TADBP_MOUSE
ID TADBP_MOUSE Reviewed; 414 AA.
AC Q921F2; Q3U591; Q3V0E7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=TAR DNA-binding protein 43;
DE Short=TDP-43;
GN Name=Tardbp; Synonyms=Tdp43;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 PROTEIN SEQUENCE OF 276-293, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [5]
RP INTERACTION WITH BRDT.
RX PubMed=22570411; DOI=10.1093/nar/gks342;
RA Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.;
RT "The testis-specific double bromodomain-containing protein BRDT forms a
RT complex with multiple spliceosome components and is required for mRNA
RT splicing and 3'-UTR truncation in round spermatids.";
RL Nucleic Acids Res. 40:7162-7175(2012).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=23449777; DOI=10.1093/brain/awt029;
RA Iguchi Y., Katsuno M., Niwa J., Takagi S., Ishigaki S., Ikenaka K.,
RA Kawai K., Watanabe H., Yamanaka K., Takahashi R., Misawa H., Sasaki S.,
RA Tanaka F., Sobue G.;
RT "Loss of TDP-43 causes age-dependent progressive motor neuron
RT degeneration.";
RL Brain 136:1371-1382(2013).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-293, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [8]
RP FUNCTION, AND INTERACTION WITH PPIA.
RX PubMed=25678563; DOI=10.1093/brain/awv005;
RA Lauranzano E., Pozzi S., Pasetto L., Stucchi R., Massignan T., Paolella K.,
RA Mombrini M., Nardo G., Lunetta C., Corbo M., Mora G., Bendotti C.,
RA Bonetto V.;
RT "Peptidylprolyl isomerase A governs TARDBP function and assembly in
RT heterogeneous nuclear ribonucleoprotein complexes.";
RL Brain 138:974-991(2015).
RN [9]
RP FUNCTION, AND INTERACTION WITH CRY2.
RX PubMed=27123980; DOI=10.1371/journal.pone.0154263;
RA Hirano A., Nakagawa T., Yoshitane H., Oyama M., Kozuka-Hata H.,
RA Lanjakornsiripan D., Fukada Y.;
RT "USP7 and TDP-43: pleiotropic regulation of cryptochrome protein stability
RT paces the oscillation of the mammalian circadian clock.";
RL PLoS ONE 11:E0154263-E0154263(2016).
RN [10]
RP INTERACTION WITH ZNF106, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28072389; DOI=10.7554/elife.19032;
RA Celona B., Dollen J.V., Vatsavayai S.C., Kashima R., Johnson J.R.,
RA Tang A.A., Hata A., Miller B.L., Huang E.J., Krogan N.J., Seeley W.W.,
RA Black B.L.;
RT "Suppression of C9orf72 RNA repeat-induced neurotoxicity by the ALS-
RT associated RNA-binding protein Zfp106.";
RL Elife 6:0-0(2017).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30464263; DOI=10.1038/s41586-018-0665-2;
RA Vogler T.O., Wheeler J.R., Nguyen E.D., Hughes M.P., Britson K.A.,
RA Lester E., Rao B., Betta N.D., Whitney O.N., Ewachiw T.E., Gomes E.,
RA Shorter J., Lloyd T.E., Eisenberg D.S., Taylor J.P., Johnson A.M.,
RA Olwin B.B., Parker R.;
RT "TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle.";
RL Nature 563:508-513(2018).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 192-265 IN COMPLEX WITH
RP SINGLE-STRANDED DNA, AND SUBUNIT.
RX PubMed=19174564; DOI=10.1093/nar/gkp013;
RA Kuo P.H., Doudeva L.G., Wang Y.T., Shen C.K., Yuan H.S.;
RT "Structural insights into TDP-43 in nucleic-acid binding and domain
RT interactions.";
RL Nucleic Acids Res. 37:1799-1808(2009).
CC -!- FUNCTION: RNA-binding protein that is involved in various steps of RNA
CC biogenesis and processing. Preferentially binds, via its two RNA
CC recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules
CC predominantly localized within long introns and in the 3'UTR of mRNAs.
