ADH1_YEAST
ID ADH1_YEAST Reviewed; 348 AA.
AC P00330; D6W1Y3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 5.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1 {ECO:0000269|PubMed:6985717};
DE AltName: Full=Alcohol dehydrogenase I;
DE AltName: Full=YADH-1;
GN Name=ADH1; Synonyms=ADC1; OrderedLocusNames=YOL086C; ORFNames=O0947;
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=6277922; DOI=10.1016/s0021-9258(19)81067-0;
RA Bennetzen J.L., Hall B.D.;
RT "The primary structure of the Saccharomyces cerevisiae gene for alcohol
RT dehydrogenase.";
RL J. Biol. Chem. 257:3018-3025(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6279086; DOI=10.1007/978-1-4684-4142-0_26;
RA Young E.T., Williamson V.M., Taguchi A., Smith M., Sledziewski A.,
RA Russell D.W., Osterman J., Denis C., Cox D., Beier D.;
RT "The alcohol dehydrogenase genes of the yeast, Saccharomyces cerevisiae:
RT isolation, structure, and regulation.";
RL Basic Life Sci. 19:335-361(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8533473; DOI=10.1002/yea.320111009;
RA Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
RT "A 29.425 kb segment on the left arm of yeast chromosome XV contains more
RT than twice as many unknown as known open reading frames.";
RL Yeast 11:975-986(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-348, ACETYLATION AT SER-2, AND VARIANT ILE-236.
RX PubMed=320000; DOI=10.1111/j.1432-1033.1977.tb11267.x;
RA Joernvall H.;
RT "The primary structure of yeast alcohol dehydrogenase.";
RL Eur. J. Biochem. 72:425-442(1977).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 214-333, AND CATALYTIC ACTIVITY.
RX PubMed=6985717; DOI=10.1038/283214a0;
RA Williamson V.M., Bennetzen J.L., Young E.T., Nasmyth K., Hall B.D.;
RT "Isolation of the structural gene for alcohol dehydrogenase by genetic
RT complementation in yeast.";
RL Nature 283:214-216(1980).
RN [8]
RP PROTEIN SEQUENCE OF 62-76; 320-332 AND 337-348.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [9]
RP PROTEIN SEQUENCE OF 9-17; 40-48 AND 304-310.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=7737086; DOI=10.1002/elps.1150160124;
RA Norbeck J., Blomberg A.;
RT "Gene linkage of two-dimensional polyacrylamide gel electrophoresis
RT resolved proteins from isogene families in Saccharomyces cerevisiae by
RT microsequencing of in-gel trypsin generated peptides.";
RL Electrophoresis 16:149-156(1995).
RN [10]
RP REVIEW.
RX PubMed=12702265; DOI=10.1111/j.1567-1364.2002.tb00116.x;
RA Leskovac V., Trivic S., Pericin D.;
RT "The three zinc-containing alcohol dehydrogenases from baker's yeast,
RT Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 2:481-494(2002).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND THR-223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND SER-316, 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 [17]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-226; LYS-234; LYS-287 AND
RP LYS-319, AND IDENTIFICATION BY 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: This isozyme preferentially catalyzes the conversion of
CC primary unbranched alcohols to their corresponding aldehydes. Also
CC shows activity toward secondary alcohols.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:6985717};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10741;
CC Evidence={ECO:0000305|PubMed:6985717};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P00330; P00330: ADH1; NbExp=2; IntAct=EBI-2218, EBI-2218;
CC P00330; P34230: PXA2; NbExp=2; IntAct=EBI-2218, EBI-2464632;
CC P00330; P39109: YCF1; NbExp=2; IntAct=EBI-2218, EBI-21779;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: PubMed:320000 sequence has several conflicting residues
CC and reports microheterogeneities at additional postitions. Analysis of
CC the sequence suggests that the sequenced protein was a mixture of at
CC least 3 of the different isoforms of alcohol dehydrogenases found in
CC yeast. {ECO:0000305|PubMed:320000}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; V01292; CAA24601.1; -; Genomic_DNA.
DR EMBL; M38456; AAA34410.1; -; Genomic_DNA.
DR EMBL; X83121; CAA58193.1; -; Genomic_DNA.
DR EMBL; Z74828; CAA99098.1; -; Genomic_DNA.
