AKR2A_ARATH
ID AKR2A_ARATH Reviewed; 342 AA.
AC Q9SAR5; O81128; Q9SVX0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Ankyrin repeat domain-containing protein 2A {ECO:0000303|PubMed:18193034};
DE Short=AtAKR2;
GN Name=AKR2A {ECO:0000303|PubMed:18193034}; Synonyms=AFT, AKR2;
GN OrderedLocusNames=At4g35450; ORFNames=F15J1.20;
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].
RC STRAIN=cv. Landsberg erecta;
RA Wang J., Hocart C.H., Wei K.-J., John P.C.L.;
RT "Nucleotide sequence of a cDNA clone containing tandem ankyrin repeats and
RT a glycosyl hydrolase family I signature from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR98-150(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH APX3 AND GRF6, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. C24;
RX PubMed=11862948; DOI=10.1046/j.0960-7412.2001.01205.x;
RA Yan J., Wang J., Zhang H.;
RT "An ankyrin repeat-containing protein plays a role in both disease
RT resistance and antioxidation metabolism.";
RL Plant J. 29:193-202(2002).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=18193034; DOI=10.1038/ncb1683;
RA Bae W., Lee Y.J., Kim D.H., Lee J., Kim S., Sohn E.J., Hwang I.;
RT "AKR2A-mediated import of chloroplast outer membrane proteins is essential
RT for chloroplast biogenesis.";
RL Nat. Cell Biol. 10:220-227(2008).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-25; PRO-113 AND GLU-150,
RP INTERACTION WITH TOM20-4; CYTB5-E; CBR1; APX3; APX5 AND TOC34, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=20215589; DOI=10.1105/tpc.109.065979;
RA Shen G., Kuppu S., Venkataramani S., Wang J., Yan J., Qiu X., Zhang H.;
RT "ANKYRIN REPEAT-CONTAINING PROTEIN 2A is an essential molecular chaperone
RT for peroxisomal membrane-bound ASCORBATE PEROXIDASE3 in Arabidopsis.";
RL Plant Cell 22:811-831(2010).
RN [9]
RP INTERACTION WITH APX3, AND REVIEW.
RX PubMed=21057222; DOI=10.4161/psb.5.11.13714;
RA Zhang H., Li X., Zhang Y., Kuppu S., Shen G.;
RT "Is AKR2A an essential molecular chaperone for a class of membrane-bound
RT proteins in plants?";
RL Plant Signal. Behav. 5:1520-1522(2010).
RN [10]
RP INTERACTION WITH HSP17.8; HSP17.4A; HSP17.6A AND HSP18.1.
RC STRAIN=cv. Columbia;
RX PubMed=21730198; DOI=10.1104/pp.111.178681;
RA Kim D.H., Xu Z.-Y., Na Y.J., Yoo Y.-J., Lee J., Sohn E.-J., Hwang I.;
RT "Small heat shock protein Hsp17.8 functions as an AKR2A cofactor in the
RT targeting of chloroplast outer membrane proteins in Arabidopsis.";
RL Plant Physiol. 157:132-146(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 211-342, FUNCTION, DOMAIN,
RP SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH
RP MONOGALACTOSYLDIACYLGLYCEROL AND PHOSPHATIDYLGLYCEROL, AND MUTAGENESIS OF
RP HIS-223; GLU-246; TYR-294 AND ARG-296.
RX PubMed=25203210; DOI=10.1016/j.devcel.2014.07.026;
RA Kim D.H., Park M.-J., Gwon G.H., Silkov A., Xu Z.-Y., Yang E.C., Song S.,
RA Song K., Kim Y., Yoon H.S., Honig B., Cho W., Cho Y., Hwang I.;
RT "An ankyrin repeat domain of AKR2 drives chloroplast targeting through
RT coincident binding of two chloroplast lipids.";
RL Dev. Cell 30:598-609(2014).
CC -!- FUNCTION: Exhibits chaperone activity toward chloroplast outer envelope
CC membrane, mitochondrion outer membrane, endoplasmic reticulum membrane
CC and peroxisomal proteins, by recruiting specific proteins containing a
CC single transmembrane associated with an AKR2A-binding sequence (ABS)
CC and subsequently binding glycolipids (e.g. monogalactosyldiacylglycerol
CC (MGDG) and phosphatidylglycerol (PG)) present in the membrane of the
CC target organelle (PubMed:18193034, PubMed:20215589, PubMed:25203210).
CC Seems to be involved in the regulation of hydrogen peroxide levels
CC during biotic and abiotic stresses by optimizing the ascorbate
CC peroxidase 3 (APX3) hydrogen peroxide-degrading activity. This
CC regulation might be monitored by GRF6. Cytosolic targeting factor for
CC chloroplast outer membrane (COM) proteins that mediates sorting and
CC targeting of nascent chloroplast outer envelope membrane (OEM) proteins
CC to the chloroplast. Facilitates the targeting of OEP7 to chloroplasts
CC (PubMed:18193034). Facilitates the targeting of APX3 to peroxisomes.
