FAS1_YEAST
ID FAS1_YEAST Reviewed; 2051 AA.
AC P07149; D6VX19; Q05747;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Fatty acid synthase subunit beta;
DE EC=2.3.1.86;
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase;
DE EC=4.2.1.59;
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH];
DE EC=1.3.1.9;
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] acetyltransferase;
DE EC=2.3.1.38;
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] malonyltransferase;
DE EC=2.3.1.39;
DE Includes:
DE RecName: Full=S-acyl fatty acid synthase thioesterase;
DE EC=3.1.2.14;
GN Name=FAS1; OrderedLocusNames=YKL182W;
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=2034224; DOI=10.1007/bf00273618;
RA Koettig H., Rottner G., Beck K.-F., Schweizer M., Schweizer E.;
RT "The pentafunctional FAS1 genes of Saccharomyces cerevisiae and Yarrowia
RT lipolytica are co-linear and considerably longer than previously
RT estimated.";
RL Mol. Gen. Genet. 226:310-314(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2025.
RX PubMed=3528750; DOI=10.1007/bf00422073;
RA Schweizer M., Roberts L.M., Hoeltke H.-J., Takabayashi K., Hoellerer E.,
RA Hoffmann B., Mueller G., Koettig H., Schweizer E.;
RT "The pentafunctional FAS1 gene of yeast: its nucleotide sequence and order
RT of the catalytic domains.";
RL Mol. Gen. Genet. 203:479-486(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1980.
RC STRAIN=ATCC 26787 / X2180-1B;
RX PubMed=3031066; DOI=10.1016/s0021-9258(18)61337-7;
RA Chirala S.S., Kuziora M.A., Spector D.M., Wakil S.J.;
RT "Complementation of mutations and nucleotide sequence of FAS1 gene encoding
RT beta subunit of yeast fatty acid synthase.";
RL J. Biol. Chem. 262:4231-4240(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1947-2051.
RC STRAIN=ATCC 26786 / X2180-1A;
RX PubMed=7992503; DOI=10.1002/yea.320100805;
RA Carter A.T., Narbad A., Pearson B.M., Beck K.-F., Logghe M., Contreras R.,
RA Schweizer M.;
RT "Phosphoribosylpyrophosphate synthetase (PRS): a new gene family in
RT Saccharomyces cerevisiae.";
RL Yeast 10:1031-1044(1994).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1121, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-733 AND SER-1121, AND
RP IDENTIFICATION BY 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1364, AND IDENTIFICATION BY
RP MASS 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).
CC -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain
CC fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit
CC contains domains for: [acyl-carrier-protein] acetyltransferase and
CC malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-
CC [acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-
CC protein] dehydratase.
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=acetyl-CoA + holo-[ACP] = 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 -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
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 -!- 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) +
CC holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta).
CC -!- INTERACTION:
CC P07149; P19097: FAS2; NbExp=9; IntAct=EBI-6795, EBI-6806;
CC -!- MISCELLANEOUS: Present with 91800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27616.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M30162; AAB59310.1; -; Genomic_DNA.
DR EMBL; X74151; CAA52256.1; -; Genomic_DNA.
DR EMBL; Z28182; CAA82025.1; -; Genomic_DNA.
DR EMBL; X03977; CAA27616.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M31034; AAA34602.1; -; Genomic_DNA.
DR EMBL; X70069; CAA49673.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08985.1; -; Genomic_DNA.
DR PIR; S34688; S34688.
DR RefSeq; NP_012739.1; NM_001179748.1.
DR PDB; 2PFF; X-ray; 4.00 A; B/E/H=1-545, B/E/H=1669-1940.
DR PDB; 2UV8; X-ray; 3.10 A; G/H/I=1-2051.
DR PDB; 2VKZ; X-ray; 4.00 A; G/H/I=1-2051.
DR PDB; 3HMJ; X-ray; 4.00 A; G/H/I=1-2051.
DR PDB; 6JSH; EM; 5.10 A; B/F/G=1-2051.
DR PDB; 6JSI; EM; 4.70 A; B/F/G=1-2051.
DR PDB; 6QL5; EM; 2.80 A; G/H/I/J/K/L=5-2050.
DR PDB; 6QL6; EM; 2.90 A; G/H/I/J/K/L=5-2050.
DR PDB; 6QL7; X-ray; 4.60 A; G/H/I/J/K/L/g/h/i/j/k/l=1-2051.
DR PDB; 6QL9; X-ray; 2.82 A; G/H/I/J/K/L=1-2051.
DR PDB; 6TA1; EM; 3.10 A; C/E/G/H/J/L=1-2051.
DR PDB; 6U5T; EM; 2.90 A; G=1-2051.
DR PDB; 6U5U; EM; 2.80 A; G=1-2051.
