VEP1_ARATH
ID VEP1_ARATH Reviewed; 388 AA.
AC Q9STX2; A8MRU3; Q39171;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=3-oxo-Delta(4,5)-steroid 5-beta-reductase;
DE EC=1.3.1.3 {ECO:0000269|PubMed:19166903, ECO:0000269|PubMed:20598327, ECO:0000269|PubMed:22357344};
DE AltName: Full=Delta(4)-3-oxosteroid 5-beta-reductase;
DE AltName: Full=Delta-4,5-steroid 5-beta-reductase;
DE Short=At5beta-StR;
DE AltName: Full=Progesterone 5-beta-reductase;
DE Short=5beta-POR;
DE AltName: Full=Protein VEIN PATTERNING 1;
GN Name=VEP1; Synonyms=AWI31; OrderedLocusNames=At4g24220; ORFNames=T22A6.50;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RX PubMed=9085278;
RA Yang K.Y., Moon Y.H., Choi K.H., Kim Y.H., Eun M.Y., Guh J.O., Kim K.C.,
RA Cho B.H.;
RT "Structure and expression of the AWI 31 gene specifically induced by
RT wounding in Arabidopsis thaliana.";
RL Mol. Cells 7:131-135(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION BY WOUNDING.
RX PubMed=11917087; DOI=10.1093/pcp/pcf042;
RA Jun J.H., Ha C.M., Nam H.G.;
RT "Involvement of the VEP1 gene in vascular strand development in Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 43:323-330(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Leaf;
RX AGRICOLA=IND44043462; DOI=10.1007/s00606-007-0616-0;
RA Herl V., Albach D.C., Mueller-Uri F., Braeuchler C., Heubl G., Kreis W.;
RT "Using progesterone 5beta-reductase, a gene encoding a key enzyme in the
RT cardenolide biosynthesis, to infer the phylogeny of the genus Digitalis.";
RL Plant Syst. Evol. 271:65-78(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY,
RP SUBUNIT, AND 3D-STRUCTURE MODELING.
RX PubMed=19166903; DOI=10.1016/j.biochi.2008.12.005;
RA Herl V., Fischer G., Reva V.A., Stiebritz M., Muller Y.A., Mueller-Uri F.,
RA Kreis W.;
RT "The VEP1 gene (At4g24220) encodes a short-chain dehydrogenase/reductase
RT with 3-oxo-Delta4,5-steroid 5beta-reductase activity in Arabidopsis
RT thaliana L.";
RL Biochimie 91:517-525(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=20598327; DOI=10.1016/j.phytochem.2010.06.004;
RA Bauer P., Munkert J., Brydziun M., Burda E., Mueller-Uri F., Groeger H.,
RA Muller Y.A., Kreis W.;
RT "Highly conserved progesterone 5 beta-reductase genes (P5 beta R) from 5
RT beta-cardenolide-free and 5 beta-cardenolide-producing angiosperms.";
RL Phytochemistry 71:1495-1505(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22357344; DOI=10.1016/j.phytochem.2012.01.022;
RA Bauer P., Rudolph K., Mueller-Uri F., Kreis W.;
RT "Vein Patterning 1-encoded progesterone 5?-reductase: activity-guided
RT improvement of catalytic efficiency.";
RL Phytochemistry 77:53-59(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 17-388.
RX PubMed=30172078; DOI=10.1016/j.phytochem.2018.08.012;
RA Schmidt K., Petersen J., Munkert J., Egerer-Sieber C., Hornig M.,
RA Muller Y.A., Kreis W.;
RT "PRISEs (progesterone 5beta-reductase and/or iridoid synthase-like 1,4-
RT enone reductases): Catalytic and substrate promiscuity allows for
RT realization of multiple pathways in plant metabolism.";
RL Phytochemistry 156:9-19(2018).