CC In turn, regulates the splicing of many non-coding and protein-coding
CC RNAs including proteins involved in neuronal survival, as well as mRNAs
CC that encode proteins relevant for neurodegenerative diseases. Plays a
CC role in maintaining mitochondrial homeostasis by regulating the
CC processing of mitochondrial transcripts. Regulates also mRNA stability
CC by recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A)
CC tail deadenylation and thus shortening. In response to oxidative
CC insult, associates with stalled ribosomes localized to stress granules
CC (SGs) and contributes to cell survival (By similarity). Participates
CC also in the normal skeletal muscle formation and regeneration, forming
CC cytoplasmic myo-granules and binding mRNAs that encode sarcomeric
CC proteins (PubMed:30464263). Plays a role in the maintenance of the
CC circadian clock periodicity via stabilization of the CRY1 and CRY2
CC proteins in a FBXL3-dependent manner (PubMed:27123980). Negatively
CC regulates the expression of CDK6 (By similarity). Regulates the
CC expression of HDAC6, ATG7 and VCP in a PPIA/CYPA-dependent manner
CC (PubMed:25678563). {ECO:0000250|UniProtKB:Q13148,
CC ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:27123980,
CC ECO:0000269|PubMed:30464263}.
CC -!- SUBUNIT: Homodimer. Homooligomer (via its N-terminal domain) (By
CC similarity). Interacts with BRDT (PubMed:22570411). Binds specifically
CC to pyrimidine-rich motifs of TAR DNA and to single stranded TG repeated
CC sequences. Binds to RNA, specifically to UG repeated sequences with a
CC minimum of six contiguous repeats. Interacts with ATXN2; the
CC interaction is RNA-dependent. Interacts with MATR3. Interacts with
CC UBQLN2. Interacts with HNRNPA2B1 (By similarity). Interacts with ZNF106
CC (PubMed:28072389). Interacts with CNOT7/CAF1 (By similarity). Interacts
CC with CRY2 (PubMed:27123980). Interacts with PPIA/CYPA; the interaction
CC is dependent on RNA-binding activity of TARDBP and PPIase activity of
CC PPIA/CYPA (PubMed:25678563). Acetylation of PPIA/CYPA at 'Lys-125'
CC favors the interaction of TARDBP with PPIA/CYPA (By similarity).
CC {ECO:0000250|UniProtKB:Q13148, ECO:0000269|PubMed:22570411,
CC ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:27123980,
CC ECO:0000269|PubMed:28072389}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13148}. Cytoplasm
CC {ECO:0000269|PubMed:30464263}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q13148}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q13148}. Note=Continuously travels in and out of
CC the nucleus. Localizes to stress granules in response to oxidative
CC stress. A small subset localizes in mitochondria.
CC {ECO:0000250|UniProtKB:Q13148}.
CC -!- DOMAIN: The RRM domains can bind to both DNA and RNA.
CC -!- PTM: Hyperphosphorylated. {ECO:0000250|UniProtKB:Q13148}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q13148}.
CC -!- DISRUPTION PHENOTYPE: TARDBP depletion leads to atrophy of spinal motor
CC neurons. Affects motor axon, neuromuscular junction and skeletal
CC muscle. {ECO:0000269|PubMed:23449777}.
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DR EMBL; AK133207; BAE21557.1; -; mRNA.
DR EMBL; AK153803; BAE32189.1; -; mRNA.
DR EMBL; BC012873; AAH12873.1; -; mRNA.
DR EMBL; BC025544; AAH25544.1; -; mRNA.
DR EMBL; BC027772; AAH27772.1; -; mRNA.
DR EMBL; BC031126; AAH31126.1; -; mRNA.
DR EMBL; BC033475; AAH33475.1; -; mRNA.
DR CCDS; CCDS38971.1; -.
DR RefSeq; NP_001003899.1; NM_001003899.2.
DR RefSeq; NP_001008545.1; NM_001008545.2.
DR RefSeq; NP_001008546.1; NM_001008546.2.
DR RefSeq; NP_001292354.1; NM_001305425.1.
DR RefSeq; NP_663531.1; NM_145556.4.
DR PDB; 3D2W; X-ray; 1.65 A; A=192-265.
DR PDBsum; 3D2W; -.
DR AlphaFoldDB; Q921F2; -.
DR BMRB; Q921F2; -.
DR SMR; Q921F2; -.
DR BioGRID; 231054; 77.
DR CORUM; Q921F2; -.