DR PDB; 6WC7; EM; 5.80 A; G=1-2051.
DR PDBsum; 2PFF; -.
DR PDBsum; 2UV8; -.
DR PDBsum; 2VKZ; -.
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; 6U5T; -.
DR PDBsum; 6U5U; -.
DR PDBsum; 6WC7; -.
DR AlphaFoldDB; P07149; -.
DR SMR; P07149; -.
DR BioGRID; 33940; 126.
DR ComplexPortal; CPX-1162; Fatty-acyl-CoA synthase.
DR DIP; DIP-742N; -.
DR IntAct; P07149; 101.
DR MINT; P07149; -.
DR STRING; 4932.YKL182W; -.
DR CarbonylDB; P07149; -.
DR iPTMnet; P07149; -.
DR MaxQB; P07149; -.
DR PaxDb; P07149; -.
DR PRIDE; P07149; -.
DR EnsemblFungi; YKL182W_mRNA; YKL182W; YKL182W.
DR GeneID; 853653; -.
DR KEGG; sce:YKL182W; -.
DR SGD; S000001665; FAS1.
DR VEuPathDB; FungiDB:YKL182W; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR GeneTree; ENSGT00940000176444; -.
DR HOGENOM; CLU_000114_5_0_1; -.
DR InParanoid; P07149; -.
DR OMA; LTHRNKD; -.
DR BioCyc; MetaCyc:YKL182W-MON; -.
DR BioCyc; YEAST:YKL182W-MON; -.
DR BRENDA; 2.3.1.86; 984.
DR SABIO-RK; P07149; -.
DR EvolutionaryTrace; P07149; -.
DR PRO; PR:P07149; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P07149; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005835; C:fatty acid synthase complex; IDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0019171; F:3-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IDA:SGD.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IDA:SGD.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IDA:SGD.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004319; F:enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity; IDA:SGD.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:SGD.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IDA:ComplexPortal.
DR Gene3D; 3.20.20.70; -; 2.
DR Gene3D; 3.40.366.10; -; 3.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR016452; Fas1/AflB-like.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR041099; FAS1_N.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR039569; MaoC-like_dehydrat_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR032088; SAT.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; DUF1729; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF17828; FAS_N; 1.
DR Pfam; PF13452; MaoC_dehydrat_N; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PIRSF; PIRSF005562; FAS_yeast_beta; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; SSF52151; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Fatty acid biosynthesis; Fatty acid metabolism;
KW Hydrolase; Isopeptide bond; Lipid biosynthesis; Lipid metabolism; Lyase;
KW Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..2051
FT /note="Fatty acid synthase subunit beta"
FT /id="PRO_0000180282"
FT DOMAIN 1523..1648
FT /note="MaoC-like"
FT REGION 1..468
FT /note="Acetyltransferase"
FT REGION 480..868
FT /note="Enoyl reductase"
FT REGION 1144..1626
FT /note="Dehydratase"
FT REGION 1627..1845
FT /note="Malonyl/palmitoyl transferase"
FT ACT_SITE 274
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 1808
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 733
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 1364
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 191
FT /note="S -> F (in Ref. 1; AAB59310 and 5; CAA27616)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="G -> D (in Ref. 6; AAA34602)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="D -> G (in Ref. 6; AAA34602)"
FT /evidence="ECO:0000305"
FT CONFLICT 1039
FT /note="H -> Q (in Ref. 1; AAB59310 and 5; CAA27616)"
FT /evidence="ECO:0000305"
FT CONFLICT 1149
FT /note="W -> R (in Ref. 6; AAA34602)"
FT /evidence="ECO:0000305"
FT CONFLICT 1184
FT /note="I -> F (in Ref. 1; AAB59310 and 5; CAA27616)"
FT /evidence="ECO:0000305"
FT CONFLICT 1290..1292
FT /note="FEI -> SET (in Ref. 6; AAA34602)"
FT /evidence="ECO:0000305"
FT CONFLICT 1331..1333
FT /note="WRA -> LRG (in Ref. 1; AAB59310 and 5; CAA27616)"
FT /evidence="ECO:0000305"
FT CONFLICT 1407..1411
FT /note="TSSFF -> IFLFL (in Ref. 6; AAA34602)"
FT /evidence="ECO:0000305"
FT CONFLICT 1559
FT /note="D -> H (in Ref. 1; AAB59310 and 5; CAA27616)"
FT /evidence="ECO:0000305"
FT CONFLICT 1576
FT /note="P -> L (in Ref. 6; AAA34602)"
FT /evidence="ECO:0000305"
FT CONFLICT 1587
FT /note="A -> T (in Ref. 6; AAA34602)"
FT /evidence="ECO:0000305"
FT CONFLICT 1631
FT /note="M -> T (in Ref. 6; AAA34602)"
FT /evidence="ECO:0000305"
FT CONFLICT 1647
FT /note="D -> H (in Ref. 5; CAA27616)"
FT /evidence="ECO:0000305"
FT CONFLICT 1661
FT /note="V -> G (in Ref. 1; AAB59310 and 5; CAA27616)"
FT /evidence="ECO:0000305"
FT CONFLICT 1876
FT /note="E -> K (in Ref. 6; AAA34602)"
FT /evidence="ECO:0000305"
FT CONFLICT 1980
FT /note="Y -> T (in Ref. 6; AAA34602)"
FT /evidence="ECO:0000305"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 24..40
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 116..132
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 181..201
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 234..255
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 292..311
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 325..331
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 346..357
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 373..381
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 383..394
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:6U5T"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 436..445
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:6U5T"
FT HELIX 475..484
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 499..503
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 512..519
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 521..524
