DXO_MOUSE
ID DXO_MOUSE Reviewed; 397 AA.
AC O70348; Q99KD8;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Decapping and exoribonuclease protein {ECO:0000303|PubMed:23523372};
DE Short=DXO {ECO:0000303|PubMed:23523372};
DE EC=3.6.1.- {ECO:0000269|PubMed:23523372};
DE AltName: Full=5'-3' exoribonuclease DXO {ECO:0000305};
DE EC=3.1.13.- {ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:30180947};
DE AltName: Full=Dom-3 homolog Z {ECO:0000303|PubMed:14656967};
DE AltName: Full=NAD-capped RNA hydrolase DXO {ECO:0000305};
DE Short=DeNADding enzyme DXO {ECO:0000305};
DE EC=3.6.1.- {ECO:0000269|PubMed:28283058};
GN Name=Dxo {ECO:0000303|PubMed:23523372};
GN Synonyms=Dom3z {ECO:0000303|PubMed:14656967}, Ng6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32432673; DOI=10.1093/nar/gkaa402;
RA Sharma S., Grudzien-Nogalska E., Hamilton K., Jiao X., Yang J., Tong L.,
RA Kiledjian M.;
RT "Mammalian Nudix proteins cleave nucleotide metabolite caps on RNAs.";
RL Nucleic Acids Res. 48:6788-6798(2020).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH GDP.
RX PubMed=19194460; DOI=10.1038/nature07731;
RA Xiang S., Cooper-Morgan A., Jiao X., Kiledjian M., Manley J.L., Tong L.;
RT "Structure and function of the 5'-->3' exoribonuclease Rat1 and its
RT activating partner Rai1.";
RL Nature 458:784-788(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 27-397 IN COMPLEX WITH MAGNESIUM
RP AND M(7)GPPPG CAP, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF GLU-234 AND ASP-236.
RX PubMed=23523372; DOI=10.1016/j.molcel.2013.02.017;
RA Jiao X., Chang J.H., Kilic T., Tong L., Kiledjian M.;
RT "A mammalian pre-mRNA 5' end capping quality control mechanism and an
RT unexpected link of capping to pre-mRNA processing.";
RL Mol. Cell 50:104-115(2013).
RN [7] {ECO:0007744|PDB:5ULI}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-384 IN COMPLEX WITH CALCIUM,
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-234 AND ASP-236.
RX PubMed=28283058; DOI=10.1016/j.cell.2017.02.019;
RA Jiao X., Doamekpor S.K., Bird J.G., Nickels B.E., Tong L., Hart R.P.,
RA Kiledjian M.;
RT "5' end nicotinamide adenine dinucleotide cap in human cells promotes RNA
RT decay through DXO-mediated deNADding.";
RL Cell 168:1015-1027(2017).
RN [8] {ECO:0007744|PDB:6AIX, ECO:0007744|PDB:6AIY}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 27-384 IN COMPLEX WITH MAGNESIUM
RP AND ADENOSINE 3',5'-BISPHOSPHATE, FUNCTION, ACTIVITY REGULATION, COFACTOR,
RP AND MUTAGENESIS OF GLU-234.
RX PubMed=30180947; DOI=10.1016/j.bbrc.2018.08.135;
RA Yun J.S., Yoon J.H., Choi Y.J., Son Y.J., Kim S., Tong L., Chang J.H.;
RT "Molecular mechanism for the inhibition of DXO by adenosine 3',5'-
RT bisphosphate.";
RL Biochem. Biophys. Res. Commun. 504:89-95(2018).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF IN COMPLEX WITH COA AND 3'-FADP,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32374864; DOI=10.1093/nar/gkaa297;
RA Doamekpor S.K., Grudzien-Nogalska E., Mlynarska-Cieslak A., Kowalska J.,
RA Kiledjian M., Tong L.;
RT "DXO/Rai1 enzymes remove 5'-end FAD and dephospho-CoA caps on RNAs.";
RL Nucleic Acids Res. 48:6136-6148(2020).
CC -!- FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes
CC the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs
CC by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA
CC (PubMed:28283058, PubMed:32374864). The NAD-cap is present at the 5'-
CC end of some RNAs and snoRNAs (PubMed:28283058). In contrast to the
CC canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes
CC mRNA decay (PubMed:28283058). Preferentially acts on NAD-capped
CC transcripts in response to environmental stress (By similarity). Also
CC acts as a non-canonical decapping enzyme that removes the entire cap
CC structure of m7G capped or incompletely capped RNAs and mediates their
CC subsequent degradation (PubMed:23523372, PubMed:28283058). Specifically
CC degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a
CC pre-mRNA capping quality control (PubMed:23523372). Has decapping
CC activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated
CC 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose
CC methylated m7G cap (cap1) (PubMed:23523372). In contrast to canonical
CC decapping enzymes DCP2 and NUDT16, which cleave the cap within the
CC triphosphate linkage, the decapping activity releases the entire cap
CC structure GpppN and a 5'-end monophosphate RNA (PubMed:23523372). Also
CC has 5'-3' exoribonuclease activities: The 5'-end monophosphate RNA is
CC then degraded by the 5'-3' exoribonuclease activity, enabling this
CC enzyme to decap and degrade incompletely capped mRNAs (PubMed:23523372,
CC PubMed:30180947). Also possesses RNA 5'-pyrophosphohydrolase activity
CC by hydrolyzing the 5'-end triphosphate to release pyrophosphates
CC (PubMed:23523372). Exhibits decapping activity towards FAD-capped RNAs
CC (PubMed:32432673, PubMed:32374864). Exhibits decapping activity towards
CC dpCoA-capped RNAs in vitro (PubMed:32432673, PubMed:32374864).
