ENDO2_ARATH
ID ENDO2_ARATH Reviewed; 290 AA.
AC Q9C9G4; Q8LCL6;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Endonuclease 2 {ECO:0000303|PubMed:17651368};
DE Short=AtENDO2 {ECO:0000303|PubMed:17651368};
DE EC=3.1.30.1 {ECO:0000269|PubMed:22506810, ECO:0000269|PubMed:23620482};
DE AltName: Full=Deoxyribonuclease ENDO2 {ECO:0000303|PubMed:17651368};
DE AltName: Full=Single-stranded-nucleate endonuclease ENDO2 {ECO:0000303|PubMed:17651368};
DE Flags: Precursor;
GN Name=ENDO2 {ECO:0000303|PubMed:17651368};
GN OrderedLocusNames=At1g68290 {ECO:0000312|Araport:AT1G68290};
GN ORFNames=T22E19.8 {ECO:0000312|EMBL:AAG52597.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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 [4]
RP FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17651368; DOI=10.1111/j.1365-313x.2007.03201.x;
RA Triques K., Sturbois B., Gallais S., Dalmais M., Chauvin S., Clepet C.,
RA Aubourg S., Rameau C., Caboche M., Bendahmane A.;
RT "Characterization of Arabidopsis thaliana mismatch specific endonucleases:
RT application to mutation discovery by TILLING in pea.";
RL Plant J. 51:1116-1125(2007).
RN [5]
RP PROTEIN SEQUENCE OF 28-36, SIGNAL PEPTIDE, FUNCTION, BIOTECHNOLOGY,
RP GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=22506810; DOI=10.1021/jf300945c;
RA Ko C.-Y., Lai Y.-L., Liu W.-Y., Lin C.-H., Chen Y.-T., Chen L.-F.O.,
RA Lin T.-Y., Shaw J.-F.;
RT "Arabidopsis ENDO2: its catalytic role and requirement of N-glycosylation
RT for function.";
RL J. Agric. Food Chem. 60:5169-5179(2012).
RN [6]
RP FUNCTION, MUTAGENESIS OF 283-ALA--GLY-290, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, COFACTOR, PROTEOLYTIC CLEAVAGE, AND GENE FAMILY.
RX PubMed=23620482; DOI=10.1093/pcp/pct061;
RA Lesniewicz K., Karlowski W.M., Pienkowska J.R., Krzywkowski P., Poreba E.;
RT "The plant s1-like nuclease family has evolved a highly diverse range of
RT catalytic capabilities.";
RL Plant Cell Physiol. 54:1064-1078(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 28-290 IN COMPLEX WITH ZINC,
RP GLYCOSYLATION AT ASN-118; ASN-137 AND ASN-211, AND DISULFIDE BONDS.
RX DOI=10.1016/j.bcab.2013.03.006;
RA Chou T.-L., Ko T.-P., Ko C.-Y., Lin T.-Y., Guo R.-T., Yu T.-F., Chan H.-C.,
RA Shaw J.-F., Wang A.H.-J.;
RT "Mechanistic insights to catalysis by a zinc-dependent bi-functional
RT nuclease from Arabidopsis thaliana.";
RL Biocatal. Agric. Biotechnol. 2:191-195(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 28-290 IN COMPLEX WITH ZINC AND
RP SUBSTRATE, GLYCOSYLATION AT ASN-118; ASN-137 AND ASN-211, DISULFIDE BONDS,
RP AND ACTIVITY REGULATION.
RX PubMed=25157844; DOI=10.1371/journal.pone.0105821;
RA Yu T.-F., Maestre-Reyna M., Ko C.-Y., Ko T.-P., Sun Y.-J., Lin T.-Y.,
RA Shaw J.-F., Wang A.H.-J.;
RT "Structural insights of the ssDNA binding site in the multifunctional
RT endonuclease AtBFN2 from Arabidopsis thaliana.";
RL PLoS ONE 9:e105821-e105821(2014).
CC -!- FUNCTION: Endonuclease mostly active on RNA and ssDNA, and to a lower
CC extent, on dsDNA (PubMed:22506810, PubMed:23620482). Can cleave
CC mismatch regions in heteroduplex DNA containing single base pair
CC mismatches or insertion/deletion bases (PubMed:22506810). In
CC contradiction with PubMed:22506810, cannot hydrolyze single-stranded
CC DNA and does not cleave mismatches (PubMed:17651368).
