MBTD1_HUMAN
ID MBTD1_HUMAN Reviewed; 628 AA.
AC Q05BQ5; Q6ZVU7; Q9NXU1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=MBT domain-containing protein 1 {ECO:0000305};
GN Name=MBTD1 {ECO:0000303|PubMed:23915195, ECO:0000312|HGNC:HGNC:19866};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Colon, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-577 (ISOFORM 1).
RC TISSUE=Eye;
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 CHROMOSOMAL TRANSLOCATION WITH ZMYND11.
RX PubMed=23915195; DOI=10.3109/10428194.2013.820292;
RA De Braekeleer E., Auffret R., Douet-Guilbert N., Basinko A., Le Bris M.J.,
RA Morel F., De Braekeleer M.;
RT "Recurrent translocation (10;17)(p15;q21) in acute poorly differentiated
RT myeloid leukemia likely results in ZMYND11-MBTD1 fusion.";
RL Leuk. Lymphoma 55:1189-1190(2014).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN NUA4 COMPLEX.
RX PubMed=27153538; DOI=10.1016/j.molcel.2016.03.031;
RA Jacquet K., Fradet-Turcotte A., Avvakumov N., Lambert J.P., Roques C.,
RA Pandita R.K., Paquet E., Herst P., Gingras A.C., Pandita T.K., Legube G.,
RA Doyon Y., Durocher D., Cote J.;
RT "The TIP60 complex regulates bivalent chromatin recognition by 53BP1
RT through direct H4K20me binding and H2AK15 acetylation.";
RL Mol. Cell 62:409-421(2016).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 130-566, SUBUNIT, AND FUNCTION.
RX PubMed=19841675; DOI=10.1371/journal.pone.0007274;
RA Eryilmaz J., Pan P., Amaya M.F., Allali-Hassani A., Dong A.,
RA Adams-Cioaba M.A., Mackenzie F., Vedadi M., Min J.;
RT "Structural studies of a four-MBT repeat protein MBTD1.";
RL PLoS ONE 4:E7274-E7274(2009).
RN [8] {ECO:0007744|PDB:6NFX}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 140-562 IN COMPLEX WITH EPC1,
RP FUNCTION, IDENTIFICATION IN NUA4 COMPLEX, INTERACTION WITH EPC1, AND
RP MUTAGENESIS OF ALA-236 AND 259-LEU--LEU-263.
RX PubMed=32209463; DOI=10.1016/j.celrep.2020.03.003;
RA Zhang H., Devoucoux M., Song X., Li L., Ayaz G., Cheng H., Tempel W.,
RA Dong C., Loppnau P., Cote J., Min J.;
RT "Structural basis for EPC1-mediated recruitment of MBTD1 into the
RT NuA4/TIP60 acetyltransferase complex.";
RL Cell Rep. 30:3996-4002(2020).
CC -!- FUNCTION: Chromatin reader component of the NuA4 histone
CC acetyltransferase complex, a multiprotein complex involved in
CC transcriptional activation of select genes principally by acetylation
CC of nucleosomal histones H4 and H2A (PubMed:27153538, PubMed:32209463).
CC The NuA4 complex plays a direct role in repair of DNA double-strand
CC breaks (DSBs) by promoting homologous recombination (HR)
CC (PubMed:27153538). MBTD1 specifically recognizes and binds
CC monomethylated and dimethylated 'Lys-20' on histone H4 (H4K20me1 and
CC H4K20me2, respectively) (PubMed:19841675, PubMed:27153538,
CC PubMed:32209463). In the NuA4 complex, MBTD1 promotes recruitment of
CC the complex to H4K20me marks by competing with TP53BP1 for binding to
CC H4K20me (PubMed:27153538). Following recruitment to H4K20me at DNA
CC breaks, the NuA4 complex catalyzes acetylation of 'Lys-15' on histone
CC H2A (H2AK15), blocking the ubiquitination mark required for TP53BP1
CC localization at DNA breaks, thereby promoting homologous recombination
CC (HR) (PubMed:27153538). {ECO:0000269|PubMed:19841675,
CC ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:32209463}.
CC -!- SUBUNIT: Monomer (PubMed:19841675). Component of the NuA4 histone
CC acetyltransferase complex (PubMed:27153538, PubMed:32209463). Interacts
CC with EPC1; interaction is direct and promotes recruitment of MBTD1 into
CC the NuA4 histone acetyltransferase complex (PubMed:32209463).
CC {ECO:0000269|PubMed:19841675, ECO:0000269|PubMed:27153538,
CC ECO:0000269|PubMed:32209463}.
