ACOX4_ARATH
ID ACOX4_ARATH Reviewed; 436 AA.
AC Q96329;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Acyl-coenzyme A oxidase 4, peroxisomal {ECO:0000305};
DE Short=AOX 4 {ECO:0000305};
DE EC=1.3.3.6 {ECO:0000269|PubMed:10212254};
DE AltName: Full=G6p {ECO:0000312|EMBL:AAB18129.1};
DE AltName: Full=Short-chain acyl-CoA oxidase {ECO:0000303|PubMed:10212254};
DE Short=AtCX4 {ECO:0000303|PubMed:12682048};
DE Short=AtG6 {ECO:0000312|EMBL:AAB18129.1};
DE Short=SAOX {ECO:0000305};
GN Name=ACX4 {ECO:0000303|PubMed:12682048};
GN Synonyms=G6 {ECO:0000312|EMBL:AAB18129.1};
GN OrderedLocusNames=At3g51840 {ECO:0000312|Araport:AT3G51840};
GN ORFNames=ATEM1.9 {ECO:0000312|EMBL:AAC14411.1};
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].
RC STRAIN=cv. Columbia;
RA Grellet F., Gaubier P., Wu H.-J., Laudie M., Berger C., Delseny M.;
RT "Structure of the Arabidopsis thaliana Em1 locus.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=10212254; DOI=10.1074/jbc.274.18.12715;
RA Hayashi H., De Bellis L., Ciurli A., Kondo M., Hayashi M., Nishimura M.;
RT "A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant
RT peroxisomes.";
RL J. Biol. Chem. 274:12715-12721(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10645728; DOI=10.1023/a:1006395324818;
RA Comella P., Wu H.-J., Laudie M., Berger C., Cooke R., Delseny M.,
RA Grellet F.;
RT "Fine sequence analysis of 60 kb around the Arabidopsis thaliana AtEm1
RT locus on chromosome III.";
RL Plant Mol. Biol. 41:687-700(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.
RX PubMed=12682048; DOI=10.1074/jbc.m300826200;
RA Rylott E.L., Rogers C.A., Gilday A.D., Edgell T., Larson T.R., Graham I.A.;
RT "Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities
RT accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential
RT for embryo development.";
RL J. Biol. Chem. 278:21370-21377(2003).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=15743450; DOI=10.1111/j.1365-313x.2005.02343.x;
RA Adham A.R., Zolman B.K., Millius A., Bartel B.;
RT "Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and
RT overlapping roles in beta-oxidation.";
RL Plant J. 41:859-874(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31064880; DOI=10.1073/pnas.1904143116;
RA Wang L., Wang C., Liu X., Cheng J., Li S., Zhu J.K., Gong Z.;
RT "Peroxisomal beta-oxidation regulates histone acetylation and DNA
RT methylation in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:10576-10585(2019).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FAD AND ACYL-COA,
RP AND SUBUNIT.
RX PubMed=16887802; DOI=10.1074/jbc.m603405200;
RA Mackenzie J., Pedersen L., Arent S., Henriksen A.;
RT "Controlling electron transfer in acyl-CoA oxidases and dehydrogenases: a
RT structural view.";
RL J. Biol. Chem. 281:31012-31020(2006).
CC -!- FUNCTION: Catalyzes the desaturation of short-chain acyl-CoAs to 2-
CC trans-enoyl-CoAs (PubMed:10212254, PubMed:15743450). Active on butyryl-
CC CoA (C4), hexanoyl-CoA (C6), and octanoyl-CoA (C8) (PubMed:10212254).
CC Has no activity as acyl-CoA dehydrogenase or on crotonyl-CoA (an
CC unsaturated C4:1 carbocyclic ester) or glutaryl-CoA (a dicarboxylic
CC ester) (PubMed:10212254). Peroxisomal fatty acid beta-oxidation is
CC essential for embryo development (PubMed:12682048). Acts as a
CC suppressor of transcriptional silencing (PubMed:31064880). Required for
CC nuclear histone acetylation and DNA demethylation at some endogenous
CC genomic loci (PubMed:31064880). {ECO:0000269|PubMed:10212254,
CC ECO:0000269|PubMed:12682048, ECO:0000269|PubMed:15743450,
CC ECO:0000269|PubMed:31064880}.
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:10212254};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000269|PubMed:10212254};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + O2 = (2E)-butenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:41964, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57332, ChEBI:CHEBI:57371;
CC Evidence={ECO:0000269|PubMed:10212254};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41965;
CC Evidence={ECO:0000269|PubMed:10212254};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexanoyl-CoA + O2 = (2E)-hexenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40311, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000269|PubMed:10212254};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40312;
CC Evidence={ECO:0000269|PubMed:10212254};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10212254};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.3 uM for hexanoyl-CoA {ECO:0000269|PubMed:10212254};
CC pH dependence:
CC Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:10212254};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16887802}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000269|PubMed:10212254}.
CC Peroxisome {ECO:0000269|PubMed:10212254, ECO:0000269|PubMed:31064880}.
CC -!- TISSUE SPECIFICITY: Particularly abundant in etiolated cotyledons. Also
CC present in flowers, roots and siliques, but not detected in green
CC cotyledons, rosette leaves and stems. {ECO:0000269|PubMed:10212254}.
CC -!- DEVELOPMENTAL STAGE: Induced by seed imbibition with a peak at day 5 to
CC 7. Decreases after illumination but still detectable 5 days after
CC illumination (PubMed:10212254). {ECO:0000269|PubMed:10212254}.
