JOX2_ARATH
ID JOX2_ARATH Reviewed; 371 AA.
AC Q9FFF6; Q8LF06;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Jasmonate-induced oxygenase 2 {ECO:0000303|PubMed:28559313};
DE EC=1.14.11.- {ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569, ECO:0000269|PubMed:33516967};
DE AltName: Full=2-oxoglutarate-dependent dioxygenase JOX2 {ECO:0000305};
DE AltName: Full=Jasmonic acid oxidase 2 {ECO:0000303|PubMed:28760569};
GN Name=JOX2 {ECO:0000303|PubMed:28559313};
GN Synonyms=JAO2 {ECO:0000303|PubMed:28760569};
GN OrderedLocusNames=At5g05600 {ECO:0000312|Araport:AT5G05600};
GN ORFNames=MOP10.14 {ECO:0000312|EMBL:BAB11549.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-371.
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 [5]
RP INDUCTION BY SALT STRESS.
RX PubMed=11351099; DOI=10.1104/pp.126.1.363;
RA Gong Z., Koiwa H., Cushman M.A., Ray A., Bufford D., Kore-eda S.,
RA Matsumoto T.K., Zhu J., Cushman J.C., Bressan R.A., Hasegawa P.M.;
RT "Genes that are uniquely stress regulated in salt overly sensitive (sos)
RT mutants.";
RL Plant Physiol. 126:363-375(2001).
RN [6]
RP INDUCTION.
RX PubMed=17587374; DOI=10.1111/j.1469-8137.2007.02092.x;
RA Hectors K., Prinsen E., De Coen W., Jansen M.A., Guisez Y.;
RT "Arabidopsis thaliana plants acclimated to low dose rates of ultraviolet B
RT radiation show specific changes in morphology and gene expression in the
RT absence of stress symptoms.";
RL New Phytol. 175:255-270(2007).
RN [7]
RP FUNCTION, INDUCTION BY PHENANTHRENE, AND DISRUPTION PHENOTYPE.
RX PubMed=27637093; DOI=10.1016/j.jhazmat.2016.08.058;
RA Hernandez-Vega J.C., Cady B., Kayanja G., Mauriello A., Cervantes N.,
RA Gillespie A., Lavia L., Trujillo J., Alkio M., Colon-Carmona A.;
RT "Detoxification of polycyclic aromatic hydrocarbons (PAHs) in Arabidopsis
RT thaliana involves a putative flavonol synthase.";
RL J. Hazard. Mater. 321:268-280(2016).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND INDUCTION.
RX PubMed=28760569; DOI=10.1016/j.molp.2017.07.010;
RA Smirnova E., Marquis V., Poirier L., Aubert Y., Zumsteg J., Menard R.,
RA Miesch L., Heitz T.;
RT "Jasmonic acid oxidase 2 hydroxylates jasmonic acid and represses basal
RT defense and resistance responses against Botrytis cinerea infection.";
RL Mol. Plant 10:1159-1173(2017).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28559313; DOI=10.1073/pnas.1701101114;
RA Caarls L., Elberse J., Awwanah M., Ludwig N.R., de Vries M., Zeilmaker T.,
RA Van Wees S.C.M., Schuurink R.C., Van den Ackerveken G.;
RT "Arabidopsis JASMONATE-INDUCED OXYGENASES down-regulate plant immunity by
RT hydroxylation and inactivation of the hormone jasmonic acid.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6388-6393(2017).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 18-370 IN COMPLEX WITH
RP 2-OXOGLUTARATE; JASMONATE AND IRON ION, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-135;
RP LEU-142; PHE-157; ARG-225; HIS-244; ASP-246; PHE-317; PHE-346; ARG-350;
RP ILE-353 AND ARG-354.
RX PubMed=33516967; DOI=10.1016/j.molp.2021.01.017;
RA Zhang X., Wang D., Elberse J., Qi L., Shi W., Peng Y.L., Schuurink R.C.,
RA Van den Ackerveken G., Liu J.;
RT "Structure-guided analysis of the Arabidopsis JASMONATE-INDUCED OXYGENASE
RT (JOX) 2 reveals key residues of plant JOX recognizing jasmonic acid
RT substrate.";
RL Mol. Plant 14:820-828(2021).
