ACOX1_ARATH
ID ACOX1_ARATH Reviewed; 664 AA.
AC O65202; O23518;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 1 {ECO:0000303|PubMed:10571860};
DE Short=AOX 1 {ECO:0000305};
DE EC=1.3.3.6 {ECO:0000269|PubMed:10571860};
DE AltName: Full=Long-chain acyl-CoA oxidase {ECO:0000305};
DE Short=AtCX1 {ECO:0000303|PubMed:10571860};
GN Name=ACX1 {ECO:0000303|PubMed:10571860};
GN OrderedLocusNames=At4g16760 {ECO:0000312|Araport:AT4G16760};
GN ORFNames=dl4405c {ECO:0000312|EMBL:CAB10450.1},
GN FCAALL.119 {ECO:0000312|EMBL:CAB78718.1};
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, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX PubMed=10571860; DOI=10.1046/j.1365-313x.1999.00559.x;
RA Hooks M.A., Kellas F., Graham I.A.;
RT "Long-chain acyl-CoA oxidases of Arabidopsis.";
RL Plant J. 20:1-13(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
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 [6]
RP INDUCTION.
RX PubMed=15141068; DOI=10.1104/pp.104.039925;
RA Cruz-Castillo M., Martinez C., Buchala A., Metraux J.-P., Leon J.;
RT "Gene-specific involvement of beta-oxidation in wound-activated responses
RT in Arabidopsis.";
RL Plant Physiol. 135:85-94(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-659 OF MUTANT LEU-155 IN COMPLEX
RP WITH FAD, SUBUNIT, ACTIVE SITE, AND DISULFIDE BOND.
RX PubMed=15581893; DOI=10.1016/j.jmb.2004.10.062;
RA Pedersen L., Henriksen A.;
RT "Acyl-CoA oxidase 1 from Arabidopsis thaliana. Structure of a key enzyme in
RT plant lipid metabolism.";
RL J. Mol. Biol. 345:487-500(2005).
CC -!- FUNCTION: Catalyzes the desaturation of both long- and medium-chain
CC acyl-CoAs to 2-trans-enoyl-CoAs. Most active with C14-CoA. Activity on
CC long-chain mono-unsaturated substrates is 40% higher than with the
CC corresponding saturated substrates. Seems to be an important factor in
CC the general metabolism of root tips. May be involved in the
CC biosynthesis of jasmonic acid. {ECO:0000269|PubMed:10571860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6;
CC Evidence={ECO:0000269|PubMed:10571860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000269|PubMed:10571860};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15581893};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:15581893};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.3 uM for C14-CoA;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15581893}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=O65202-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed mainly in flowers and young seedlings.
CC Lower expression in roots, leaves and bracts.
CC {ECO:0000269|PubMed:10571860}.
CC -!- DEVELOPMENTAL STAGE: Induced by seed imbibition with a peak at day 2
CC and then declines to reach a basal level 4 days after sowing.
CC {ECO:0000269|PubMed:10571860}.
CC -!- INDUCTION: Induced by dehydration, abscisic acid (ABA) and jasmonic
CC acid (JA), and localy and systemically by wounding.
CC {ECO:0000269|PubMed:15141068}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10450.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78718.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF057044; AAC13498.1; -; mRNA.
DR EMBL; Z97341; CAB10450.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161544; CAB78718.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83798.1; -; Genomic_DNA.
DR EMBL; AY058849; AAL24237.1; -; mRNA.
DR EMBL; BT001067; AAN46824.1; -; mRNA.
DR PIR; H71434; H71434.
DR PIR; T52121; T52121.
DR RefSeq; NP_567513.4; NM_117778.8. [O65202-1]
DR PDB; 1W07; X-ray; 2.00 A; A/B=1-659.
DR PDBsum; 1W07; -.
DR AlphaFoldDB; O65202; -.
DR SMR; O65202; -.
DR BioGRID; 12674; 21.
DR IntAct; O65202; 2.
DR STRING; 3702.AT4G16760.1; -.
DR MetOSite; O65202; -.
DR PaxDb; O65202; -.
DR PRIDE; O65202; -.
DR ProteomicsDB; 244350; -. [O65202-1]
DR EnsemblPlants; AT4G16760.1; AT4G16760.1; AT4G16760. [O65202-1]
DR GeneID; 827381; -.