CC -!- INDUCTION: Induced by dehydration and abscisic acid (ABA).
CC {ECO:0000269|PubMed:15141068}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U72505; AAB18129.1; -; mRNA.
DR EMBL; AB017643; BAA82478.1; -; mRNA.
DR EMBL; AF049236; AAC14411.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78851.1; -; Genomic_DNA.
DR EMBL; AY094441; AAM19813.1; -; mRNA.
DR EMBL; AY125536; AAM78046.1; -; mRNA.
DR EMBL; AY087793; AAM65329.1; -; mRNA.
DR PIR; T46895; T46895.
DR RefSeq; NP_190752.1; NM_115043.3.
DR PDB; 2IX5; X-ray; 2.70 A; A/B/C/D=1-436.
DR PDB; 2IX6; X-ray; 3.90 A; A/B/C/D/E/F=1-436.
DR PDBsum; 2IX5; -.
DR PDBsum; 2IX6; -.
DR AlphaFoldDB; Q96329; -.
DR SMR; Q96329; -.
DR BioGRID; 9665; 3.
DR STRING; 3702.AT3G51840.1; -.
DR SwissLipids; SLP:000000862; -.
DR iPTMnet; Q96329; -.
DR PaxDb; Q96329; -.
DR PRIDE; Q96329; -.
DR ProteomicsDB; 244351; -.
DR EnsemblPlants; AT3G51840.1; AT3G51840.1; AT3G51840.
DR GeneID; 824347; -.
DR Gramene; AT3G51840.1; AT3G51840.1; AT3G51840.
DR KEGG; ath:AT3G51840; -.
DR Araport; AT3G51840; -.
DR TAIR; locus:2074403; AT3G51840.
DR eggNOG; KOG0138; Eukaryota.
DR HOGENOM; CLU_018204_8_2_1; -.
DR InParanoid; Q96329; -.
DR OMA; AAMDCYD; -.
DR OrthoDB; 589058at2759; -.
DR PhylomeDB; Q96329; -.
DR BioCyc; ARA:AT3G51840-MON; -.
DR BioCyc; MetaCyc:AT3G51840-MON; -.
DR BRENDA; 1.3.3.6; 399.
DR EvolutionaryTrace; Q96329; -.
DR PRO; PR:Q96329; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q96329; baseline and differential.
DR Genevisible; Q96329; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IDA:TAIR.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:TAIR.
DR GO; GO:0046459; P:short-chain fatty acid metabolic process; TAS:TAIR.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR045008; ACX4-like.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR PANTHER; PTHR43188; PTHR43188; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; FAD; Fatty acid metabolism; Flavoprotein;
KW Glyoxysome; Lipid metabolism; Oxidoreductase; Peroxisome;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..436
FT /note="Acyl-coenzyme A oxidase 4, peroxisomal"
FT /id="PRO_0000201211"
FT MOTIF 434..436
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 172..175
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5, ECO:0007744|PDB:2IX6"
FT BINDING 181..184
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5, ECO:0007744|PDB:2IX6"
FT BINDING 207
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5"
FT BINDING 288
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5"
FT BINDING 313..315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5, ECO:0007744|PDB:2IX6"
FT BINDING 324
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5"
FT BINDING 381
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5, ECO:0007744|PDB:2IX6"
FT BINDING 385
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5, ECO:0007744|PDB:2IX6"
FT BINDING 409
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5"
FT BINDING 410..412
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5, ECO:0007744|PDB:2IX6"
FT BINDING 428
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16887802,
FT ECO:0007744|PDB:2IX5, ECO:0007744|PDB:2IX6"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:2IX5"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:2IX5"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:2IX5"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:2IX5"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2IX5"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:2IX5"
FT STRAND 196..207
FT /evidence="ECO:0007829|PDB:2IX5"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:2IX5"
FT STRAND 213..221
FT /evidence="ECO:0007829|PDB:2IX5"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2IX5"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:2IX5"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:2IX5"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2IX5"
FT STRAND 255..266
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 277..312
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 324..352
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 358..382
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 383..388
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 394..406
FT /evidence="ECO:0007829|PDB:2IX5"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:2IX5"
FT HELIX 411..423
FT /evidence="ECO:0007829|PDB:2IX5"
SQ SEQUENCE 436 AA; 47557 MW; B6050262D9482C6D CRC64;
MAVLSSADRA SNEKKVKSSY FDLPPMEMSV AFPQATPAST FPPCTSDYYH FNDLLTPEEQ
AIRKKVRECM EKEVAPIMTE YWEKAEFPFH ITPKLGAMGV AGGSIKGYGC PGLSITANAI
ATAEIARVDA SCSTFILVHS SLGMLTIALC GSEAQKEKYL PSLAQLNTVA CWALTEPDNG
SDASGLGTTA TKVEGGWKIN GQKRWIGNST FADLLIIFAR NTTTNQINGF IVKKDAPGLK
ATKIPNKIGL RMVQNGDILL QNVFVPDEDR LPGVNSFQDT SKVLAVSRVM VAWQPIGISM
GIYDMCHRYL KERKQFGAPL AAFQLNQQKL VQMLGNVQAM FLMGWRLCKL YETGQMTPGQ
ASLGKAWISS KARETASLGR ELLGGNGILA DFLVAKAFCD LEPIYTYEGT YDINTLVTGR
EVTGIASFKP ATRSRL