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 526..531
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 544..548
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 561..564
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 584..587
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 591..594
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 598..602
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 606..612
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 616..620
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 628..638
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 647..654
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 656..671
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 678..684
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 690..693
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 694..697
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 701..706
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 711..722
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 728..732
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 737..740
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 747..758
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 763..767
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 774..782
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 784..786
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 787..790
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:6U5T"
FT TURN 803..807
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 808..811
FT /evidence="ECO:0007829|PDB:6U5T"
FT HELIX 815..823
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 829..831
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 833..835
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 840..842
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 844..847
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 853..856
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 860..871
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 877..879
FT /evidence="ECO:0007829|PDB:2UV8"
FT HELIX 880..886
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 888..897
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 903..907
FT /evidence="ECO:0007829|PDB:6U5T"
FT HELIX 914..916
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 919..930
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 933..936
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 937..939
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 941..958
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 970..974
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 976..984
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 988..991
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 998..1005
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 1006..1008
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1010..1012
FT /evidence="ECO:0007829|PDB:2UV8"
FT STRAND 1016..1018
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1025..1030
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1035..1042
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1043..1046
FT /evidence="ECO:0007829|PDB:6U5T"
FT HELIX 1048..1050
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1059..1062
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1070..1089
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1094..1096
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1099..1102
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1126..1128
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1135..1143
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1149..1155
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1158..1163
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1165..1167
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1169..1173
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1181..1186
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1188..1190
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1194..1198
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1209..1212
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1215..1217
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1218..1225
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1229..1232
FT /evidence="ECO:0007829|PDB:6U5T"
FT STRAND 1234..1242
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1251..1253
FT /evidence="ECO:0007829|PDB:6U5T"
FT HELIX 1258..1270
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1281..1286
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1294..1303
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1325..1334
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1335..1337
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1339..1343
FT /evidence="ECO:0007829|PDB:6U5T"
FT HELIX 1347..1349
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1354..1359
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1367..1369
FT /evidence="ECO:0007829|PDB:6U5T"
FT STRAND 1371..1382
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1387..1398
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1401..1414
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1419..1421
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1423..1427
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1431..1434
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1437..1439
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1440..1445
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1447..1453