DR IntAct; Q921F2; 16.
DR MINT; Q921F2; -.
DR STRING; 10090.ENSMUSP00000081142; -.
DR iPTMnet; Q921F2; -.
DR PhosphoSitePlus; Q921F2; -.
DR SwissPalm; Q921F2; -.
DR REPRODUCTION-2DPAGE; Q921F2; -.
DR EPD; Q921F2; -.
DR jPOST; Q921F2; -.
DR MaxQB; Q921F2; -.
DR PaxDb; Q921F2; -.
DR PRIDE; Q921F2; -.
DR ProteomicsDB; 254644; -.
DR TopDownProteomics; Q921F2; -.
DR Antibodypedia; 1854; 958 antibodies from 47 providers.
DR DNASU; 230908; -.
DR Ensembl; ENSMUST00000084125; ENSMUSP00000081142; ENSMUSG00000041459.
DR GeneID; 230908; -.
DR KEGG; mmu:230908; -.
DR UCSC; uc008vvg.1; mouse.
DR CTD; 23435; -.
DR MGI; MGI:2387629; Tardbp.
DR VEuPathDB; HostDB:ENSMUSG00000041459; -.
DR eggNOG; ENOG502QPQ8; Eukaryota.
DR GeneTree; ENSGT00940000154343; -.
DR HOGENOM; CLU_012062_6_1_1; -.
DR InParanoid; Q921F2; -.
DR OMA; WGSASNP; -.
DR OrthoDB; 1425837at2759; -.
DR PhylomeDB; Q921F2; -.
DR TreeFam; TF315657; -.
DR BioGRID-ORCS; 230908; 30 hits in 76 CRISPR screens.
DR ChiTaRS; Tardbp; mouse.
DR EvolutionaryTrace; Q921F2; -.
DR PRO; PR:Q921F2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q921F2; protein.
DR Bgee; ENSMUSG00000041459; Expressed in presomitic mesoderm and 266 other tissues.
DR ExpressionAtlas; Q921F2; baseline and differential.
DR Genevisible; Q921F2; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0035061; C:interchromatin granule; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005726; C:perichromatin fibrils; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISO:MGI.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISO:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0071765; P:nuclear inner membrane organization; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IMP:MGI.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR041105; TDP43_N.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF18694; TDP43_N; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Biological rhythms; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Methylation; Mitochondrion; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..414
FT /note="TAR DNA-binding protein 43"
FT /id="PRO_0000081973"
FT DOMAIN 104..200
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 191..262
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 216..414
FT /note="Interaction with UBQLN2"
FT /evidence="ECO:0000250|UniProtKB:Q13148"
FT REGION 261..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13148"
FT MOD_RES 293
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13148"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13148"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13148"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13148"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13148"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13148"
FT CONFLICT 8
FT /note="T -> K (in Ref. 1; BAE32189)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="V -> G (in Ref. 1; BAE32189)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="G -> C (in Ref. 1; BAE21557)"
FT /evidence="ECO:0000305"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:3D2W"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:3D2W"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:3D2W"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:3D2W"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:3D2W"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:3D2W"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:3D2W"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:3D2W"
SQ SEQUENCE 414 AA; 44548 MW; 2BE6A695EC2CA106 CRC64;
MSEYIRVTED ENDEPIEIPS EDDGTVLLST VTAQFPGACG LRYRNPVSQC MRGVRLVEGI
LHAPDAGWGN LVYVVNYPKD NKRKMDETDA SSAVKVKRAV QKTSDLIVLG LPWKTTEQDL
KDYFSTFGEV LMVQVKKDLK TGHSKGFGFV RFTEYETQVK VMSQRHMIDG RWCDCKLPNS
KQSPDEPLRS RKVFVGRCTE DMTAEELQQF FCQYGEVVDV FIPKPFRAFA FVTFADDKVA
QSLCGEDLII KGISVHISNA EPKHNSNRQL ERSGRFGGNP GGFGNQGGFG NSRGGGAGLG
NNQGGNMGGG MNFGAFSINP AMMAAAQAAL QSSWGMMGML ASQQNQSGPS GNNQSQGSMQ
REPNQAFGSG NNSYSGSNSG APLGWGSASN AGSGSGFNGG FGSSMDSKSS GWGM
