TYDP2_MOUSE
ID TYDP2_MOUSE Reviewed; 370 AA.
AC Q9JJX7; A2RTH9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Tyrosyl-DNA phosphodiesterase 2;
DE Short=Tyr-DNA phosphodiesterase 2;
DE EC=3.1.4.- {ECO:0000269|PubMed:23104055, ECO:0000269|PubMed:24808172, ECO:0000269|PubMed:27060144, ECO:0000269|PubMed:27099339};
DE AltName: Full=5'-tyrosyl-DNA phosphodiesterase;
DE Short=5'-Tyr-DNA phosphodiesterase;
DE AltName: Full=TRAF and TNF receptor-associated protein;
GN Name=Tdp2; Synonyms=Ttrap;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10764746; DOI=10.1074/jbc.m000531200;
RA Pype S., Declercq W., Ibrahimi A., Michiels C., Van Rietschoten J.G.I.,
RA Dewulf N., de Boer M., Vandenabeele P., Huylebroeck D., Remacle J.E.;
RT "TTRAP, a novel protein that associates with CD40, tumor necrosis factor
RT (TNF) receptor-75 and TNF receptor-associated factors (TRAFs), and that
RT inhibits nuclear factor-kappa B activation.";
RL J. Biol. Chem. 275:18586-18593(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP FUNCTION.
RX PubMed=22740648; DOI=10.1093/nar/gks622;
RA Zeng Z., Sharma A., Ju L., Murai J., Umans L., Vermeire L., Pommier Y.,
RA Takeda S., Huylebroeck D., Caldecott K.W., El-Khamisy S.F.;
RT "TDP2 promotes repair of topoisomerase I-mediated DNA damage in the absence
RT of TDP1.";
RL Nucleic Acids Res. 40:8371-8380(2012).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=24658003; DOI=10.1038/ng.2929;
RA Gomez-Herreros F., Schuurs-Hoeijmakers J.H., McCormack M., Greally M.T.,
RA Rulten S., Romero-Granados R., Counihan T.J., Chaila E., Conroy J.,
RA Ennis S., Delanty N., Cortes-Ledesma F., de Brouwer A.P., Cavalleri G.L.,
RA El-Khamisy S.F., de Vries B.B., Caldecott K.W.;
RT "TDP2 protects transcription from abortive topoisomerase activity and is
RT required for normal neural function.";
RL Nat. Genet. 46:516-521(2014).
RN [7] {ECO:0007744|PDB:4GYZ, ECO:0007744|PDB:4GZ0, ECO:0007744|PDB:4GZ1, ECO:0007744|PDB:4GZ2}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 118-370 IN COMPLEXES WITH DNA;
RP AMP AND MAGNESIUM, CATALYTIC ACTIVITY, FUNCTION, AND COFACTOR.
RX PubMed=23104055; DOI=10.1038/nsmb.2418;
RA Schellenberg M.J., Appel C.D., Adhikari S., Robertson P.D., Ramsden D.A.,
RA Williams R.S.;
RT "Mechanism of repair of 5'-topoisomerase II-DNA adducts by mammalian
RT tyrosyl-DNA phosphodiesterase 2.";
RL Nat. Struct. Mol. Biol. 19:1363-1371(2012).
RN [8] {ECO:0007744|PDB:4PUQ}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 118-370 IN COMPLEX WITH DNA AND
RP MAGNESIUM, FUNCTION, COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=24808172; DOI=10.1074/jbc.m114.565374;
RA Gao R., Schellenberg M.J., Huang S.Y., Abdelmalak M., Marchand C.,
RA Nitiss K.C., Nitiss J.L., Williams R.S., Pommier Y.;
RT "Proteolytic degradation of topoisomerase II (Top2) enables the processing
RT of Top2DNA and Top2RNA covalent complexes by tyrosyl-DNA-phosphodiesterase
RT 2 (TDP2).";
RL J. Biol. Chem. 289:17960-17969(2014).
RN [9] {ECO:0007744|PDB:5J3Z, ECO:0007744|PDB:5J42}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 118-370 IN COMPLEXES WITH
RP MAGNESIUM AND MANGANESE, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=27099339; DOI=10.1042/bcj20160180;
RA Hornyak P., Askwith T., Walker S., Komulainen E., Paradowski M.,
RA Pennicott L.E., Bartlett E.J., Brissett N.C., Raoof A., Watson M.,
RA Jordan A.M., Ogilvie D.J., Ward S.E., Atack J.R., Pearl L.H.,
RA Caldecott K.W., Oliver A.W.;
RT "Mode of action of DNA-competitive small molecule inhibitors of tyrosyl DNA
RT phosphodiesterase 2.";
RL Biochem. J. 473:1869-1879(2016).
