DHX8_HUMAN
ID DHX8_HUMAN Reviewed; 1220 AA.
AC Q14562;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=ATP-dependent RNA helicase DHX8;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P24384};
DE AltName: Full=DEAH box protein 8;
DE AltName: Full=RNA helicase HRH1 {ECO:0000303|PubMed:7935475, ECO:0000303|PubMed:8608946};
GN Name=DHX8; Synonyms=DDX8;
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 [MRNA].
RX PubMed=7935475; DOI=10.1128/mcb.14.11.7611-7620.1994;
RA Ono Y., Ohno M., Shimura Y.;
RT "Identification of a putative RNA helicase (HRH1), a human homolog of yeast
RT Prp22.";
RL Mol. Cell. Biol. 14:7611-7620(1994).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF LYS-594 AND SER-717.
RX PubMed=8608946; DOI=10.1101/gad.10.8.997;
RA Ohno M., Shimura Y.;
RT "A human RNA helicase-like protein, HRH1, facilitates nuclear export of
RT spliced mRNA by releasing the RNA from the spliceosome.";
RL Genes Dev. 10:997-1007(1996).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C
RP COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [4]
RP INTERACTION WITH ARRB2.
RX PubMed=16820410; DOI=10.1242/jcs.03046;
RA Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.;
RT "Novel function of beta-arrestin2 in the nucleus of mature spermatozoa.";
RL J. Cell Sci. 119:3047-3056(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-140 AND LYS-399, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [11]
RP VARIANT TRP-168, AND TISSUE SPECIFICITY.
RX PubMed=31256877; DOI=10.1016/j.ajhg.2019.06.001;
RG University of Washington Center for Mendelian Genomics, Baylor-Hopkins Center for Mendelian Genomics, Telethon Undiagnosed Diseases Program;
RA Paine I., Posey J.E., Grochowski C.M., Jhangiani S.N., Rosenheck S.,
RA Kleyner R., Marmorale T., Yoon M., Wang K., Robison R., Cappuccio G.,
RA Pinelli M., Magli A., Coban Akdemir Z., Hui J., Yeung W.L., Wong B.K.Y.,
RA Ortega L., Bekheirnia M.R., Bierhals T., Hempel M., Johannsen J.,
RA Santer R., Aktas D., Alikasifoglu M., Bozdogan S., Aydin H., Karaca E.,
RA Bayram Y., Ityel H., Dorschner M., White J.J., Wilichowski E.,
RA Wortmann S.B., Casella E.B., Kitajima J.P., Kok F., Monteiro F.,
RA Muzny D.M., Bamshad M., Gibbs R.A., Sutton V.R., Van Esch H.,
RA Brunetti-Pierri N., Hildebrandt F., Brautbar A., Van den Veyver I.B.,
RA Glass I., Lessel D., Lyon G.J., Lupski J.R.;
RT "Paralog studies augment gene discovery: DDX and DHX genes.";
RL Am. J. Hum. Genet. 105:302-316(2019).
RN [12]
RP STRUCTURE BY NMR OF 260-355.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the S1 RNA binding domain of human ATP-dependent RNA
RT helicase DHX8.";
RL Submitted (OCT-2007) to the PDB data bank.
RN [13] {ECO:0007744|PDB:3I4U}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 950-1183.
RX PubMed=23096351; DOI=10.1515/hsz-2012-0158;
RA Kudlinzki D., Schmitt A., Christian H., Ficner R.;
RT "Structural analysis of the C-terminal domain of the spliceosomal helicase
RT Prp22.";
RL Biol. Chem. 393:1131-1140(2012).
RN [14] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [15] {ECO:0007744|PDB:5MQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28076346; DOI=10.1038/nature21079;
RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT "Cryo-EM structure of a human spliceosome activated for step 2 of
RT splicing.";
RL Nature 542:318-323(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC (PubMed:11991638, PubMed:28502770, PubMed:28076346). Facilitates
CC nuclear export of spliced mRNA by releasing the RNA from the
CC spliceosome (PubMed:8608946). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:8608946}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:P24384};
CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638,
CC PubMed:28502770, PubMed:28076346). Interacts with ARRB2; the
CC interaction is detected in the nucleus upon OR1D2 stimulation
CC (PubMed:16820410). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:16820410, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770}.