DR EMBL; V01291; CAA24600.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10699.1; -; Genomic_DNA.
DR PIR; S57383; DEBYA.
DR RefSeq; NP_014555.1; NM_001183340.1.
DR PDB; 4W6Z; X-ray; 2.40 A; A/B/C/D=2-348.
DR PDB; 5ENV; X-ray; 3.00 A; A/B=2-348.
DR PDB; 7KCB; EM; 2.77 A; A/B/C/D=2-348.
DR PDBsum; 4W6Z; -.
DR PDBsum; 5ENV; -.
DR PDBsum; 7KCB; -.
DR AlphaFoldDB; P00330; -.
DR SASBDB; P00330; -.
DR SMR; P00330; -.
DR BioGRID; 34317; 252.
DR DIP; DIP-1143N; -.
DR IntAct; P00330; 218.
DR MINT; P00330; -.
DR STRING; 4932.YOL086C; -.
DR MoonDB; P00330; Curated.
DR iPTMnet; P00330; -.
DR SwissPalm; P00330; -.
DR COMPLUYEAST-2DPAGE; P00330; -.
DR SWISS-2DPAGE; P00330; -.
DR MaxQB; P00330; -.
DR PaxDb; P00330; -.
DR PRIDE; P00330; -.
DR TopDownProteomics; P00330; -.
DR EnsemblFungi; YOL086C_mRNA; YOL086C; YOL086C.
DR GeneID; 854068; -.
DR KEGG; sce:YOL086C; -.
DR SGD; S000005446; ADH1.
DR VEuPathDB; FungiDB:YOL086C; -.
DR eggNOG; KOG0023; Eukaryota.
DR GeneTree; ENSGT00940000171159; -.
DR HOGENOM; CLU_026673_20_1_1; -.
DR InParanoid; P00330; -.
DR OMA; QYAHNVF; -.
DR BioCyc; MetaCyc:YOL086C-MON; -.
DR BioCyc; YEAST:YOL086C-MON; -.
DR BRENDA; 1.1.1.1; 984.
DR SABIO-RK; P00330; -.
DR EvolutionaryTrace; P00330; -.
DR PRO; PR:P00330; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P00330; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0046809; C:replication compartment; IDA:SGD.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1904408; F:melatonin binding; IDA:SGD.
DR GO; GO:0019170; F:methylglyoxal reductase (NADH-dependent) activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000947; P:amino acid catabolic process to alcohol via Ehrlich pathway; IGI:SGD.
DR GO; GO:0043458; P:ethanol biosynthetic process involved in glucose fermentation to ethanol; IMP:SGD.
DR GO; GO:0006116; P:NADH oxidation; IDA:SGD.
DR GO; GO:0045069; P:regulation of viral genome replication; IDA:SGD.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Metal-binding; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:320000"
FT CHAIN 2..348
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160730"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 178..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 269..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:320000"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 234
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 319
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT VARIANT 236
FT /note="T -> I"
FT /evidence="ECO:0000269|PubMed:320000"
FT CONFLICT 21
FT /note="Y -> H (in Ref. 1; CAA24601 and 2; AAA34410)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="V -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="Q -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="I -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="D -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="V -> I (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="I -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4W6Z"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:4W6Z"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:4W6Z"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:4W6Z"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4W6Z"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:4W6Z"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:4W6Z"
SQ SEQUENCE 348 AA; 36849 MW; F14AE24B5D8D12A5 CRC64;
MSIPETQKGV IFYESHGKLE YKDIPVPKPK ANELLINVKY SGVCHTDLHA WHGDWPLPVK
LPLVGGHEGA GVVVGMGENV KGWKIGDYAG IKWLNGSCMA CEYCELGNES NCPHADLSGY
THDGSFQQYA TADAVQAAHI PQGTDLAQVA PILCAGITVY KALKSANLMA GHWVAISGAA
GGLGSLAVQY AKAMGYRVLG IDGGEGKEEL FRSIGGEVFI DFTKEKDIVG AVLKATDGGA
HGVINVSVSE AAIEASTRYV RANGTTVLVG MPAGAKCCSD VFNQVVKSIS IVGSYVGNRA
DTREALDFFA RGLVKSPIKV VGLSTLPEIY EKMEKGQIVG RYVVDTSK