RN [10] {ECO:0007744|PDB:5HT2, ECO:0007744|PDB:5INK, ECO:0007744|PDB:5INL, ECO:0007744|PDB:5INM, ECO:0007744|PDB:5INN, ECO:0007744|PDB:5INP, ECO:0007744|PDB:5INQ}
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 118-370 IN COMPLEXES WITH DNA;
RP MAGNESIUM AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP MUTAGENESIS OF ASP-358.
RX PubMed=27060144; DOI=10.1093/nar/gkw228;
RA Schellenberg M.J., Perera L., Strom C.N., Waters C.A., Monian B.,
RA Appel C.D., Vilas C.K., Williams J.G., Ramsden D.A., Williams R.S.;
RT "Reversal of DNA damage induced Topoisomerase 2 DNA-protein crosslinks by
RT Tdp2.";
RL Nucleic Acids Res. 44:3829-3844(2016).
CC -!- FUNCTION: DNA repair enzyme that can remove a variety of covalent
CC adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving
CC rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-
CC end complexes between DNA and the topoisomerase 2 (TOP2) active site
CC tyrosine residue. The 5'-tyrosyl DNA phosphodiesterase activity can
CC enable the repair of TOP2-induced DNA double-strand breaks/DSBs without
CC the need for nuclease activity, creating a 'clean' DSB with 5'-
CC phosphate termini that are ready for ligation (PubMed:23104055,
CC PubMed:24808172, PubMed:27099339, PubMed:27060144). Thereby, protects
CC the transcription of many genes involved in neurological development
CC and maintenance from the abortive activity of TOP2 (PubMed:22740648).
CC Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DSBs due to
CC DNA damage by radiation and free radicals. Has preference for single-
CC stranded DNA or duplex DNA with a 4 base pair overhang as substrate.
CC Has also 3'-tyrosyl DNA phosphodiesterase activity, but less
CC efficiently and much slower than TDP1. Constitutes the major if not
CC only 5'-tyrosyl-DNA phosphodiesterase in cells. Also acts as an adapter
CC by participating in the specific activation of MAP3K7/TAK1 in response
CC to TGF-beta: associates with components of the TGF-beta receptor-TRAF6-
CC TAK1 signaling module and promotes their ubiquitination dependent
CC complex formation. Involved in non-canonical TGF-beta induced signaling
CC routes. May also act as a negative regulator of ETS1 and may inhibit
CC NF-kappa-B activation. Acts as a regulator of ribosome biogenesis
CC following stress (By similarity). {ECO:0000250|UniProtKB:O95551,
CC ECO:0000269|PubMed:22740648, ECO:0000269|PubMed:23104055,
CC ECO:0000269|PubMed:24808172, ECO:0000269|PubMed:27060144,
CC ECO:0000269|PubMed:27099339}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23104055, ECO:0000269|PubMed:24808172,
CC ECO:0000269|PubMed:27060144, ECO:0000269|PubMed:27099339};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23104055, ECO:0000269|PubMed:27060144};
CC Note=Binds 1 magnesium or manganese ion per subunit.
CC {ECO:0000269|PubMed:23104055, ECO:0000269|PubMed:24808172,
CC ECO:0000269|PubMed:27060144, ECO:0000269|PubMed:27099339};
CC -!- SUBUNIT: Interacts with TRAF2, TRAF3, TRAF5, TRAF6, TNFRSF8/CD30,
CC TNFRSF5/CD40, TNFRSF1B/TNF-R75, ETS1, ETS2, FLI1, SMAD3 and
CC ACVR1B/ALK4. {ECO:0000250|UniProtKB:O95551}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95551}. Nucleus,
CC PML body {ECO:0000250|UniProtKB:O95551}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O95551}. Cytoplasm
CC {ECO:0000250|UniProtKB:O95551}. Note=Localizes to nucleolar cavities
CC following stress; localization to nucleolus is dependent on PML
CC protein. {ECO:0000250|UniProtKB:O95551}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:10764746). Expressed in
CC whole brain, cerebellum, quiescent cortical astrocytes and cerebellar
CC granule neurons (PubMed:24658003). {ECO:0000269|PubMed:10764746,
CC ECO:0000269|PubMed:24658003}.
CC -!- PTM: Ubiquitinated by TRAF6. {ECO:0000250|UniProtKB:O95551}.
CC -!- MISCELLANEOUS: Can partially complement the absence of Tdp1 due to its
CC weak 3'-tyrosyl DNA phosphodiesterase activity.