CC -!- FUNCTION: 2-oxoglutarate-dependent dioxygenase involved in the
CC oxidation of jasmonate (JA), a stress-induced phytohormone synthesized
CC in response to attack by pathogens and herbivores, which triggers the
CC activation of defense responses via the JA-mediated signaling pathway
CC (PubMed:28760569, PubMed:28559313). Converts JA to 12-hydroxyjasmonate
CC (12OH-JA), an inactive form of JA (PubMed:28760569, PubMed:28559313,
CC PubMed:33516967). Is specific to free JA, and cannot oxidize the
CC bioactive form jasmonoyl-L-isoleucine (JA-Ile) or other JA-amino acid
CC conjugates (PubMed:28760569, PubMed:33516967). Prevents over-
CC accumulation of JA and indirectly its bioactive form JA-Ile under
CC stress response (PubMed:28760569, PubMed:28559313). Acts as negative
CC regulator of JA-mediated defense signaling, by contributing to 12OH-JA
CC accumulation, which represses JA defense responses upon infection by
CC the fungal pathogen Botrytis cinerea (PubMed:28760569,
CC PubMed:28559313). Acts as negative regulator of JA-mediated defense
CC responses upon infestation by the herbivorous caterpillar Mamestra
CC brassicae (PubMed:28559313). May be involved in the catabolism of
CC cytotoxic polycyclic aromatic hydrocarbons (PAHs) (PubMed:27637093).
CC {ECO:0000269|PubMed:27637093, ECO:0000269|PubMed:28559313,
CC ECO:0000269|PubMed:28760569, ECO:0000269|PubMed:33516967}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + jasmonate + O2 = (1R,2R)-12-hydroxyjasmonate
CC + CO2 + succinate; Xref=Rhea:RHEA:67144, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:58431, ChEBI:CHEBI:132022;
CC Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569,
CC ECO:0000269|PubMed:33516967};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67145;
CC Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569,
CC ECO:0000269|PubMed:33516967};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569,
CC ECO:0000269|PubMed:33516967};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
CC ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569,
CC ECO:0000269|PubMed:33516967};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805, ECO:0000269|PubMed:33516967};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.3 uM for jasmonate {ECO:0000269|PubMed:33516967};
CC -!- INDUCTION: Induced by salt stress (PubMed:11351099). Induced by
CC phenanthrene (PubMed:27637093). Down-regulated by UV-B
CC (PubMed:17587374). Induced by wounding (PubMed:28760569). Induced by
CC the infection with the fungal pathogen Botrytis cinerea
CC (PubMed:28760569, PubMed:28559313). Induced by methyl jasmonate (MeJA)
CC (PubMed:28559313). Induced by infestation with the caterpillar Mamestra
CC brassicae (PubMed:28559313). {ECO:0000269|PubMed:11351099,
CC ECO:0000269|PubMed:17587374, ECO:0000269|PubMed:27637093,
CC ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569}.
CC -!- DISRUPTION PHENOTYPE: Constitutive activation of stress-induced
CC jasmonate-dependent responses and increased antifungal resistance to
CC Botrytis cinerea (PubMed:28760569). The quadruple mutant jox1, jox2,
CC jox3 and jox4 exhibit reduced root and shoot growth, delayed flowering,
CC reduced seed production, constitutively elevated jasmonate and
CC jasmonoyl-L-isoleucine levels, and enhanced resistance to the
CC necrotrophic fungal pathogen Botrytis cinerea and the herbivorous
CC caterpillar Mamestra brassicae (PubMed:28559313). No visible phenotype
CC under normal growth conditions, but mutant seedlings have increased
CC tolerance to the cytotoxic compound phenanthrene.
CC {ECO:0000269|PubMed:27637093, ECO:0000269|PubMed:28559313,
CC ECO:0000269|PubMed:28760569}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB005241; BAB11549.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90897.1; -; Genomic_DNA.
DR EMBL; AY039893; AAK63997.1; -; mRNA.
DR EMBL; AY133665; AAM91495.1; -; mRNA.
DR EMBL; AY085111; AAM61665.1; -; mRNA.
DR RefSeq; NP_196179.1; NM_120642.3.
DR PDB; 6LSV; X-ray; 2.65 A; A/B=18-370.
DR PDBsum; 6LSV; -.
DR AlphaFoldDB; Q9FFF6; -.
DR SMR; Q9FFF6; -.
DR STRING; 3702.AT5G05600.1; -.
DR iPTMnet; Q9FFF6; -.
DR PaxDb; Q9FFF6; -.
DR PRIDE; Q9FFF6; -.
DR ProteomicsDB; 222154; -.