CC -!- FUNCTION: Involved in vascular strand development. Catalyzes the
CC stereospecific conversion of progesterone to 5-beta-pregnane-3,20-
CC dione. Can use progesterone, testosterone, 21-acetyl cortexone, 2-
CC cyclohexenone, but-1-en-3-one, ethyl acrylate, ethylmethacrylate,
CC cortisone and canarigenone as substrates, lower activity with 3-methyl-
CC 2-cyclohexenone and 3,5,5-trimethyl-2-cyclohexenone as substrate, and
CC no activity with canarigenin, canarigenin digitoxoside and
CC pregnenolone. May be involved in the formation of 5-beta
CC phytoecdysteroids. {ECO:0000269|PubMed:11917087,
CC ECO:0000269|PubMed:19166903}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5beta-cholestan-3-one + NADP(+) = cholest-4-en-3-one + H(+) +
CC NADPH; Xref=Rhea:RHEA:11524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16074,
CC ChEBI:CHEBI:16175, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.3;
CC Evidence={ECO:0000269|PubMed:19166903, ECO:0000269|PubMed:20598327,
CC ECO:0000269|PubMed:22357344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,5beta-dihydrocortisone + NADP(+) = cortisone + H(+) + NADPH;
CC Xref=Rhea:RHEA:14037, ChEBI:CHEBI:15378, ChEBI:CHEBI:16962,
CC ChEBI:CHEBI:18093, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.3;
CC Evidence={ECO:0000269|PubMed:19166903, ECO:0000269|PubMed:20598327,
CC ECO:0000269|PubMed:22357344};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=268 uM for progesterone {ECO:0000269|PubMed:19166903,
CC ECO:0000269|PubMed:22357344};
CC KM=755 uM for cortisol {ECO:0000269|PubMed:19166903,
CC ECO:0000269|PubMed:22357344};
CC KM=1423 uM for 4-androstene-3,17-dione {ECO:0000269|PubMed:19166903,
CC ECO:0000269|PubMed:22357344};
CC KM=764 uM for cortexone {ECO:0000269|PubMed:19166903,
CC ECO:0000269|PubMed:22357344};
CC KM=5 uM for NADPH {ECO:0000269|PubMed:19166903,
CC ECO:0000269|PubMed:22357344};
CC KM=116 uM for 2-cyclohexen-1-one {ECO:0000269|PubMed:19166903,
CC ECO:0000269|PubMed:22357344};
CC Note=kcat is 10.11 min(-1) with progesterone as substrate. kcat is
CC 66.85 min(-1) with 2-cyclohexen-1-one as substrate.;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:19166903,
CC ECO:0000269|PubMed:22357344};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:19166903, ECO:0000269|PubMed:22357344};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19166903}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9STX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9STX2-2; Sequence=VSP_044368;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers, seeds
CC and siliques. Expressed in the vascular bundles.
CC {ECO:0000269|PubMed:11917087, ECO:0000269|PubMed:19166903}.
CC -!- INDUCTION: Up-regulated by wounding. Not induced by drought, high salt,
CC low temperature or herbicide treatment. {ECO:0000269|PubMed:11917087,
CC ECO:0000269|PubMed:9085278}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. Highly divergent. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA68126.1; Type=Frameshift; Evidence={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; X99793; CAA68126.1; ALT_FRAME; Genomic_DNA.
DR EMBL; EF579963; ABU55811.1; -; mRNA.
DR EMBL; AL078637; CAB45057.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79332.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84868.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84869.1; -; Genomic_DNA.
DR EMBL; AY062451; AAL32529.1; -; mRNA.
DR EMBL; BT008479; AAP37838.1; -; mRNA.
DR EMBL; AY087323; AAM64873.1; -; mRNA.
DR PIR; T09885; T09885.
DR RefSeq; NP_001078438.1; NM_001084969.1. [Q9STX2-2]
DR RefSeq; NP_194153.1; NM_118555.4. [Q9STX2-1]
DR PDB; 6EL3; X-ray; 1.90 A; A/B/C/D/E/F=17-388.
DR PDBsum; 6EL3; -.
DR AlphaFoldDB; Q9STX2; -.
DR SMR; Q9STX2; -.
DR BioGRID; 13812; 1.
DR STRING; 3702.AT4G24220.1; -.
DR iPTMnet; Q9STX2; -.
DR PaxDb; Q9STX2; -.
DR PRIDE; Q9STX2; -.