CC {ECO:0000305|PubMed:22740648}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
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DR EMBL; AJ251328; CAB92971.1; -; mRNA.
DR EMBL; AL589699; CAI26084.1; -; Genomic_DNA.
DR EMBL; CH466561; EDL32475.1; -; Genomic_DNA.
DR EMBL; BC132511; AAI32512.1; -; mRNA.
DR EMBL; BC132513; AAI32514.1; -; mRNA.
DR CCDS; CCDS26381.1; -.
DR RefSeq; NP_062424.1; NM_019551.2.
DR PDB; 4GYZ; X-ray; 2.56 A; A/B/C/D/E/F/G/H/I=118-370.
DR PDB; 4GZ0; X-ray; 2.11 A; A/B/E/G/I/K=118-370.
DR PDB; 4GZ1; X-ray; 1.50 A; A/B=118-370.
DR PDB; 4GZ2; X-ray; 1.85 A; A/B=118-369.
DR PDB; 4PUQ; X-ray; 1.60 A; A/B=118-370.
DR PDB; 5HT2; X-ray; 1.43 A; A/B=118-370.
DR PDB; 5INK; X-ray; 2.15 A; A/B=118-370.
DR PDB; 5INL; X-ray; 1.55 A; A/B=118-370.
DR PDB; 5INM; X-ray; 2.40 A; A/B/C/D/E=118-370.
DR PDB; 5INN; X-ray; 2.80 A; A/B/C/D/E=118-370.
DR PDB; 5INP; X-ray; 1.95 A; A/B=118-370.
DR PDB; 5INQ; X-ray; 1.85 A; A/B=118-370.
DR PDB; 5J3Z; X-ray; 1.80 A; A/B=118-370.
DR PDB; 5J42; X-ray; 1.70 A; A/B=118-370.
DR PDB; 5TVP; X-ray; 2.40 A; A/B/E/G/I/K/M/O=118-370.
DR PDB; 5TVQ; X-ray; 2.35 A; A=118-370.
DR PDBsum; 4GYZ; -.
DR PDBsum; 4GZ0; -.
DR PDBsum; 4GZ1; -.
DR PDBsum; 4GZ2; -.
DR PDBsum; 4PUQ; -.
DR PDBsum; 5HT2; -.
DR PDBsum; 5INK; -.
DR PDBsum; 5INL; -.
DR PDBsum; 5INM; -.
DR PDBsum; 5INN; -.
DR PDBsum; 5INP; -.
DR PDBsum; 5INQ; -.
DR PDBsum; 5J3Z; -.
DR PDBsum; 5J42; -.
DR PDBsum; 5TVP; -.
DR PDBsum; 5TVQ; -.
DR AlphaFoldDB; Q9JJX7; -.
DR SMR; Q9JJX7; -.
DR BioGRID; 207835; 2.
DR STRING; 10090.ENSMUSP00000035660; -.
DR BindingDB; Q9JJX7; -.
DR ChEMBL; CHEMBL3813588; -.
DR iPTMnet; Q9JJX7; -.
DR PhosphoSitePlus; Q9JJX7; -.
DR EPD; Q9JJX7; -.
DR MaxQB; Q9JJX7; -.
DR PaxDb; Q9JJX7; -.
DR PeptideAtlas; Q9JJX7; -.
DR PRIDE; Q9JJX7; -.
DR ProteomicsDB; 298400; -.
DR Antibodypedia; 10651; 309 antibodies from 33 providers.
DR DNASU; 56196; -.
DR Ensembl; ENSMUST00000038039; ENSMUSP00000035660; ENSMUSG00000035958.
DR GeneID; 56196; -.
DR KEGG; mmu:56196; -.
DR UCSC; uc007pwl.2; mouse.
DR CTD; 51567; -.
DR MGI; MGI:1860486; Tdp2.
DR VEuPathDB; HostDB:ENSMUSG00000035958; -.
DR eggNOG; KOG2756; Eukaryota.
DR GeneTree; ENSGT00390000014242; -.
DR HOGENOM; CLU_047318_0_0_1; -.
DR InParanoid; Q9JJX7; -.
DR OMA; AENDWDM; -.
DR OrthoDB; 1612152at2759; -.
DR PhylomeDB; Q9JJX7; -.
DR TreeFam; TF314813; -.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR BioGRID-ORCS; 56196; 6 hits in 108 CRISPR screens.
DR ChiTaRS; Tdp2; mouse.
DR PRO; PR:Q9JJX7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JJX7; protein.
DR Bgee; ENSMUSG00000035958; Expressed in otic placode and 260 other tissues.
DR ExpressionAtlas; Q9JJX7; baseline and differential.