DR EnsemblPlants; AT5G05600.1; AT5G05600.1; AT5G05600.
DR GeneID; 830443; -.
DR Gramene; AT5G05600.1; AT5G05600.1; AT5G05600.
DR KEGG; ath:AT5G05600; -.
DR Araport; AT5G05600; -.
DR TAIR; locus:2169697; AT5G05600.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_0_1; -.
DR InParanoid; Q9FFF6; -.
DR OMA; RGKYDTW; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q9FFF6; -.
DR PRO; PR:Q9FFF6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFF6; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0120091; F:jasmonic acid hydrolase; IDA:TAIR.
DR GO; GO:0097237; P:cellular response to toxic substance; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900366; P:negative regulation of defense response to insect; IMP:UniProtKB.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IGI:TAIR.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Jasmonic acid signaling pathway;
KW Metal-binding; Oxidoreductase; Plant defense; Reference proteome.
FT CHAIN 1..371
FT /note="Jasmonate-induced oxygenase 2"
FT /id="PRO_0000438435"
FT DOMAIN 219..320
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 225
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000269|PubMed:33516967,
FT ECO:0007744|PDB:6LSV"
FT BINDING 227
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:33516967,
FT ECO:0007744|PDB:6LSV"
FT BINDING 229
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:33516967,
FT ECO:0007744|PDB:6LSV"
FT BINDING 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000269|PubMed:33516967, ECO:0007744|PDB:6LSV"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000269|PubMed:33516967, ECO:0007744|PDB:6LSV"
FT BINDING 301
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000269|PubMed:33516967, ECO:0007744|PDB:6LSV"
FT BINDING 311
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000269|PubMed:33516967, ECO:0007744|PDB:6LSV"
FT BINDING 313
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:33516967,
FT ECO:0007744|PDB:6LSV"
FT BINDING 350
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000269|PubMed:33516967,
FT ECO:0007744|PDB:6LSV"
FT BINDING 354
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000269|PubMed:33516967,
FT ECO:0007744|PDB:6LSV"
FT MUTAGEN 135
FT /note="Y->A: Reduces enzymatic activity 8-fold."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 142
FT /note="L->A: Reduces enzymatic activity 5-fold."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 157
FT /note="F->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 157
FT /note="F->Y: Increases enzymatic activity 1.2-fold."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 225
FT /note="R->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 244
FT /note="H->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 246
FT /note="D->A: Reduces enzymatic activity 4-fold."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 317
FT /note="F->A: No effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 317
FT /note="F->Y: Reduces enzymatic activity 2.5-fold."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 346
FT /note="F->A: Reduces enzymatic activity 5-fold."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 346
FT /note="F->Y: No effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 350
FT /note="R->A: Reduces enzymatic activity 2-fold."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 353
FT /note="I->A: Reduces enzymatic activity 4-fold."
FT /evidence="ECO:0000269|PubMed:33516967"
FT MUTAGEN 354
FT /note="R->A: Reduces enzymatic activity 2.5-fold."
FT /evidence="ECO:0000269|PubMed:33516967"
FT CONFLICT 236
FT /note="E -> V (in Ref. 4; AAM61665)"
FT /evidence="ECO:0000305"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:6LSV"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6LSV"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 178..203
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:6LSV"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 221..229
FT /evidence="ECO:0007829|PDB:6LSV"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:6LSV"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:6LSV"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:6LSV"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:6LSV"
SQ SEQUENCE 371 AA; 42177 MW; 37F8BF2370EFCEF8 CRC64;
MNKNKIDVKI ETKKGSMDEW PEPIVRVQSL AESNLSSLPD RYIKPASLRP TTTEDAPTAT
NIPIIDLEGL FSEEGLSDDV IMARISEACR GWGFFQVVNH GVKPELMDAA RENWREFFHM
PVNAKETYSN SPRTYEGYGS RLGVEKGASL DWSDYYFLHL LPHHLKDFNK WPSFPPTIRE
VIDEYGEELV KLSGRIMRVL STNLGLKEDK FQEAFGGENI GACLRVNYYP KCPRPELALG
LSPHSDPGGM TILLPDDQVF GLQVRKDDTW ITVKPHPHAF IVNIGDQIQI LSNSTYKSVE
HRVIVNSDKE RVSLAFFYNP KSDIPIQPLQ ELVSTHNPPL YPPMTFDQYR LFIRTQGPQG
KSHVESHISP R
