DR EMBL; Z73587; CAA97948.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11205.1; -; Genomic_DNA. DR PIR; S61703; S61703. DR RefSeq; NP_015093.1; NM_001184045.1. DR PDB; 2ML8; NMR; -; A=138-302. DR PDB; 2PFF; X-ray; 4.00 A; A/D/G=671-1744. DR PDB; 2UV8; X-ray; 3.10 A; A/B/C=1-1887. DR PDB; 2VKZ; X-ray; 4.00 A; A/B/C=1-1887. DR PDB; 2WAS; X-ray; 1.90 A; A/B/C/D/E/F=1766-1887. DR PDB; 2WAT; X-ray; 2.20 A; A/B/C/D/E/F=1766-1887. DR PDB; 3HMJ; X-ray; 4.00 A; A/B/C=1-1887. DR PDB; 6JSH; EM; 5.10 A; C/H/I=1443-1513. DR PDB; 6JSI; EM; 4.70 A; C/H/I=1443-1513. DR PDB; 6QL5; EM; 2.80 A; A/B/C/D/E/F=1-1887. DR PDB; 6QL6; EM; 2.90 A; A/B/C/D/E/F=1-1887. DR PDB; 6QL7; X-ray; 4.60 A; A/B/C/D/E/F/a/b/c/d/e/f=1-1887. DR PDB; 6QL9; X-ray; 2.82 A; A/B/C/D/E/F=1-1887. DR PDB; 6TA1; EM; 3.10 A; A/B/D/F/I/K=1-1887. DR PDB; 6WC7; EM; 5.80 A; A=1-1887. DR PDB; 8PRV; EM; 2.90 A; A/B=1-1887. DR PDB; 8PRW; EM; 1.90 A; A/B/C/D/E/F=1-1887. DR PDB; 8PS1; EM; 2.80 A; A/B=1-1887. DR PDB; 8PS2; EM; 2.90 A; A/B=1-1887. DR PDB; 8PS8; EM; 4.00 A; A/B=1-1887. DR PDB; 8PS9; EM; 2.90 A; A/B=1-1887. DR PDB; 8PSA; EM; 3.60 A; A/B=1-1887. DR PDB; 8PSF; EM; 2.80 A; A/B=1-1887. DR PDB; 8PSG; EM; 3.70 A; A/B=1-1887. DR PDB; 8PSJ; EM; 3.40 A; A/B=1-1887. DR PDB; 8PSK; EM; 2.80 A; A/B=1-1887. DR PDB; 8PSL; EM; 3.70 A; A/B=1-1887. DR PDB; 8PSM; EM; 3.10 A; A/B=1-1887. DR PDB; 8PSP; EM; 2.90 A; A/B=1-1887. DR PDBsum; 2ML8; -. DR PDBsum; 2PFF; -. DR PDBsum; 2UV8; -. DR PDBsum; 2VKZ; -. DR PDBsum; 2WAS; -. DR PDBsum; 2WAT; -. DR PDBsum; 3HMJ; -. DR PDBsum; 6JSH; -. DR PDBsum; 6JSI; -. DR PDBsum; 6QL5; -. DR PDBsum; 6QL6; -. DR PDBsum; 6QL7; -. DR PDBsum; 6QL9; -. DR PDBsum; 6TA1; -. DR PDBsum; 6WC7; -. DR PDBsum; 8PRV; -. DR PDBsum; 8PRW; -. DR PDBsum; 8PS1; -. DR PDBsum; 8PS2; -. DR PDBsum; 8PS8; -. DR PDBsum; 8PS9; -. DR PDBsum; 8PSA; -. DR PDBsum; 8PSF; -. DR PDBsum; 8PSG; -. DR PDBsum; 8PSJ; -. DR PDBsum; 8PSK; -. DR PDBsum; 8PSL; -. DR PDBsum; 8PSM; -. DR PDBsum; 8PSP; -. DR AlphaFoldDB; P19097; -. DR BMRB; P19097; -. DR EMDB; EMD-10420; -. DR EMDB; EMD-17839; -. DR EMDB; EMD-17840; -. DR EMDB; EMD-17842; -. DR EMDB; EMD-17843; -. DR EMDB; EMD-17846; -. DR EMDB; EMD-17847; -. DR EMDB; EMD-17848; -. DR EMDB; EMD-17851; -. DR EMDB; EMD-17852; -. DR EMDB; EMD-17853; -. DR EMDB; EMD-17854; -. DR EMDB; EMD-17855; -. DR EMDB; EMD-17856; -. DR EMDB; EMD-17859; -. DR EMDB; EMD-21602; -. DR EMDB; EMD-4577; -. DR EMDB; EMD-4578; -. DR EMDB; EMD-9881; -. DR EMDB; EMD-9882; -. DR SMR; P19097; -. DR BioGRID; 35931; 423. DR ComplexPortal; CPX-1162; Fatty-acyl-CoA synthase. DR DIP; DIP-960N; -. DR IntAct; P19097; 20. DR MINT; P19097; -. DR STRING; 4932.YPL231W; -. DR iPTMnet; P19097; -. DR MaxQB; P19097; -. DR PaxDb; 4932-YPL231W; -. DR PeptideAtlas; P19097; -. DR TopDownProteomics; P19097; -. DR EnsemblFungi; YPL231W_mRNA; YPL231W; YPL231W. DR GeneID; 855845; -. DR KEGG; sce:YPL231W; -. DR AGR; SGD:S000006152; -. DR SGD; S000006152; FAS2. DR VEuPathDB; FungiDB:YPL231W; -. DR eggNOG; ENOG502QQJX; Eukaryota. DR GeneTree; ENSGT00940000176444; -. DR HOGENOM; CLU_000114_0_0_1; -. DR InParanoid; P19097; -. DR OMA; FPTLPDW; -. DR OrthoDB; 2783039at2759; -. DR BioCyc; MetaCyc:YPL231W-MONOMER; -. DR BioCyc; YEAST:YPL231W-MONOMER; -. DR BRENDA; 2.3.1.86; 984. DR SABIO-RK; P19097; -. DR BioGRID-ORCS; 855845; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P19097; -. DR PRO; PR:P19097; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; P19097; Protein. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005835; C:fatty acid synthase complex; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IDA:SGD. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IMP:SGD. DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro. DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IMP:SGD. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:SGD. DR CDD; cd00828; elong_cond_enzymes; 1. DR CDD; cd08950; KR_fFAS_SDR_c_like; 1. DR Gene3D; 3.30.70.2490; -; 1. DR Gene3D; 3.40.47.10; -; 1. DR Gene3D; 3.90.25.70; -; 1. DR Gene3D; 6.10.140.1410; -; 1. DR Gene3D; 6.10.250.1930; -; 1. DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00101; AcpS; 1. DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom. DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf. DR InterPro; IPR002582; ACPS. