CADH5_ARATH
ID CADH5_ARATH Reviewed; 357 AA.
AC O49482; Q53ZN0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cinnamyl alcohol dehydrogenase 5 {ECO:0000303|PubMed:14745009};
DE Short=AtCAD5 {ECO:0000303|PubMed:14745009};
DE EC=1.1.1.195 {ECO:0000269|PubMed:14745009};
DE AltName: Full=Cinnamyl alcohol dehydrogenase D {ECO:0000303|PubMed:15937231};
GN Name=CAD5 {ECO:0000303|PubMed:14745009};
GN Synonyms=CAD-D {ECO:0000303|PubMed:15937231}, CAD6, LCAD-D;
GN OrderedLocusNames=At4g34230 {ECO:0000312|Araport:AT4G34230};
GN ORFNames=F28A23.10 {ECO:0000312|EMBL:CAA17549.1};
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14745009; DOI=10.1073/pnas.0307987100;
RA Kim S.-J., Kim M.-R., Bedgar D.L., Moinuddin S.G.A., Cardenas C.L.,
RA Davin L.B., Kang C., Lewis N.G.;
RT "Functional reclassification of the putative cinnamyl alcohol dehydrogenase
RT multigene family in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1455-1460(2004).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12805615; DOI=10.1104/pp.103.021048;
RA Sibout R., Eudes A., Pollet B., Goujon T., Mila I., Granier F., Seguin A.,
RA Lapierre C., Jouanin L.;
RT "Expression pattern of two paralogs encoding cinnamyl alcohol
RT dehydrogenases in Arabidopsis. Isolation and characterization of the
RT corresponding mutants.";
RL Plant Physiol. 132:848-860(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15937231; DOI=10.1105/tpc.105.030767;
RA Sibout R., Eudes A., Mouille G., Pollet B., Lapierre C., Jouanin L.,
RA Seguin A.;
RT "CINNAMYL ALCOHOL DEHYDROGENASE-C and -D are the primary genes involved in
RT lignin biosynthesis in the floral stem of Arabidopsis.";
RL Plant Cell 17:2059-2076(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17467016; DOI=10.1016/j.phytochem.2007.02.032;
RA Kim S.-J., Kim K.-W., Cho M.-H., Franceschi V.R., Davin L.B., Lewis N.G.;
RT "Expression of cinnamyl alcohol dehydrogenases and their putative
RT homologues during Arabidopsis thaliana growth and development: lessons for
RT database annotations?";
RL Phytochemistry 68:1957-1974(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND NADP,
RP COFACTOR, MUTAGENESIS OF GLU-70, AND SUBUNIT.
RX PubMed=16633561; DOI=10.1039/b601672c;
RA Youn B., Camacho R., Moinuddin S.G.A., Lee C., Davin L.B., Lewis N.G.,
RA Kang C.;
RT "Crystal structures and catalytic mechanism of the Arabidopsis cinnamyl
RT alcohol dehydrogenases AtCAD5 and AtCAD4.";
RL Org. Biomol. Chem. 4:1687-1697(2006).
CC -!- FUNCTION: Involved in lignin biosynthesis in the floral stem. Catalyzes
CC the final step specific for the production of lignin monomers.
CC Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-
CC hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl
CC aldehyde to their respective alcohols. {ECO:0000269|PubMed:12805615,
CC ECO:0000269|PubMed:14745009, ECO:0000269|PubMed:15937231}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) +
CC NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.195; Evidence={ECO:0000269|PubMed:14745009};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394;
CC Evidence={ECO:0000269|PubMed:14745009};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16633561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:16633561};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for 4-coumaraldehyde (at pH 6.25-6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC KM=68 uM for caffeyl aldehyde (at pH 6.0-6.25 and 30-35 degrees
CC Celsius) {ECO:0000269|PubMed:14745009};
CC KM=35 uM for coniferaldehyde (at pH 6.0-6.25 and 30-35 degrees
CC Celsius) {ECO:0000269|PubMed:14745009};
CC KM=22 uM for 5-hydroxyconiferaldehyde (at pH 6.25-6.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:14745009};
CC KM=20 uM for sinapaldehyde (at pH 6.0-6.25 and 30-35 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC Vmax=187.3 pmol/sec/ug enzyme with 4-coumaraldehyde as substrate (at
CC pH 6.25-6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=94.1 pmol/sec/ug enzyme with caffeyl aldehyde as substrate (at
CC pH 6.0-6.25 and 30-35 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=157.4 pmol/sec/ug enzyme with coniferaldehyde as substrate (at
CC pH 6.0-6.25 and 30-35 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=106.9 pmol/sec/ug enzyme with 5-hydroxyconiferaldehyde as
CC substrate (at pH 6.25-6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC Vmax=177.0 pmol/sec/ug enzyme with sinapaldehyde as substrate (at pH
CC 6.0-6.25 and 30-35 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16633561}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O49482-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at the lateral root initiation sites, in
CC the vascular tissues of the primary lateral root and the root caps.