CC {ECO:0000269|PubMed:17651368, ECO:0000269|PubMed:22506810,
CC ECO:0000269|PubMed:23620482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-
CC phosphooligonucleotide end-products.; EC=3.1.30.1;
CC Evidence={ECO:0000269|PubMed:22506810, ECO:0000269|PubMed:23620482};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23620482};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:23620482};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:23620482, ECO:0000269|PubMed:25157844,
CC ECO:0000269|Ref.7};
CC Note=Binds 3 divalent metal cations (PubMed:23620482, Ref.7,
CC PubMed:25157844). Use Mn(2+) and Ca(2+) as cofactors with ssDNA as
CC substrate in basic conditions (pH 8) (PubMed:23620482). Can use Zn(2+)
CC with lower efficiency with dsDNA and ssDNA as substrates in acidic
CC conditions (pH 5.5) (PubMed:23620482, Ref.7, PubMed:25157844).
CC {ECO:0000269|PubMed:23620482, ECO:0000269|PubMed:25157844,
CC ECO:0000269|Ref.7};
CC -!- ACTIVITY REGULATION: ssDNase activity is inhibited by the divalent
CC cation chelator EDTA and the reducing agent DTT (PubMed:22506810).
CC Divalent metal ions (e.g. Ca(2+), Mg(2+) and Zn(2+)) and DTT represses
CC RNase activity (PubMed:22506810, PubMed:25157844). RNase activity is
CC enhanced by EDTA (PubMed:22506810). Also repressed by vanadate
CC (VO(4)(3-)) and phosphate (PO(4)(3-)) by occupying the active site
CC (PubMed:25157844). {ECO:0000269|PubMed:22506810,
CC ECO:0000269|PubMed:25157844}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.6 mM for ssDNA (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:22506810};
CC Note=kcat is 19171 min(-1) with ssDNA as substrate (at pH 7.0 and 37
CC degrees Celsius). {ECO:0000269|PubMed:22506810};
CC pH dependence:
CC Optimum pH is 7-8 with ssDNA as substrate (PubMed:22506810,
CC PubMed:23620482). Optimum pH is 6 with RNA as substrate
CC (PubMed:22506810). Optimum pH is 5.5 with dsDNA as substrate
CC (PubMed:23620482). {ECO:0000269|PubMed:22506810,
CC ECO:0000269|PubMed:23620482};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Low activity at
CC temperatures below 30 degrees Celsius. Above 70 degrees Celsius, the
CC catalytic activity declines. {ECO:0000269|PubMed:22506810};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- PTM: N-glycosylation is required for enzymatic stability and activity.
CC {ECO:0000269|PubMed:22506810}.
CC -!- BIOTECHNOLOGY: Can be applied to high-throughput detection of single
CC base mutation. {ECO:0000269|PubMed:22506810}.
CC -!- SIMILARITY: Belongs to the nuclease type I family. {ECO:0000305}.
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DR EMBL; AC016447; AAG52597.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34777.1; -; Genomic_DNA.
DR EMBL; AY086531; AAM63596.1; -; mRNA.
DR PIR; E96706; E96706.
DR RefSeq; NP_176996.1; NM_105500.2.
DR PDB; 3W52; X-ray; 1.76 A; A=28-290.
DR PDB; 4CWM; X-ray; 2.09 A; A/B=28-290.
DR PDB; 4CXO; X-ray; 1.67 A; A=28-290.
DR PDB; 4CXP; X-ray; 1.22 A; A=28-290.
DR PDB; 4CXV; X-ray; 2.00 A; A/B=28-290.
DR PDBsum; 3W52; -.
DR PDBsum; 4CWM; -.
DR PDBsum; 4CXO; -.
DR PDBsum; 4CXP; -.
DR PDBsum; 4CXV; -.
DR AlphaFoldDB; Q9C9G4; -.
DR SMR; Q9C9G4; -.
DR STRING; 3702.AT1G68290.1; -.
DR iPTMnet; Q9C9G4; -.
DR PaxDb; Q9C9G4; -.
DR PRIDE; Q9C9G4; -.
DR ProteomicsDB; 222715; -.
DR EnsemblPlants; AT1G68290.1; AT1G68290.1; AT1G68290.