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR040899; Fas_alpha_ACP. DR InterPro; IPR047224; FAS_alpha_su_C. DR InterPro; IPR026025; FAS_alpha_yeast. DR InterPro; IPR041550; FASI_helical. DR InterPro; IPR018201; Ketoacyl_synth_AS. DR InterPro; IPR014031; Ketoacyl_synth_C. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR009081; PP-bd_ACP. DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom. DR InterPro; IPR016039; Thiolase-like. DR NCBIfam; TIGR00556; pantethn_trn; 1. DR PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1. DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1. DR Pfam; PF01648; ACPS; 1. DR Pfam; PF18325; Fas_alpha_ACP; 1. DR Pfam; PF18314; FAS_I_H; 1. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR PIRSF; PIRSF000454; FAS_yeast_alpha; 1. DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1. DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF53901; Thiolase-like; 2. DR PROSITE; PS50075; CARRIER; 1. DR PROSITE; PS00606; KS3_1; 1. DR PROSITE; PS52004; KS3_2; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 1: Evidence at protein level; KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism; KW Isopeptide bond; Lipid biosynthesis; Lipid metabolism; Magnesium; KW Metal-binding; Multifunctional enzyme; NAD; NADP; Oxidoreductase; KW Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase; KW Ubl conjugation. FT CHAIN 1..1887 FT /note="Fatty acid synthase subunit alpha" FT /id="PRO_0000180287" FT DOMAIN 145..220 FT /note="Carrier" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258" FT DOMAIN 1123..1657 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT REGION 96..120 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 675..874 FT /note="Beta-ketoacyl reductase" FT ACT_SITE 1305 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 1542 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 1583 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT BINDING 1772..1774 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT BINDING 1772 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 1773 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 1774 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 1798 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:19679086" FT BINDING 1808 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:19679086" FT BINDING 1817..1827 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT BINDING 1841..1844 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT BINDING 1871..1873 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT BINDING 1872 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 1873 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT MOD_RES 50 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15665377" FT MOD_RES 180 FT /note="O-(pantetheine 4'-phosphoryl)serine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258, FT ECO:0000269|PubMed:17431182" FT MOD_RES 523 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 958 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950" FT MOD_RES 1440 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950" FT CROSSLNK 37 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT MUTAGEN 1250 FT /note="G->S: Cerulenin-resistance." FT /evidence="ECO:0000269|PubMed:8041367" FT MUTAGEN 1769 FT /note="V->D: Does not affect oligomerization; when FT associated with S-1771 and L-1773 or S-1771; L-1773; S-1879 FT and E-1881." FT /evidence="ECO:0000269|PubMed:19679086" FT MUTAGEN 1770 FT /note="G->D: Loss of transferase activity." FT /evidence="ECO:0000269|PubMed:19679086" FT MUTAGEN 1771 FT /note="V->S: Does not affect oligomerization but lacks FT transferase activity; when associated with D-1769 and FT L-1773 or D-1769; L-1773; S-1879 and E-1881." FT /evidence="ECO:0000269|PubMed:19679086" FT MUTAGEN 1772 FT /note="D->S: Loss of transferase activity; when associated FT with S-1774." FT /evidence="ECO:0000269|PubMed:19679086" FT MUTAGEN 1773 FT /note="V->L: Does not affect oligomerization but lacks FT transferase activity; when associated with D-1769 and FT S-1771 or D-1769; S-1771; S-1879 and E-1881." FT /evidence="ECO:0000269|PubMed:19679086" FT MUTAGEN 1774 FT /note="E->S: Loss of transferase activity; when