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1463..1466
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1469..1478
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1480..1492
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1498..1510
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1515..1521
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1524..1526
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1531..1545
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1551..1556
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 1562..1564
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 1568..1574
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1576..1578
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1582..1594
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 1595..1597
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1602..1604
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1605..1612
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1621..1632
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1635..1643
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1649..1657
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1662..1666
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 1674..1679
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1680..1682
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1685..1701
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1707..1711
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1715..1720
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1724..1734
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1749..1751
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1761..1765
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1770..1772
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1774..1794
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1803..1809
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1810..1818
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1824..1840
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1846..1848
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1850..1857
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1859..1862
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1868..1882
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1886..1893
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 1894..1896
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1897..1903
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1904..1920
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1924..1930
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1935..1951
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 1964..1968
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1979..1985
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 1986..1995
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 1998..2000
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 2003..2005
FT /evidence="ECO:0007829|PDB:6U5U"
FT TURN 2006..2009
FT /evidence="ECO:0007829|PDB:6U5U"
FT STRAND 2013..2015
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 2023..2033
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 2036..2042
FT /evidence="ECO:0007829|PDB:6U5U"
FT HELIX 2043..2048
FT /evidence="ECO:0007829|PDB:6U5U"
SQ SEQUENCE 2051 AA; 228691 MW; 43AA85A6071D8EAA CRC64;
MDAYSTRPLT LSHGSLEHVL LVPTASFFIA SQLQEQFNKI LPEPTEGFAA DDEPTTPAEL
VGKFLGYVSS LVEPSKVGQF DQVLNLCLTE FENCYLEGND IHALAAKLLQ ENDTTLVKTK
ELIKNYITAR IMAKRPFDKK SNSALFRAVG EGNAQLVAIF GGQGNTDDYF EELRDLYQTY
HVLVGDLIKF SAETLSELIR TTLDAEKVFT QGLNILEWLE NPSNTPDKDY LLSIPISCPL
IGVIQLAHYV VTAKLLGFTP GELRSYLKGA TGHSQGLVTA VAIAETDSWE SFFVSVRKAI
TVLFFIGVRC YEAYPNTSLP PSILEDSLEN NEGVPSPMLS ISNLTQEQVQ DYVNKTNSHL
PAGKQVEISL VNGAKNLVVS GPPQSLYGLN LTLRKAKAPS GLDQSRIPFS ERKLKFSNRF
LPVASPFHSH LLVPASDLIN KDLVKNNVSF NAKDIQIPVY DTFDGSDLRV LSGSISERIV
DCIIRLPVKW ETTTQFKATH ILDFGPGGAS GLGVLTHRNK DGTGVRVIVA GTLDINPDDD
YGFKQEIFDV TSNGLKKNPN WLEEYHPKLI KNKSGKIFVE TKFSKLIGRP PLLVPGMTPC
TVSPDFVAAT TNAGYTIELA GGGYFSAAGM TAAIDSVVSQ IEKGSTFGIN LIYVNPFMLQ
WGIPLIKELR SKGYPIQFLT IGAGVPSLEV ASEYIETLGL KYLGLKPGSI DAISQVINIA
KAHPNFPIAL QWTGGRGGGH HSFEDAHTPM LQMYSKIRRH PNIMLIFGSG FGSADDTYPY
LTGEWSTKFD YPPMPFDGFL FGSRVMIAKE VKTSPDAKKC IAACTGVPDD KWEQTYKKPT
GGIVTVRSEM GEPIHKIATR GVMLWKEFDE TIFNLPKNKL VPTLEAKRDY IISRLNADFQ
KPWFATVNGQ ARDLATMTYE EVAKRLVELM FIRSTNSWFD VTWRTFTGDF LRRVEERFTK
SKTLSLIQSY SLLDKPDEAI EKVFNAYPAA REQFLNAQDI DHFLSMCQNP MQKPVPFVPV
LDRRFEIFFK KDSLWQSEHL EAVVDQDVQR TCILHGPVAA QFTKVIDEPI KSIMDGIHDG
HIKKLLHQYY GDDESKIPAV EYFGGESPVD VQSQVDSSSV SEDSAVFKAT SSTDEESWFK
ALAGSEINWR HASFLCSFIT QDKMFVSNPI RKVFKPSQGM VVEISNGNTS SKTVVTLSEP
VQGELKPTVI LKLLKENIIQ MEMIENRTMD GKPVSLPLLY NFNPDNGFAP ISEVMEDRNQ
RIKEMYWKLW IDEPFNLDFD PRDVIKGKDF EITAKEVYDF THAVGNNCED FVSRPDRTML
APMDFAIVVG WRAIIKAIFP NTVDGDLLKL VHLSNGYKMI PGAKPLQVGD VVSTTAVIES
VVNQPTGKIV DVVGTLSRNG KPVMEVTSSF FYRGNYTDFE NTFQKTVEPV YQMHIKTSKD
IAVLRSKEWF QLDDEDFDLL NKTLTFETET EVTFKNANIF SSVKCFGPIK VELPTKETVE
IGIVDYEAGA SHGNPVVDFL KRNGSTLEQK VNLENPIPIA VLDSYTPSTN EPYARVSGDL
NPIHVSRHFA SYANLPGTIT HGMFSSASVR ALIENWAADS VSSRVRGYTC QFVDMVLPNT
ALKTSIQHVG MINGRKLIKF ETRNEDDVVV LTGEAEIEQP VTTFVFTGQG SQEQGMGMDL
YKTSKAAQDV WNRADNHFKD TYGFSILDIV INNPVNLTIH FGGEKGKRIR ENYSAMIFET
IVDGKLKTEK IFKEINEHST SYTFRSEKGL LSATQFTQPA LTLMEKAAFE DLKSKGLIPA
DATFAGHSLG EYAALASLAD VMSIESLVEV VFYRGMTMQV AVPRDELGRS NYGMIAINPG
RVAASFSQEA LQYVVERVGK RTGWLVEIVN YNVENQQYVA AGDLRALDTV TNVLNFIKLQ
KIDIIELQKS LSLEEVEGHL FEIIDEASKK SAVKPRPLKL ERGFACIPLV GISVPFHSTY
LMNGVKPFKS FLKKNIIKEN VKVARLAGKY IPNLTAKPFQ VTKEYFQDVY DLTGSEPIKE
IIDNWEKYEQ S