CC Involved in cellular metabolism (e.g. peroxisome activity) and required
CC for plant growth and development (PubMed:20215589).
CC {ECO:0000269|PubMed:11862948, ECO:0000269|PubMed:18193034,
CC ECO:0000269|PubMed:20215589, ECO:0000269|PubMed:25203210}.
CC -!- SUBUNIT: Interacts with TOM20-4, CYTB5-E, CBR1, APX3, APX5, TOC34 and
CC GRF6. Binds to chloroplast outer envelope membrane (OEM) protein
CC targeting signals, as well as to chloroplasts. Interacts with OEP7
CC (PubMed:18193034). Binds to HSP17.8 via its ankyrin repeats, this
CC interaction enhances chaperone activity and chloroplast binding.
CC Interacts also with HSP17.4A, HSP17.6A and HSP18.1 (PubMed:21730198).
CC Binds specifically to two chloroplast glycolipids,
CC monogalactosyldiacylglycerol (MGDG) and phosphatidylglycerol (PG)
CC (PubMed:25203210). {ECO:0000269|PubMed:11862948,
CC ECO:0000269|PubMed:18193034, ECO:0000269|PubMed:20215589,
CC ECO:0000269|PubMed:21057222, ECO:0000269|PubMed:21730198,
CC ECO:0000269|PubMed:25203210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20215589}. Nucleus
CC {ECO:0000269|PubMed:20215589}. Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:25203210}; Peripheral membrane protein
CC {ECO:0000269|PubMed:25203210}; Cytoplasmic side
CC {ECO:0000269|PubMed:25203210}.
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=Q9SAR5-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at basal level.
CC {ECO:0000269|PubMed:11862948}.
CC -!- DOMAIN: The ankyrin repeats (ANK) mediate interactions with hexoses-
CC containing lipids present in organellar membranes (e.g. chloroplast),
CC such as monogalactosyldiacylglycerol (MGDG) and phosphatidylglycerol
CC (PG). {ECO:0000269|PubMed:25203210}.
CC -!- DISRUPTION PHENOTYPE: Lethal chlorotic phenotype when homozygote
CC (PubMed:20215589). Reduced levels of chloroplast proteins, including
CC outer envelope membrane (OEM) proteins. Defective chloroplast
CC biogenesis (PubMed:18193034). Reduced APX3 levels and reduced targeting
CC of APX3 to peroxisomes. Compromised peroxisomal function leading to
CC increased sensitivity to aminotriazole during seed germination and
CC shorter hypocotyls in darkness in the absence of sucrose
CC (PubMed:20215589). {ECO:0000269|PubMed:18193034,
CC ECO:0000269|PubMed:20215589}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC33264.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF034387; AAC33264.2; ALT_INIT; mRNA.
DR EMBL; U70425; AAD10949.1; -; mRNA.
DR EMBL; AL117188; CAB54873.1; -; Genomic_DNA.
DR EMBL; AL161587; CAB80261.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86513.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86515.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86516.1; -; Genomic_DNA.
DR EMBL; AF386982; AAK62427.1; -; mRNA.
DR EMBL; AY081477; AAM10039.1; -; mRNA.
DR EMBL; AY087377; AAM64927.1; -; mRNA.
DR PIR; T41742; T41742.
DR RefSeq; NP_195270.1; NM_119710.5. [Q9SAR5-1]
DR RefSeq; NP_849497.1; NM_179166.1. [Q9SAR5-1]
DR RefSeq; NP_849498.1; NM_179167.2. [Q9SAR5-1]
DR PDB; 4TUM; X-ray; 2.30 A; A/B/C/D/E=211-342.
DR PDB; 5EID; X-ray; 2.00 A; A=211-342.
DR PDBsum; 4TUM; -.
DR PDBsum; 5EID; -.
DR AlphaFoldDB; Q9SAR5; -.
DR SMR; Q9SAR5; -.
DR BioGRID; 14979; 16.
DR IntAct; Q9SAR5; 1.
DR STRING; 3702.AT4G35450.5; -.
DR iPTMnet; Q9SAR5; -.
DR PaxDb; Q9SAR5; -.
DR EnsemblPlants; AT4G35450.1; AT4G35450.1; AT4G35450. [Q9SAR5-1]
DR EnsemblPlants; AT4G35450.2; AT4G35450.2; AT4G35450. [Q9SAR5-1]
DR EnsemblPlants; AT4G35450.3; AT4G35450.3; AT4G35450. [Q9SAR5-1]
DR GeneID; 829697; -.
DR Gramene; AT4G35450.1; AT4G35450.1; AT4G35450. [Q9SAR5-1]
DR Gramene; AT4G35450.2; AT4G35450.2; AT4G35450. [Q9SAR5-1]
DR Gramene; AT4G35450.3; AT4G35450.3; AT4G35450. [Q9SAR5-1]
DR KEGG; ath:AT4G35450; -.