CC -!- INTERACTION:
CC Q05BQ5; Q9H2F5: EPC1; NbExp=6; IntAct=EBI-5666902, EBI-769270;
CC Q05BQ5; P62805: H4C9; NbExp=3; IntAct=EBI-5666902, EBI-302023;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:27153538}. Chromosome
CC {ECO:0000269|PubMed:27153538}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q05BQ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05BQ5-2; Sequence=VSP_042701, VSP_042702;
CC Name=3;
CC IsoId=Q05BQ5-3; Sequence=VSP_030115, VSP_030118;
CC -!- DISEASE: Note=A chromosomal aberration involving MBTD1 is a cause of
CC acute poorly differentiated myeloid leukemia. Translocation
CC (10;17)(p15;q21) with ZMYND11. {ECO:0000269|PubMed:23915195}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC85763.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AK000062; BAA90919.1; -; mRNA.
DR EMBL; AK124061; BAC85763.1; ALT_SEQ; mRNA.
DR EMBL; AC005839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94562.1; -; Genomic_DNA.
DR EMBL; BC034364; AAH34364.1; -; mRNA.
DR EMBL; BC101736; AAI01737.1; -; mRNA.
DR CCDS; CCDS11581.2; -. [Q05BQ5-1]
DR RefSeq; NP_060113.2; NM_017643.2. [Q05BQ5-1]
DR RefSeq; XP_011523238.1; XM_011524936.1.
DR PDB; 3FEO; X-ray; 2.50 A; A/B=130-566.
DR PDB; 4C5I; X-ray; 2.59 A; A/B=130-566.
DR PDB; 6NFX; X-ray; 1.95 A; A=140-562.
DR PDBsum; 3FEO; -.
DR PDBsum; 4C5I; -.
DR PDBsum; 6NFX; -.
DR AlphaFoldDB; Q05BQ5; -.
DR SMR; Q05BQ5; -.
DR BioGRID; 120158; 61.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR IntAct; Q05BQ5; 45.
DR MINT; Q05BQ5; -.
DR STRING; 9606.ENSP00000468304; -.
DR BindingDB; Q05BQ5; -.
DR ChEMBL; CHEMBL1287625; -.
DR DrugCentral; Q05BQ5; -.
DR iPTMnet; Q05BQ5; -.
DR PhosphoSitePlus; Q05BQ5; -.
DR BioMuta; MBTD1; -.
DR DMDM; 166232936; -.
DR EPD; Q05BQ5; -.
DR jPOST; Q05BQ5; -.
DR MassIVE; Q05BQ5; -.
DR MaxQB; Q05BQ5; -.
DR PaxDb; Q05BQ5; -.
DR PeptideAtlas; Q05BQ5; -.
DR PRIDE; Q05BQ5; -.
DR ProteomicsDB; 58373; -. [Q05BQ5-1]
DR ProteomicsDB; 58374; -. [Q05BQ5-2]
DR ProteomicsDB; 58375; -. [Q05BQ5-3]
DR ABCD; Q05BQ5; 1 sequenced antibody.
DR Antibodypedia; 18227; 109 antibodies from 21 providers.
DR DNASU; 54799; -.
DR Ensembl; ENST00000376381.3; ENSP00000365561.3; ENSG00000011258.16. [Q05BQ5-3]
DR Ensembl; ENST00000405860.7; ENSP00000386072.3; ENSG00000011258.16. [Q05BQ5-2]
DR Ensembl; ENST00000415868.5; ENSP00000403946.1; ENSG00000011258.16. [Q05BQ5-1]
DR Ensembl; ENST00000586178.6; ENSP00000468304.1; ENSG00000011258.16. [Q05BQ5-1]
DR GeneID; 54799; -.
DR KEGG; hsa:54799; -.
DR MANE-Select; ENST00000586178.6; ENSP00000468304.1; NM_017643.3; NP_060113.2.
DR UCSC; uc002itp.5; human. [Q05BQ5-1]
DR CTD; 54799; -.
DR DisGeNET; 54799; -.
DR GeneCards; MBTD1; -.
DR HGNC; HGNC:19866; MBTD1.
DR HPA; ENSG00000011258; Low tissue specificity.
DR MIM; 618705; gene.
DR neXtProt; NX_Q05BQ5; -.
DR OpenTargets; ENSG00000011258; -.
DR PharmGKB; PA134938339; -.
DR VEuPathDB; HostDB:ENSG00000011258; -.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000153840; -.
DR HOGENOM; CLU_005352_2_1_1; -.
DR InParanoid; Q05BQ5; -.
DR OMA; WFARVMK; -.
DR OrthoDB; 1334498at2759; -.
DR PhylomeDB; Q05BQ5; -.
DR PathwayCommons; Q05BQ5; -.
DR SignaLink; Q05BQ5; -.