associated FT with S-1772." FT /evidence="ECO:0000269|PubMed:19679086" FT MUTAGEN 1841 FT /note="R->A: Loss off transferase activity." FT /evidence="ECO:0000269|PubMed:19679086" FT MUTAGEN 1879 FT /note="V->S: Does not affect oligomerization but lacks FT transferase activity; when associated with D-1769; S-1771; FT L-1773 and E-1881." FT /evidence="ECO:0000269|PubMed:19679086" FT MUTAGEN 1881 FT /note="V->E: Does not affect oligomerization but lacks FT transferase activity; when associated with D-1769; S-1771; FT L-1773 and S-1879." FT /evidence="ECO:0000269|PubMed:19679086" FT CONFLICT 310 FT /note="G -> GTTGTGG (in Ref. 1; AAA34601)" FT /evidence="ECO:0000305" FT CONFLICT 594 FT /note="T -> I (in Ref. 1; AAA34601)" FT /evidence="ECO:0000305" FT CONFLICT 941..1019 FT /note="AKLRKELVETSEVRKAVSIETALEHKVVNGNSADAAYAQVEIQPRANIQLDF FT PELKPYKQVKQIAPAELEGLLDLERVI -> CLNCVKSWLKLLKLERQFPSKLLWSIRL FT SMAIALMLHMLKSKFNQELTFNWTSQNRNHTNRLNKLLPLSLRVCWIWKELF (in FT Ref. 1; AAA34601)" FT /evidence="ECO:0000305" FT CONFLICT 1036..1041 FT /note="RWEMEA -> KMGNGS (in Ref. 1; AAA34601)" FT /evidence="ECO:0000305" FT CONFLICT 1408 FT /note="A -> S (in Ref. 1; AAA34601)" FT /evidence="ECO:0000305" FT CONFLICT 1671 FT /note="N -> T (in Ref. 1; AAA34601)" FT /evidence="ECO:0000305" FT HELIX 3..20 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 21..23 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 28..37 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 42..51 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 52..64 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 66..71 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 85..88 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 147..157 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 158..160 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 172..176 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 180..194 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 201..203 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 206..216 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 223..236 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 243..252 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 258..260 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 261..270 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:2ML8" FT HELIX 280..298 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 329..350 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 356..382 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 384..389 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 396..398 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 400..402 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 405..421 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 430..440 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 445..456 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 460..462 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 464..483 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 497..503 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 509..515 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 522..531 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 605..607 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 609..615 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 626..629 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 637..643 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 649..651 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 653..668 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 677..682 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 685..687 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 688..698 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 702..709 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 712..725 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 731..736 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 742..753 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 756..759 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 766..770 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 781..783 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 786..795 