CC -!- INTERACTION:
CC Q14562; Q8IWX8: CHERP; NbExp=2; IntAct=EBI-2511477, EBI-2555370;
CC Q14562; Q14562: DHX8; NbExp=2; IntAct=EBI-2511477, EBI-2511477;
CC Q14562; Q9ULR0: ISY1; NbExp=2; IntAct=EBI-2511477, EBI-2557660;
CC Q14562; Q8N5F7: NKAP; NbExp=2; IntAct=EBI-2511477, EBI-721539;
CC Q14562; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-2511477, EBI-539478;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC -!- TISSUE SPECIFICITY: Expressed in skin, cervix and nerve. Also expressed
CC in the brain. {ECO:0000269|PubMed:31256877}.
CC -!- DOMAIN: The RS domain confers a nuclear localization signal, and
CC appears to facilitate the interaction with the spliceosome.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX8/PRP22 sub-subfamily. {ECO:0000305}.
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DR EMBL; D50487; BAA09078.1; -; mRNA.
DR CCDS; CCDS11464.1; -.
DR PIR; A56236; A56236.
DR RefSeq; NP_001289552.1; NM_001302623.1.
DR RefSeq; NP_004932.1; NM_004941.2.
DR PDB; 2EQS; NMR; -; A=260-355.
DR PDB; 3I4U; X-ray; 2.10 A; A=950-1183.
DR PDB; 5MQF; EM; 5.90 A; q=1-1220.
DR PDB; 5XJC; EM; 3.60 A; Y=1-1220.
DR PDB; 6HYS; X-ray; 2.60 A; A/B/C/D=548-1220.
DR PDB; 6HYT; X-ray; 2.33 A; A/B/C/D=548-1220.
DR PDB; 6HYU; X-ray; 3.22 A; A/C=548-1220.
DR PDB; 6ICZ; EM; 3.00 A; Y=1-1220.
DR PDB; 6QDV; EM; 3.30 A; V=1-1220.
DR PDBsum; 2EQS; -.
DR PDBsum; 3I4U; -.
DR PDBsum; 5MQF; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 6HYS; -.
DR PDBsum; 6HYT; -.
DR PDBsum; 6HYU; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6QDV; -.
DR AlphaFoldDB; Q14562; -.
DR SMR; Q14562; -.
DR BioGRID; 108024; 286.
DR CORUM; Q14562; -.
DR IntAct; Q14562; 65.
DR MINT; Q14562; -.
DR STRING; 9606.ENSP00000262415; -.
DR GlyGen; Q14562; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14562; -.
DR MetOSite; Q14562; -.
DR PhosphoSitePlus; Q14562; -.
DR BioMuta; DHX8; -.
DR DMDM; 3023637; -.
DR EPD; Q14562; -.
DR jPOST; Q14562; -.
DR MassIVE; Q14562; -.
DR MaxQB; Q14562; -.
DR PaxDb; Q14562; -.
DR PeptideAtlas; Q14562; -.
DR PRIDE; Q14562; -.
DR ProteomicsDB; 60044; -.
DR Antibodypedia; 29563; 195 antibodies from 25 providers.
DR DNASU; 1659; -.
DR Ensembl; ENST00000262415.8; ENSP00000262415.2; ENSG00000067596.12.
DR Ensembl; ENST00000650571.1; ENSP00000496923.1; ENSG00000067596.12.
DR GeneID; 1659; -.
DR KEGG; hsa:1659; -.
DR MANE-Select; ENST00000262415.8; ENSP00000262415.2; NM_004941.3; NP_004932.1.
DR UCSC; uc002idu.2; human.
DR CTD; 1659; -.
DR DisGeNET; 1659; -.
DR GeneCards; DHX8; -.
DR HGNC; HGNC:2749; DHX8.
DR HPA; ENSG00000067596; Low tissue specificity.
DR MIM; 600396; gene.
DR neXtProt; NX_Q14562; -.
DR OpenTargets; ENSG00000067596; -.
DR PharmGKB; PA27231; -.
DR VEuPathDB; HostDB:ENSG00000067596; -.
DR eggNOG; KOG0922; Eukaryota.
DR GeneTree; ENSGT00940000155510; -.
DR HOGENOM; CLU_001832_2_1_1; -.
DR InParanoid; Q14562; -.