DR Genevisible; Q9JJX7; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0070260; F:5'-tyrosyl-DNA phosphodiesterase activity; ISS:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; ISA:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; ISA:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0036317; F:tyrosyl-RNA phosphodiesterase activity; ISO:MGI.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; DNA damage; DNA repair; Hydrolase;
KW Isopeptide bond; Magnesium; Metal-binding; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..370
FT /note="Tyrosyl-DNA phosphodiesterase 2"
FT /id="PRO_0000065679"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..134
FT /note="Interaction with 5' end of substrate DNA"
FT /evidence="ECO:0000269|PubMed:23104055,
FT ECO:0000269|PubMed:27060144"
FT REGION 236..241
FT /note="Interaction with 5' end of substrate DNA"
FT /evidence="ECO:0000269|PubMed:23104055,
FT ECO:0000269|PubMed:24808172, ECO:0000269|PubMed:27060144"
FT REGION 274..276
FT /note="Interaction with 5' end of substrate DNA"
FT /evidence="ECO:0000269|PubMed:23104055,
FT ECO:0000269|PubMed:24808172, ECO:0000269|PubMed:27060144"
FT REGION 315..321
FT /note="Interaction with 5' end of substrate DNA"
FT /evidence="ECO:0000269|PubMed:23104055,
FT ECO:0000269|PubMed:24808172, ECO:0000269|PubMed:27060144"
FT ACT_SITE 272
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:23104055,
FT ECO:0000305|PubMed:27060144"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:23104055,
FT ECO:0000269|PubMed:27099339, ECO:0007744|PDB:4GYZ,
FT ECO:0007744|PDB:4GZ2, ECO:0007744|PDB:5J42"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:23104055,
FT ECO:0000269|PubMed:24808172, ECO:0000269|PubMed:27099339,
FT ECO:0007744|PDB:4GYZ, ECO:0007744|PDB:4GZ1,
FT ECO:0007744|PDB:4GZ2, ECO:0007744|PDB:4PUQ,
FT ECO:0007744|PDB:5HT2, ECO:0007744|PDB:5INP,
FT ECO:0007744|PDB:5J42"
FT SITE 188
FT /note="Interaction with 5' end of substrate DNA"
FT /evidence="ECO:0000269|PubMed:23104055,
FT ECO:0000269|PubMed:27060144"
FT SITE 307
FT /note="Interaction with 5' end of substrate DNA"
FT /evidence="ECO:0000269|PubMed:23104055,
FT ECO:0000269|PubMed:24808172, ECO:0000269|PubMed:27060144"
FT SITE 325
FT /note="Interaction with 5' end of substrate DNA"
FT /evidence="ECO:0000269|PubMed:23104055"
FT SITE 359
FT /note="Interaction with 5' end of substrate DNA"
FT /evidence="ECO:0000269|PubMed:23104055,
FT ECO:0000269|PubMed:24808172, ECO:0000269|PubMed:27060144"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O95551"
FT MOD_RES 99
FT /note="Phosphothreonine; by ACVR1B"
FT /evidence="ECO:0000250|UniProtKB:O95551"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95551"
FT MUTAGEN 358
FT /note="D->N: Loss of magnesium binding."
FT /evidence="ECO:0000269|PubMed:27060144"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:5HT2"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:5HT2"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:5HT2"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:5TVQ"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 185..195
FT /evidence="ECO:0007829|PDB:5HT2"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:5HT2"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:5HT2"
FT HELIX 244..260
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:5HT2"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:5HT2"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:5HT2"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:5HT2"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:4PUQ"
FT STRAND 336..345
FT /evidence="ECO:0007829|PDB:5HT2"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:5HT2"
SQ SEQUENCE 370 AA; 41034 MW; A773A8889DF5BE83 CRC64;
MASGSSSDAA EPAGPAGRAA SAPEAAQAEE DRVKRRRLQC LGFALVGGCD PTMVPSVLRE
NDWQTQKALS AYFELPENDQ GWPRQPPTSF KSEAYVDLTN EDANDTTILE ASPSGTPLED
SSTISFITWN IDGLDGCNLP ERARGVCSCL ALYSPDVVFL QEVIPPYCAY LKKRAASYTI
ITGNEEGYFT AILLKKGRVK FKSQEIIPFP NTKMMRNLLC VNVSLGGNEF CLMTSHLEST
REHSAERIRQ LKTVLGKMQE APDSTTVIFA GDTNLRDQEV IKCGGLPDNV FDAWEFLGKP
KHCQYTWDTK ANNNLRIPAA YKHRFDRIFF RAEEGHLIPQ SLDLVGLEKL DCGRFPSDHW
GLLCTLNVVL