DR GeneID; 843158; -.
DR Gramene; AT1G68290.1; AT1G68290.1; AT1G68290.
DR KEGG; ath:AT1G68290; -.
DR Araport; AT1G68290; -.
DR TAIR; locus:2199297; AT1G68290.
DR eggNOG; ENOG502QRXU; Eukaryota.
DR HOGENOM; CLU_044365_3_0_1; -.
DR InParanoid; Q9C9G4; -.
DR OMA; GYRLANW; -.
DR OrthoDB; 1114699at2759; -.
DR PhylomeDB; Q9C9G4; -.
DR BRENDA; 3.1.30.2; 399.
DR PRO; PR:Q9C9G4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9G4; baseline and differential.
DR Genevisible; Q9C9G4; AT.
DR GO; GO:0008309; F:double-stranded DNA exodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0043765; F:T/G mismatch-specific endonuclease activity; IDA:UniProtKB.
DR GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:UniProtKB.
DR CDD; cd11010; S1-P1_nuclease; 1.
DR Gene3D; 1.10.575.10; -; 1.
DR InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR InterPro; IPR003154; S1/P1nuclease.
DR PANTHER; PTHR33146; PTHR33146; 1.
DR Pfam; PF02265; S1-P1_nuclease; 1.
DR SUPFAM; SSF48537; SSF48537; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Endonuclease; Glycoprotein; Hydrolase; Manganese; Metal-binding; Nuclease;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:22506810"
FT CHAIN 28..282
FT /note="Endonuclease 2"
FT /id="PRO_0000417620"
FT PROPEP 283..290
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:23620482"
FT /id="PRO_0000445541"
FT REGION 147..196
FT /note="Substrate binding"
FT /evidence="ECO:0000269|PubMed:25157844,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXV"
FT BINDING 28..33
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25157844,
FT ECO:0007744|PDB:4CXV"
FT BINDING 28
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT BINDING 33
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT BINDING 72..76
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25157844,
FT ECO:0007744|PDB:4CXV"
FT BINDING 72
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25157844,
FT ECO:0007744|PDB:4CWM, ECO:0007744|PDB:4CXO,
FT ECO:0007744|PDB:4CXP, ECO:0007744|PDB:4CXV"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT BINDING 85
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT BINDING 94..99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25157844,
FT ECO:0007744|PDB:4CXO"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25157844,
FT ECO:0007744|PDB:4CXO"
FT BINDING 147
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT BINDING 181
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT BINDING 185
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT SITE 72
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P24021"
FT SITE 75
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT DISULFID 37..68
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:3W52"
FT DISULFID 93..245
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT DISULFID 101..111
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT DISULFID 226..232
FT /evidence="ECO:0000269|PubMed:25157844, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM,
FT ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP,
FT ECO:0007744|PDB:4CXV"
FT MUTAGEN 283..290
FT /note="Missing: Loss of activity."
FT /evidence="ECO:0000269|PubMed:23620482"
FT CONFLICT 224
FT /note="E -> D (in Ref. 3; AAM63596)"
FT /evidence="ECO:0000305"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:4CXP"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:4CXP"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4CXP"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:4CXP"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:4CXV"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4CXP"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4CXP"
FT TURN 164..168
FT /evidence="ECO:0007829|PDB:4CXP"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:4CXP"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:4CXP"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:4CXP"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3W52"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:4CXP"
FT HELIX 260..289
FT /evidence="ECO:0007829|PDB:4CXP"
SQ SEQUENCE 290 AA; 32745 MW; 1FA734DAA2AC5736 CRC64;
MANQKGLHVV MMIITVWLLY AAPNIHGWGK EGHEIICKIA QTRLDETAAK AVKELLPESA
EGDLSSLCLW ADRVKFRYHW SSPLHYINTP DACSYQYNRD CKDESGEKGR CVAGAIYNYT
TQLLSYKTAA SSQSQYNLTE ALLFVSHFMG DIHQPLHVSY ASDKGGNTIE VHWYTRKANL
HHIWDSNIIE TAEADLYNSA LEGMVDALKK NITTEWADQV KRWETCTKKT ACPDIYASEG
IQAACDWAYK GVTEGDTLED EYFYSRLPIV YQRLAQGGVR LAATLNRIFG