DR OMA; DPMVAPE; -.
DR OrthoDB; 354219at2759; -.
DR PhylomeDB; Q14562; -.
DR TreeFam; TF300509; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; Q14562; -.
DR SignaLink; Q14562; -.
DR BioGRID-ORCS; 1659; 776 hits in 1079 CRISPR screens.
DR ChiTaRS; DHX8; human.
DR EvolutionaryTrace; Q14562; -.
DR GenomeRNAi; 1659; -.
DR Pharos; Q14562; Tbio.
DR PRO; PR:Q14562; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14562; protein.
DR Bgee; ENSG00000067596; Expressed in lower esophagus mucosa and 150 other tissues.
DR ExpressionAtlas; Q14562; baseline and differential.
DR Genevisible; Q14562; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; TAS:ProtInc.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IBA:GO_Central.
DR CDD; cd17971; DEXHc_DHX8; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR044762; DHX8/Prp22_DEXHc.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome; Ubl conjugation.
FT CHAIN 1..1220
FT /note="ATP-dependent RNA helicase DHX8"
FT /id="PRO_0000055131"
FT DOMAIN 265..336
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 575..738
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 756..936
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 153..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 685..688
FT /note="DEAH box"
FT COMPBIAS 195..226
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 588..595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 168
FT /note="R -> W (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083620"
FT VARIANT 1069
FT /note="A -> G (in dbSNP:rs34285079)"
FT /id="VAR_052174"
FT MUTAGEN 594
FT /note="K->E: In GET; inhibition of pre-mRNA splicing and
FT nuclear export of unspliced RNA."
FT /evidence="ECO:0000269|PubMed:8608946"
FT MUTAGEN 717
FT /note="S->L: In LAT; inhibition of pre-mRNA splicing and
FT nuclear export of unspliced RNA."
FT /evidence="ECO:0000269|PubMed:8608946"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:2EQS"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:2EQS"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:2EQS"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:2EQS"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:2EQS"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:2EQS"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:2EQS"
FT STRAND 318..327
FT /evidence="ECO:0007829|PDB:2EQS"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:2EQS"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:2EQS"
FT HELIX 397..407
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 524..527
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 535..541
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 558..563
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 566..570
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 571..580
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 582..588
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 594..604
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 607..609
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 611..619
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 620..634
FT /evidence="ECO:0007829|PDB:6HYT"
FT TURN 639..641
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 642..646
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 657..662
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 663..672
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 679..684
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 687..689
FT /evidence="ECO:0007829|PDB:6HYS"
FT HELIX 692..707
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 712..717
FT /evidence="ECO:0007829|PDB:6HYT"
FT TURN 719..721
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 722..728
FT /evidence="ECO:0007829|PDB:6HYT"
FT TURN 729..731
FT /evidence="ECO:0007829|PDB:6HYU"
FT STRAND 734..737
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 744..748
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 756..770