CC {ECO:0000250|UniProtKB:O77932, ECO:0000269|PubMed:23523372,
CC ECO:0000269|PubMed:28283058, ECO:0000269|PubMed:30180947,
CC ECO:0000269|PubMed:32374864, ECO:0000269|PubMed:32432673}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC end phospho-ribonucleoside in mRNA + H(+) + NAD(+);
CC Xref=Rhea:RHEA:60880, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:15698,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:144029;
CC Evidence={ECO:0000269|PubMed:28283058, ECO:0000269|PubMed:32374864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60881;
CC Evidence={ECO:0000269|PubMed:28283058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in snoRNA + H2O = a 5'-
CC end phospho-ribonucleoside in snoRNA + H(+) + NAD(+);
CC Xref=Rhea:RHEA:60892, Rhea:RHEA-COMP:15699, Rhea:RHEA-COMP:15700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:144029;
CC Evidence={ECO:0000269|PubMed:28283058};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60893;
CC Evidence={ECO:0000269|PubMed:28283058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside-
CC ribonucleotide in mRNA + H2O = a (N(7)-methyl 5'-triphospho-
CC guanosine)-nucleoside + a 5'-end phospho-ribonucleoside in mRNA +
CC H(+); Xref=Rhea:RHEA:66928, Rhea:RHEA-COMP:15692, Rhea:RHEA-
CC COMP:17313, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:138282,
CC ChEBI:CHEBI:172876, ChEBI:CHEBI:172877;
CC Evidence={ECO:0000269|PubMed:23523372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66929;
CC Evidence={ECO:0000269|PubMed:23523372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end
CC phospho-ribonucleoside in mRNA + FAD + H(+); Xref=Rhea:RHEA:67492,
CC Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17275, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:138282,
CC ChEBI:CHEBI:172372; Evidence={ECO:0000269|PubMed:32374864,
CC ECO:0000269|PubMed:32432673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67493;
CC Evidence={ECO:0000305|PubMed:32432673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = 3'-dephospho-CoA +
CC a 5'-end phospho-ribonucleoside in mRNA + H(+); Xref=Rhea:RHEA:67496,
CC Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57328, ChEBI:CHEBI:138282,
CC ChEBI:CHEBI:172371; Evidence={ECO:0000305|PubMed:32374864,
CC ECO:0000305|PubMed:32432673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67497;
CC Evidence={ECO:0000305|PubMed:32432673};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:30180947};
CC Note=Binds 2 magnesium ions. {ECO:0000269|PubMed:23523372,
CC ECO:0000269|PubMed:30180947};
CC -!- ACTIVITY REGULATION: The 5'-3' exoribonuclease activity is inhibited by
CC adenosine 3',5'-bisphosphate. {ECO:0000269|PubMed:30180947}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O77932}.
CC -!- SIMILARITY: Belongs to the DXO/Dom3Z family. {ECO:0000305}.
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DR EMBL; AF049850; AAC05281.1; -; Genomic_DNA.
DR EMBL; BC004713; AAH04713.1; -; mRNA.
DR CCDS; CCDS28660.1; -.
DR RefSeq; NP_001157242.1; NM_001163770.1.
DR RefSeq; NP_291091.2; NM_033613.2.
DR PDB; 3FQI; X-ray; 2.01 A; A=1-397.
DR PDB; 3FQJ; X-ray; 2.62 A; A=1-397.
DR PDB; 4J7L; X-ray; 1.80 A; A=27-384.
DR PDB; 4J7M; X-ray; 1.70 A; A=27-384.
DR PDB; 4J7N; X-ray; 1.50 A; A=27-384.
DR PDB; 5ULI; X-ray; 2.10 A; A=27-384.
DR PDB; 6AIX; X-ray; 1.80 A; A=27-384.
DR PDB; 6AIY; X-ray; 1.90 A; A=27-384.
DR PDB; 6WRE; X-ray; 2.00 A; A=27-384.
DR PDB; 6WUF; X-ray; 1.60 A; A=1-397.
DR PDB; 6WUK; X-ray; 1.60 A; A=1-397.
DR PDBsum; 3FQI; -.
DR PDBsum; 3FQJ; -.
DR PDBsum; 4J7L; -.
DR PDBsum; 4J7M; -.
DR PDBsum; 4J7N; -.