CC Expressed in the hypocotyl, cotyledon and leaf veins, apical meristem
CC region, at the base of the trichomes, hydathodes and cauline leaves. In
CC stems, expressed in the cells associated with the vascular cambium,
CC interfascicular cambium and the developing xylem. Expressed in the
CC vascular strand of petals and sepals, anthers, stamen filaments, stigma
CC in flowers, and abscission, style and stigmatic regions of siliques.
CC {ECO:0000269|PubMed:12805615, ECO:0000269|PubMed:17467016}.
CC -!- DISRUPTION PHENOTYPE: Reduced lignin content and rigidity of the floral
CC stems. {ECO:0000269|PubMed:15937231}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AY302082; AAP59435.1; -; mRNA.
DR EMBL; AL021961; CAA17549.1; -; Genomic_DNA.
DR EMBL; AL161585; CAB80140.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86344.1; -; Genomic_DNA.
DR EMBL; AY034919; AAK59426.1; -; mRNA.
DR EMBL; AY113919; AAM44967.1; -; mRNA.
DR PIR; T05413; T05413.
DR RefSeq; NP_195149.1; NM_119587.4. [O49482-1]
DR PDB; 2CF5; X-ray; 2.00 A; A=1-357.
DR PDB; 2CF6; X-ray; 2.60 A; A=1-357.
DR PDBsum; 2CF5; -.
DR PDBsum; 2CF6; -.
DR AlphaFoldDB; O49482; -.
DR SMR; O49482; -.
DR BioGRID; 14854; 6.
DR IntAct; O49482; 4.
DR STRING; 3702.AT4G34230.2; -.
DR MetOSite; O49482; -.
DR PaxDb; O49482; -.
DR PRIDE; O49482; -.
DR ProteomicsDB; 240585; -. [O49482-1]
DR EnsemblPlants; AT4G34230.1; AT4G34230.1; AT4G34230. [O49482-1]
DR GeneID; 829572; -.
DR Gramene; AT4G34230.1; AT4G34230.1; AT4G34230. [O49482-1]
DR KEGG; ath:AT4G34230; -.
DR Araport; AT4G34230; -.
DR TAIR; locus:2124311; AT4G34230.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_2_1; -.
DR InParanoid; O49482; -.
DR PhylomeDB; O49482; -.
DR BioCyc; MetaCyc:AT4G34230-MON; -.
DR BRENDA; 1.1.1.195; 399.
DR SABIO-RK; O49482; -.
DR UniPathway; UPA00711; -.
DR EvolutionaryTrace; O49482; -.
DR PRO; PR:O49482; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49482; baseline and differential.
DR Genevisible; O49482; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IDA:TAIR.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0052747; F:sinapyl alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
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; Alternative splicing; Lignin biosynthesis; Metal-binding;
KW NADP; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..357
FT /note="Cinnamyl alcohol dehydrogenase 5"
FT /id="PRO_0000160791"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF5, ECO:0007744|PDB:2CF6"
FT BINDING 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF6"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF5, ECO:0007744|PDB:2CF6"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF5, ECO:0007744|PDB:2CF6"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF5, ECO:0007744|PDB:2CF6"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF5, ECO:0007744|PDB:2CF6"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF5, ECO:0007744|PDB:2CF6"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF5, ECO:0007744|PDB:2CF6"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF5, ECO:0007744|PDB:2CF6"
FT BINDING 167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF6"
FT BINDING 188..193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF6"
FT BINDING 211..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF6"
FT BINDING 251
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF6"
FT BINDING 275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF6"
FT BINDING 298..300
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16633561,
FT ECO:0007744|PDB:2CF6"
FT MUTAGEN 70
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16633561"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2CF6"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:2CF5"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2CF5"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:2CF6"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:2CF5"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 303..315
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:2CF5"
FT HELIX 330..338
FT /evidence="ECO:0007829|PDB:2CF5"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:2CF5"
SQ SEQUENCE 357 AA; 38744 MW; A505D5C28A41E933 CRC64;
MGIMEAERKT TGWAARDPSG ILSPYTYTLR ETGPEDVNIR IICCGICHTD LHQTKNDLGM
SNYPMVPGHE VVGEVVEVGS DVSKFTVGDI VGVGCLVGCC GGCSPCERDL EQYCPKKIWS
YNDVYINGQP TQGGFAKATV VHQKFVVKIP EGMAVEQAAP LLCAGVTVYS PLSHFGLKQP
GLRGGILGLG GVGHMGVKIA KAMGHHVTVI SSSNKKREEA LQDLGADDYV IGSDQAKMSE
LADSLDYVID TVPVHHALEP YLSLLKLDGK LILMGVINNP LQFLTPLLML GRKVITGSFI
GSMKETEEML EFCKEKGLSS IIEVVKMDYV NTAFERLEKN DVRYRFVVDV EGSNLDA