DR BioGRID-ORCS; 54799; 116 hits in 1086 CRISPR screens.
DR ChiTaRS; MBTD1; human.
DR EvolutionaryTrace; Q05BQ5; -.
DR GenomeRNAi; 54799; -.
DR Pharos; Q05BQ5; Tbio.
DR PRO; PR:Q05BQ5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q05BQ5; protein.
DR Bgee; ENSG00000011258; Expressed in upper leg skin and 186 other tissues.
DR ExpressionAtlas; Q05BQ5; baseline and differential.
DR Genevisible; Q05BQ5; HS.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:ComplexPortal.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR Gene3D; 3.30.60.160; -; 1.
DR IDEAL; IID00562; -.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR Pfam; PF02820; MBT; 4.
DR SMART; SM00561; MBT; 4.
DR PROSITE; PS51079; MBT; 4.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Chromosomal rearrangement; Chromosome; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..628
FT /note="MBT domain-containing protein 1"
FT /id="PRO_0000313717"
FT REPEAT 141..245
FT /note="MBT 1"
FT REPEAT 253..350
FT /note="MBT 2"
FT REPEAT 351..456
FT /note="MBT 3"
FT REPEAT 464..560
FT /note="MBT 4"
FT ZN_FING 45..80
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5G3"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030115"
FT VAR_SEQ 163..169
FT /note="APMGTCW -> GRRVAPR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042701"
FT VAR_SEQ 170..628
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042702"
FT VAR_SEQ 564..628
FT /note="SSRENQSASSKQKKKAKSQQYKGHKKMTTLQLKEELLDGEDYNFLQGASDQE
FT SNGSANFYIKQEP -> CKLVYRKGVLL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030118"
FT MUTAGEN 236
FT /note="A->D: Impaired interaction with EPC1; when
FT associated with 259-D--D-263."
FT /evidence="ECO:0000269|PubMed:32209463"
FT MUTAGEN 236
FT /note="A->G: Impaired interaction with EPC1. Abolished
FT interaction with EPC1; when associated with 259-G--G-263."
FT /evidence="ECO:0000269|PubMed:32209463"
FT MUTAGEN 259..263
FT /note="LVKRL->DVKRD: Impaired interaction with EPC1; when
FT associated with D-236."
FT /evidence="ECO:0000269|PubMed:32209463"
FT MUTAGEN 259..263
FT /note="LVKRL->GVKRG: Impaired interaction with EPC1.
FT Abolished interaction with EPC1; when associated with G-
FT 236."
FT /evidence="ECO:0000269|PubMed:32209463"
FT CONFLICT 575
FT /note="Q -> K (in Ref. 4; AAH34364)"
FT /evidence="ECO:0000305"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4C5I"
FT STRAND 192..201
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6NFX"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 273..280
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 298..311
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:3FEO"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 397..409
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:3FEO"
FT HELIX 466..473
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 480..483
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 497..501
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 509..518
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 521..526
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:6NFX"
FT STRAND 535..538
FT /evidence="ECO:0007829|PDB:6NFX"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:6NFX"
SQ SEQUENCE 628 AA; 70547 MW; 8D2E6C7EF5C5D8AA CRC64;
MFDGYDSCSE DTSSSSSSEE SEEEVAPLPS NLPIIKNNGQ VYTYPDGKSG MATCEMCGMV
GVRDAFYSKT KRFCSVSCSR SYSSNSKKAS ILARLQGKPP TKKAKVLQKQ PLVAKLAAYA
QYQATLQNQA KTKAAVSMEG FSWGNYINSN SFIAAPVTCF KHAPMGTCWG DISENVRVEV
PNTDCSLPTK VFWIAGIVKL AGYNALLRYE GFENDSGLDF WCNICGSDIH PVGWCAASGK
PLVPPRTIQH KYTNWKAFLV KRLTGAKTLP PDFSQKVSES MQYPFKPCMR VEVVDKRHLC
RTRVAVVESV IGGRLRLVYE ESEDRTDDFW CHMHSPLIHH IGWSRSIGHR FKRSDITKKQ
DGHFDTPPHL FAKVKEVDQS GEWFKEGMKL EAIDPLNLST ICVATIRKVL ADGFLMIGID
GSEAADGSDW FCYHATSPSI FPVGFCEINM IELTPPRGYT KLPFKWFDYL RETGSIAAPV
KLFNKDVPNH GFRVGMKLEA VDLMEPRLIC VATVTRIIHR LLRIHFDGWE EEYDQWVDCE
SPDLYPVGWC QLTGYQLQPP ASQSSRENQS ASSKQKKKAK SQQYKGHKKM TTLQLKEELL
DGEDYNFLQG ASDQESNGSA NFYIKQEP