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 775..779
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 783..798
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 802..804
FT /evidence="ECO:0007829|PDB:6HYS"
FT STRAND 807..812
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 818..823
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 833..838
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 841..844
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 851..856
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 859..865
FT /evidence="ECO:0007829|PDB:6HYT"
FT TURN 867..869
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 872..878
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 881..888
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 889..892
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:6HYT"
FT STRAND 897..903
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 905..911
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 919..921
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 926..934
FT /evidence="ECO:0007829|PDB:6HYT"
FT TURN 940..942
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 950..963
FT /evidence="ECO:0007829|PDB:3I4U"
FT TURN 964..966
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 969..971
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 975..980
FT /evidence="ECO:0007829|PDB:3I4U"
FT STRAND 983..985
FT /evidence="ECO:0007829|PDB:6HYT"
FT HELIX 987..998
FT /evidence="ECO:0007829|PDB:3I4U"
FT HELIX 1002..1012
FT /evidence="ECO:0007829|PDB:3I4U"
FT HELIX 1022..1024
FT /evidence="ECO:0007829|PDB:3I4U"
FT HELIX 1025..1033
FT /evidence="ECO:0007829|PDB:3I4U"
FT STRAND 1038..1040
FT /evidence="ECO:0007829|PDB:6HYU"
FT HELIX 1041..1054
FT /evidence="ECO:0007829|PDB:3I4U"
FT TURN 1055..1057
FT /evidence="ECO:0007829|PDB:3I4U"
FT HELIX 1059..1064
FT /evidence="ECO:0007829|PDB:3I4U"
FT HELIX 1069..1088
FT /evidence="ECO:0007829|PDB:3I4U"
FT HELIX 1101..1111
FT /evidence="ECO:0007829|PDB:3I4U"
FT HELIX 1112..1114
FT /evidence="ECO:0007829|PDB:3I4U"
FT STRAND 1115..1118
FT /evidence="ECO:0007829|PDB:3I4U"
FT STRAND 1120..1126
FT /evidence="ECO:0007829|PDB:3I4U"
FT TURN 1127..1129
FT /evidence="ECO:0007829|PDB:3I4U"
FT STRAND 1132..1135
FT /evidence="ECO:0007829|PDB:3I4U"
FT TURN 1140..1143
FT /evidence="ECO:0007829|PDB:3I4U"
FT STRAND 1147..1167
FT /evidence="ECO:0007829|PDB:3I4U"
FT HELIX 1170..1176
FT /evidence="ECO:0007829|PDB:3I4U"
FT TURN 1178..1180
FT /evidence="ECO:0007829|PDB:3I4U"
SQ SEQUENCE 1220 AA; 139315 MW; 17C1602A73A0EF24 CRC64;
MAVAVAMAGA LIGSEPGPAE ELAKLEYLSL VSKVCTELDN HLGINDKDLA EFVISLAEKN
TTFDTFKASL VKNGAEFTDS LISNLLRLIQ TMRPPAKPST SKDPVVKPKT EKEKLKELFP
VLCQPDNPSV RTMLDEDDVK VAVDVLKELE ALMPSAAGQE KQRDAEHRDR TKKKKRSRSR
DRNRDRDRDR ERNRDRDHKR RHRSRSRSRS RTRERNKVKS RYRSRSRSQS PPKDRKDRDK
YGERNLDRWR DKHVDRPPPE EPTIGDIYNG KVTSIMQFGC FVQLEGLRKR WEGLVHISEL
RREGRVANVA DVVSKGQRVK VKVLSFTGTK TSLSMKDVDQ ETGEDLNPNR RRNLVGETNE
ETSMRNPDRP THLSLVSAPE VEDDSLERKR LTRISDPEKW EIKQMIAANV LSKEEFPDFD
EETGILPKVD DEEDEDLEIE LVEEEPPFLR GHTKQSMDMS PIKIVKNPDG SLSQAAMMQS
ALAKERRELK QAQREAEMDS IPMGLNKHWV DPLPDAEGRQ IAANMRGIGM MPNDIPEWKK
HAFGGNKASY GKKTQMSILE QRESLPIYKL KEQLVQAVHD NQILIVIGET GSGKTTQITQ
YLAEAGYTSR GKIGCTQPRR VAAMSVAKRV SEEFGCCLGQ EVGYTIRFED CTSPETVIKY
MTDGMLLREC LIDPDLTQYA IIMLDEAHER TIHTDVLFGL LKKTVQKRQD MKLIVTSATL
DAVKFSQYFY EAPIFTIPGR TYPVEILYTK EPETDYLDAS LITVMQIHLT EPPGDILVFL
TGQEEIDTAC EILYERMKSL GPDVPELIIL PVYSALPSEM QTRIFDPAPP GSRKVVIATN
IAETSLTIDG IYYVVDPGFV KQKVYNSKTG IDQLVVTPIS QAQAKQRAGR AGRTGPGKCY
RLYTERAYRD EMLTTNVPEI QRTNLASTVL SLKAMGINDL LSFDFMDAPP METLITAMEQ
LYTLGALDDE GLLTRLGRRM AEFPLEPMLC KMLIMSVHLG CSEEMLTIVS MLSVQNVFYR
PKDKQALADQ KKAKFHQTEG DHLTLLAVYN SWKNNKFSNP WCYENFIQAR SLRRAQDIRK
QMLGIMDRHK LDVVSCGKST VRVQKAICSG FFRNAAKKDP QEGYRTLIDQ QVVYIHPSSA
LFNRQPEWVV YHELVLTTKE YMREVTTIDP RWLVEFAPAF FKVSDPTKLS KQKKQQRLEP
LYNRYEEPNA WRISRAFRRR