DR Gramene; AT4G16760.1; AT4G16760.1; AT4G16760. [O65202-1]
DR KEGG; ath:AT4G16760; -.
DR Araport; AT4G16760; -.
DR TAIR; locus:2129121; AT4G16760.
DR eggNOG; KOG0136; Eukaryota.
DR InParanoid; O65202; -.
DR OMA; WNMYNVL; -.
DR OrthoDB; 416859at2759; -.
DR PhylomeDB; O65202; -.
DR BioCyc; ARA:AT4G16760-MON; -.
DR BioCyc; MetaCyc:AT4G16760-MON; -.
DR BRENDA; 1.3.3.6; 399.
DR EvolutionaryTrace; O65202; -.
DR PRO; PR:O65202; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65202; baseline and differential.
DR Genevisible; O65202; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IDA:TAIR.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:TAIR.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IBA:GO_Central.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IMP:TAIR.
DR GO; GO:0009620; P:response to fungus; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR029320; Acyl-CoA_ox_N.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR012258; Acyl-CoA_oxidase.
DR InterPro; IPR002655; Acyl-CoA_oxidase_C.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR PANTHER; PTHR10909; PTHR10909; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF14749; Acyl-CoA_ox_N; 1.
DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR SUPFAM; SSF47203; SSF47203; 2.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; FAD;
KW Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..664
FT /note="Peroxisomal acyl-coenzyme A oxidase 1"
FT /id="PRO_0000204689"
FT MOTIF 662..664
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 424
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:15581893"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT BINDING 137
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT BINDING 138
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT BINDING 144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT BINDING 310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT BINDING 333
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT BINDING 401
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT BINDING 422
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT BINDING 426
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT DISULFID 467..576
FT /evidence="ECO:0000269|PubMed:15581893,
FT ECO:0007744|PDB:1W07"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1W07"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 58..78
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1W07"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1W07"
FT TURN 177..182
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 184..194
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 197..207
FT /evidence="ECO:0007829|PDB:1W07"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 240..250
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1W07"
FT TURN 278..282
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 283..309
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 328..361
FT /evidence="ECO:0007829|PDB:1W07"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 370..397
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 398..404
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 410..417
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:1W07"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 427..442
FT /evidence="ECO:0007829|PDB:1W07"
FT TURN 443..447
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 453..460
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 474..478
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 480..502
FT /evidence="ECO:0007829|PDB:1W07"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 508..514
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 516..538
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 548..566
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 568..573
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 579..596
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 600..605
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 611..614
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 626..635
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 637..640
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 647..650
FT /evidence="ECO:0007829|PDB:1W07"
FT HELIX 652..655
FT /evidence="ECO:0007829|PDB:1W07"
SQ SEQUENCE 664 AA; 74302 MW; 44AFD139D5434636 CRC64;
MEGIDHLADE RNKAEFDVED MKIVWAGSRH AFEVSDRIAR LVASDPVFEK SNRARLSRKE
LFKSTLRKCA HAFKRIIELR LNEEEAGRLR HFIDQPAYVD LHWGMFVPAI KGQGTEEQQK
KWLSLANKMQ IIGCYAQTEL GHGSNVQGLE TTATFDPKTD EFVIHTPTQT ASKWWPGGLG
KVSTHAVVYA RLITNGKDYG IHGFIVQLRS LEDHSPLPNI TVGDIGTKMG NGAYNSMDNG
FLMFDHVRIP RDQMLMRLSK VTREGEYVPS DVPKQLVYGT MVYVRQTIVA DASNALSRAV
CIATRYSAVR RQFGAHNGGI ETQVIDYKTQ QNRLFPLLAS AYAFRFVGEW LKWLYTDVTE
RLAASDFATL PEAHACTAGL KSLTTTATAD GIEECRKLCG GHGYLWCSGL PELFAVYVPA
CTYEGDNVVL QLQVARFLMK TVAQLGSGKV PVGTTAYMGR AAHLLQCRSG VQKAEDWLNP
DVVLEAFEAR ALRMAVTCAK NLSKFENQEQ GFQELLADLV EAAIAHCQLI VVSKFIAKLE
QDIGGKGVKK QLNNLCYIYA LYLLHKHLGD FLSTNCITPK QASLANDQLR SLYTQVRPNA
VALVDAFNYT DHYLNSVLGR YDGNVYPKLF EEALKDPLND SVVPDGYQEY LRPVLQQQLR
TARL