DR PDBsum; 5ULI; -.
DR PDBsum; 6AIX; -.
DR PDBsum; 6AIY; -.
DR PDBsum; 6WRE; -.
DR PDBsum; 6WUF; -.
DR PDBsum; 6WUK; -.
DR AlphaFoldDB; O70348; -.
DR SMR; O70348; -.
DR STRING; 10090.ENSMUSP00000047018; -.
DR iPTMnet; O70348; -.
DR PhosphoSitePlus; O70348; -.
DR EPD; O70348; -.
DR MaxQB; O70348; -.
DR PaxDb; O70348; -.
DR PRIDE; O70348; -.
DR ProteomicsDB; 277793; -.
DR GeneID; 112403; -.
DR KEGG; mmu:112403; -.
DR UCSC; uc008cdr.2; mouse.
DR CTD; 1797; -.
DR MGI; MGI:1890444; Dxo.
DR eggNOG; KOG1982; Eukaryota.
DR InParanoid; O70348; -.
DR OrthoDB; 1034620at2759; -.
DR PhylomeDB; O70348; -.
DR TreeFam; TF322812; -.
DR BioGRID-ORCS; 112403; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Dxo; mouse.
DR EvolutionaryTrace; O70348; -.
DR PRO; PR:O70348; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70348; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0110152; F:RNA NAD-cap (NAD-forming) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0034353; F:RNA pyrophosphohydrolase activity; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0110155; P:NAD-cap decapping; IDA:UniProtKB.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:UniProtKB.
DR GO; GO:0050779; P:RNA destabilization; IMP:UniProtKB.
DR InterPro; IPR013961; RAI1.
DR InterPro; IPR039039; RAI1-like_fam.
DR PANTHER; PTHR12395; PTHR12395; 1.
DR Pfam; PF08652; RAI1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..397
FT /note="Decapping and exoribonuclease protein"
FT /id="PRO_0000249823"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..256
FT /note="Adenosine 3',5'-bisphosphate; inhibitor"
FT /evidence="ECO:0000269|PubMed:30180947"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:28283058"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23523372"
FT BINDING 131..133
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:28283058"
FT BINDING 185
FT /ligand="adenosine 3',5'-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58343"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:30180947"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23523372"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23523372"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23523372"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:30180947"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:28283058"
FT BINDING 236
FT /ligand="adenosine 3',5'-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58343"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:30180947"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:30180947, ECO:0000305|PubMed:28283058"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:30180947"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:30180947, ECO:0000305|PubMed:28283058"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:30180947, ECO:0000305|PubMed:28283058"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:28283058"
FT BINDING 280
FT /ligand="adenosine 3',5'-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58343"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:30180947"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:28283058"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6MG77"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 234
FT /note="E->A: Abolishes the decapping activity on both
FT incomplete m7G cap and NAD-cap RNAs. Abolishes the 5'-3'
FT exoribonuclease activity."
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:28283058, ECO:0000269|PubMed:30180947"
FT MUTAGEN 236
FT /note="D->A: Abolishes the decapping activity on both
FT incomplete m7G cap and NAD-cap RNAs."
FT /evidence="ECO:0000269|PubMed:23523372,
FT ECO:0000269|PubMed:28283058"
FT CONFLICT 20
FT /note="N -> H (in Ref. 1; AAC05281)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="S -> L (in Ref. 1; AAC05281)"
FT /evidence="ECO:0000305"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6WUK"
FT TURN 84..91
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3FQJ"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:4J7N"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6AIY"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:4J7N"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4J7N"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:4J7N"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:4J7N"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:4J7N"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6WUK"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:4J7N"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:4J7N"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:4J7N"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 298..307
FT /evidence="ECO:0007829|PDB:4J7N"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:4J7N"
FT HELIX 324..341
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:4J7N"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:4J7N"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:4J7N"
FT HELIX 376..383
FT /evidence="ECO:0007829|PDB:4J7N"
SQ SEQUENCE 397 AA; 45280 MW; 02022DF0A77D503E CRC64;
MEPRGTKRKA EKTEVEKPLN KLPRAVPSLR TQPSLYSGPF PFYRRPSELG CFSLDAQRQY
HGDARALRYY SPPPINGPGP DFDLRDGYPD RYQPRDEEVQ ERLDHLLRWV LEHRNQLEGG
PGWLAGATVT WRGHLTKLLT TPYERQEGWQ LAASRFQGTL YLSEVETPAA RAQRLARPPL
LRELMYMGYK FEQYMCADKP GGSPDPSGEV NTNVAYCSVL RSRLGNHPLL FSGEVDCLNP
QAPCTQPPSC YVELKTSKEM HSPGQWRSFY RHKLLKWWAQ SFLPGVPHVV AGFRNPEGFV
CSLKTFPTME MFENVRNDRE GWNPSVCMNF CAAFLSFAQS TVVQDDPRLV HLFSWEPGGP
VTVSVHRDAP YAFLPSWYVE TMTQDLPPLS KTPSPKD