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 797..811 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 812..814 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 820..826 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 839..845 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 846..848 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 849..855 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 859..861 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 862..869 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 885..889 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 898..906 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 907..909 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 911..919 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 922..927 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 930..932 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 933..935 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 936..968 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 971..976 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 998..1004 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1007..1009 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 1010..1012 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1015..1017 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1019..1028 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1033..1042 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1047..1056 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1059..1067 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1070..1077 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 1078..1080 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1086..1088 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1089..1099 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1101..1105 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1108..1111 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1118..1126 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1134..1136 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1138..1148 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1149..1151 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1152..1156 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 1158..1160 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1163..1167 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1172..1179 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1185..1187 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 1195..1199 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1202..1207 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1210..1225 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1231..1233 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1234..1237 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1240..1242 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1243..1245 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1248..1251 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1254..1261 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 1262..1267 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1274..1278 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1282..1290 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1304..1306 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1307..1320 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1325..1333 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1337..1345 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1352..1357 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1362..1364 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1381..1389 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1390..1396 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1402..1410 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1424..1429 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1441..1443 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1445..1474 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1483..1508 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 1512..1515 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1517..1519 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1521..1527 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 1528..1530 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1533..1535 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1536..1540 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1547..1564 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1572..1575 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1578..1581 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1585..1587 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1588..1600 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1612..1614 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1616..1620 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1638..1645 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 1646..1648 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1649..1656 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1659..1662 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1667..1693 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1708..1710 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1711..1716 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1726..1728 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1730..1732 FT /evidence="ECO:0007829|PDB:2UV8" FT TURN 1735..1739 FT /evidence="ECO:0007829|PDB:2UV8" FT HELIX 1742..1745 FT /evidence="ECO:0007829|PDB:2UV8" FT STRAND 1769..1775 FT /evidence="ECO:0007829|PDB:2WAS" FT HELIX 1776..1778 FT /evidence="ECO:0007829|PDB:2WAS" FT HELIX 1784..1790 FT /evidence="ECO:0007829|PDB:2WAS" FT HELIX 1793..1800 FT /evidence="ECO:0007829|PDB:2WAS" FT STRAND 1802..1804 FT /evidence="ECO:0007829|PDB:2WAS" FT HELIX 1805..1823 FT /evidence="ECO:0007829|PDB:2WAS" FT STRAND 1837..1842 FT /evidence="ECO:0007829|PDB:2WAS" FT STRAND 1845..1851 FT /evidence="ECO:0007829|PDB:2WAS" FT HELIX 1853..1860 FT /evidence="ECO:0007829|PDB:2WAS" FT TURN 1861..1863 FT /evidence="ECO:0007829|PDB:2WAS" FT STRAND 1866..1873 FT /evidence="ECO:0007829|PDB:2WAS" FT STRAND 1875..1885 FT /evidence="ECO:0007829|PDB:2WAS" SQ SEQUENCE 1887 AA; 206947 MW; 08B872734CF3AEEA CRC64; MKPEVEQELA HILLTELLAY QFASPVRWIE TQDVFLKDFN TERVVEIGPS PTLAGMAQRT LKNKYESYDA ALSLHREILC YSKDAKEIYY TPDPSELAAK EEPAKEEAPA PTPAASAPAP AAAAPAPVAA AAPAAAAAEI ADEPVKASLL LHVLVAHKLK KSLDSIPMSK TIKDLVGGKS TVQNEILGDL GKEFGTTPEK PEETPLEELA ETFQDTFSGA LGKQSSSLLS RLISSKMPGG FTITVARKYL QTRWGLPSGR QDGVLLVALS NEPAARLGSE ADAKAFLDSM AQKYASIVGV DLSSAASASG AAGAGAAAGA AMIDAGALEE ITKDHKVLAR QQLQVLARYL KMDLDNGERK FLKEKDTVAE LQAQLDYLNA ELGEFFVNGV ATSFSRKKAR TFDSSWNWAK QSLLSLYFEI IHGVLKNVDR EVVSEAINIM NRSNDALIKF MEYHISNTDE TKGENYQLVK TLGEQLIENC KQVLDVDPVY KDVAKPTGPK TAIDKNGNIT YSEEPREKVR KLSQYVQEMA LGGPITKESQ PTIEEDLTRV YKAISAQADK QDISSSTRVE FEKLYSDLMK FLESSKEIDP SQTTQLAGMD VEDALDKDST KEVASLPNKS TISKTVSSTI PRETIPFLHL RKKTPAGDWK YDRQLSSLFL DGLEKAAFNG VTFKDKYVLI TGAGKGSIGA EVLQGLLQGG AKVVVTTSRF SKQVTDYYQS IYAKYGAKGS TLIVVPFNQG SKQDVEALIE FIYDTEKNGG LGWDLDAIIP FAAIPEQGIE LEHIDSKSEF AHRIMLTNIL RMMGCVKKQK SARGIETRPA QVILPMSPNH GTFGGDGMYS ESKLSLETLF NRWHSESWAN QLTVCGAIIG WTRGTGLMSA NNIIAEGIEK MGVRTFSQKE MAFNLLGLLT PEVVELCQKS PVMADLNGGL QFVPELKEFT AKLRKELVET SEVRKAVSIE TALEHKVVNG NSADAAYAQV EIQPRANIQL DFPELKPYKQ VKQIAPAELE GLLDLERVIV VTGFAEVGPW GSARTRWEME AFGEFSLEGC VEMAWIMGFI SYHNGNLKGR PYTGWVDSKT KEPVDDKDVK AKYETSILEH SGIRLIEPEL FNGYNPEKKE MIQEVIVEED LEPFEASKET AEQFKHQHGD KVDIFEIPET GEYSVKLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI SDDIISQVDP ITLFVLVSVV EAFIASGITD PYEMYKYVHV SEVGNCSGSG MGGVSALRGM FKDRFKDEPV QNDILQESFI NTMSAWVNML LISSSGPIKT PVGACATSVE SVDIGVETIL SGKARICIVG GYDDFQEEGS FEFGNMKATS NTLEEFEHGR TPAEMSRPAT TTRNGFMEAQ GAGIQIIMQA DLALKMGVPI YGIVAMAATA TDKIGRSVPA PGKGILTTAR EHHSSVKYAS PNLNMKYRKR QLVTREAQIK DWVENELEAL KLEAEEIPSE DQNEFLLERT REIHNEAESQ LRAAQQQWGN DFYKRDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND KNESATINEM MKHLGRSEGN PVIGVFQKFL TGHPKGAAGA WMMNGALQIL NSGIIPGNRN ADNVDKILEQ FEYVLYPSKT LKTDGVRAVS ITSFGFGQKG GQAIVVHPDY LYGAITEDRY NEYVAKVSAR EKSAYKFFHN GMIYNKLFVS KEHAPYTDEL EEDVYLDPLA RVSKDKKSGS LTFNSKNIQS KDSYINANTI ETAKMIENMT KEKVSNGGVG VDVELITSIN VENDTFIERN FTPQEIEYCS AQPSVQSSFA GTWSAKEAVF KSLGVKSLGG GAALKDIEIV RVNKNAPAVE LHGNAKKAAE EAGVTDVKVS ISHDDLQAVA VAVSTKK //