DR ProteomicsDB; 243229; -. [Q9STX2-1]
DR EnsemblPlants; AT4G24220.1; AT4G24220.1; AT4G24220. [Q9STX2-1]
DR EnsemblPlants; AT4G24220.2; AT4G24220.2; AT4G24220. [Q9STX2-2]
DR GeneID; 828523; -.
DR Gramene; AT4G24220.1; AT4G24220.1; AT4G24220. [Q9STX2-1]
DR Gramene; AT4G24220.2; AT4G24220.2; AT4G24220. [Q9STX2-2]
DR KEGG; ath:AT4G24220; -.
DR Araport; AT4G24220; -.
DR TAIR; locus:2135932; AT4G24220.
DR eggNOG; ENOG502QSRH; Eukaryota.
DR InParanoid; Q9STX2; -.
DR OMA; GRPFVFP; -.
DR PhylomeDB; Q9STX2; -.
DR BioCyc; ARA:AT4G24220-MON; -.
DR BioCyc; MetaCyc:AT4G24220-MON; -.
DR BRENDA; 1.3.1.3; 399.
DR PRO; PR:Q9STX2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STX2; baseline and differential.
DR Genevisible; Q9STX2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0047787; F:delta4-3-oxosteroid 5beta-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0035671; F:enone reductase activity; IDA:TAIR.
DR GO; GO:0046983; F:protein dimerization activity; IPI:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0008202; P:steroid metabolic process; IDA:TAIR.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; NADP; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..388
FT /note="3-oxo-Delta(4,5)-steroid 5-beta-reductase"
FT /id="PRO_0000419904"
FT ACT_SITE 147
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT ACT_SITE 178
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 35..37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:30172078,
FT ECO:0007744|PDB:6EL3"
FT BINDING 63..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:30172078,
FT ECO:0007744|PDB:6EL3"
FT BINDING 81..82
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:30172078,
FT ECO:0007744|PDB:6EL3"
FT BINDING 105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:30172078,
FT ECO:0007744|PDB:6EL3"
FT BINDING 143
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:30172078,
FT ECO:0007744|PDB:6EL3"
FT BINDING 178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:30172078,
FT ECO:0007744|PDB:6EL3"
FT BINDING 205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:30172078,
FT ECO:0007744|PDB:6EL3"
FT BINDING 212..214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:30172078,
FT ECO:0007744|PDB:6EL3"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044368"
FT CONFLICT 2
FT /note="S -> R (in Ref. 1; CAA68126)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="G -> A (in Ref. 1; CAA68126)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="I -> T (in Ref. 1; CAA68126)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="S -> R (in Ref. 1; CAA68126)"
FT /evidence="ECO:0000305"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:6EL3"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6EL3"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:6EL3"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:6EL3"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6EL3"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6EL3"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6EL3"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:6EL3"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:6EL3"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:6EL3"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:6EL3"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:6EL3"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:6EL3"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:6EL3"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:6EL3"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 340..346
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:6EL3"
FT HELIX 370..381
FT /evidence="ECO:0007829|PDB:6EL3"
SQ SEQUENCE 388 AA; 44230 MW; 5ED9D6C12330A161 CRC64;
MSWWWAGAIG AAKKKLDEDE PSQSFESVAL IIGVTGIVGN SLAEILPLSD TPGGPWKVYG
VARRPRPTWN ADHPIDYIQC DVSDAEDTRS KLSPLTDVTH VFYVTWTNRE SESENCEANG
SMLRNVLQAI IPYAPNLRHV CLQTGTKHYL GPFTNVDGPR HDPPFTEDMP RLQIQNFYYT
QEDILFEEIK KIETVTWSIH RPNMIFGFSP YSLMNIVGTL CVYAAICKHE GSPLLFPGSK
KAWEGFMTAS DADLIAEQQI WAAVDPYAKN EAFNCNNADI FKWKHLWKIL AEQFGIEEYG
FEEGKNLGLV EMMKGKERVW EEMVKENQLQ EKKLEEVGVW WFADVILGVE GMIDSMNKSK
EYGFLGFRNS NNSFISWIDK YKAFKIVP