DR Araport; AT4G35450; -.
DR eggNOG; KOG0504; Eukaryota.
DR InParanoid; Q9SAR5; -.
DR PhylomeDB; Q9SAR5; -.
DR PRO; PR:Q9SAR5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SAR5; baseline and differential.
DR Genevisible; Q9SAR5; AT.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031359; C:integral component of chloroplast outer membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030941; F:chloroplast targeting sequence binding; IDA:UniProtKB.
DR GO; GO:0051861; F:glycolipid binding; IDA:UniProtKB.
DR GO; GO:0045036; P:protein targeting to chloroplast; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR041243; STI1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF17830; STI1; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Chaperone; Chloroplast;
KW Cytoplasm; Lipid-binding; Membrane; Nucleus; Plastid;
KW Plastid outer membrane; Reference proteome; Repeat.
FT CHAIN 1..342
FT /note="Ankyrin repeat domain-containing protein 2A"
FT /id="PRO_0000067059"
FT REPEAT 217..246
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 250..279
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 283..312
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 316..342
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 223
FT /ligand="a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:17615"
FT /evidence="ECO:0000269|PubMed:25203210"
FT BINDING 246
FT /ligand="a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:17615"
FT /evidence="ECO:0000269|PubMed:25203210"
FT BINDING 294
FT /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT /ligand_id="ChEBI:CHEBI:64716"
FT /evidence="ECO:0000269|PubMed:25203210"
FT BINDING 296
FT /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT /ligand_id="ChEBI:CHEBI:64716"
FT /evidence="ECO:0000269|PubMed:25203210"
FT MUTAGEN 25
FT /note="S->F: In akr2a-1; small plants with small and curled
FT rosette leaves, as well as delayed flowering, especially in
FT chilling temperature conditions. Abnormal abaxial epidermal
FT wavy cell shape and absence of cell boundaries between the
FT neighboring surface cells. Impaired interaction with APX3."
FT /evidence="ECO:0000269|PubMed:20215589"
FT MUTAGEN 113
FT /note="P->L: In akr2a-3; small plants with small and curled
FT rosette leaves, as well as delayed flowering, especially in
FT chilling temperature conditions.Abnormal abaxial epidermal
FT wavy cell shape and absence of cell boundaries between the
FT neighboring surface cells. Impaired interaction with APX3."
FT /evidence="ECO:0000269|PubMed:20215589"
FT MUTAGEN 150
FT /note="E->K: In akr2a-6; small plants with small and curled
FT rosette leaves, as well as delayed flowering, especially in
FT chilling temperature conditions. Reduced interaction with
FT APX3."
FT /evidence="ECO:0000269|PubMed:20215589"
FT MUTAGEN 223
FT /note="H->A: Reduced binding to
FT monogalactosyldiacylglycerol (MGDG)."
FT /evidence="ECO:0000269|PubMed:25203210"
FT MUTAGEN 246
FT /note="E->A: Reduced binding to
FT monogalactosyldiacylglycerol (MGDG) and
FT phosphatidylglycerol (PG)."
FT /evidence="ECO:0000269|PubMed:25203210"
FT MUTAGEN 294
FT /note="Y->A: Reduced binding to phosphatidylglycerol (PG)."
FT /evidence="ECO:0000269|PubMed:25203210"
FT MUTAGEN 296
FT /note="R->A: Reduced binding to phosphatidylglycerol (PG)."
FT /evidence="ECO:0000269|PubMed:25203210"
FT CONFLICT 243
FT /note="N -> T (in Ref. 1; AAC33264)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="C -> S (in Ref. 2; AAD10949)"
FT /evidence="ECO:0000305"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:5EID"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:5EID"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:5EID"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:5EID"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:5EID"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:5EID"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:5EID"
FT HELIX 330..336
FT /evidence="ECO:0007829|PDB:5EID"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:5EID"
SQ SEQUENCE 342 AA; 36984 MW; 143B612EFC0A21A4 CRC64;
MASNSEKNPL LSDEKPKSTE ENKSSKPESA SGSSTSSAMP GLNFNAFDFS NMASILNDPS
IREMAEQIAK DPAFNQLAEQ LQRSIPNAGQ EGGFPNFDPQ QYVNTMQQVM HNPEFKTMAE
KLGTALVQDP QMSPFLDAFS NPETAEHFTE RMARMKEDPE LKPILDEIDA GGPSAMMKYW
NDPEVLKKLG EAMGMPVAGL PDQTVSAEPE VAEEGEEEES IVHQTASLGD VEGLKAALAS
GGNKDEEDSE GRTALHFACG YGELKCAQVL IDAGASVNAV DKNKNTPLHY AAGYGRKECV
SLLLENGAAV TLQNLDEKTP IDVAKLNSQL EVVKLLEKDA FL
