DX39B_HUMAN
ID DX39B_HUMAN Reviewed; 428 AA.
AC Q13838; B0S8C0; O43496; Q0EFA1; Q2L6F9; Q53GL9; Q5RJ64; Q5RJ66; Q5ST94;
AC Q5STB4; Q5STB5; Q5STB7; Q5STB8; Q5STU4; Q5STU5; Q5STU6; Q5STU8; Q71V76;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Spliceosome RNA helicase DDX39B {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000269|PubMed:17984224};
DE AltName: Full=56 kDa U2AF65-associated protein;
DE AltName: Full=ATP-dependent RNA helicase p47;
DE AltName: Full=DEAD box protein UAP56;
DE AltName: Full=HLA-B-associated transcript 1 protein;
GN Name=DDX39B {ECO:0000312|HGNC:HGNC:13917}; Synonyms=BAT1, UAP56;
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] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=7601445; DOI=10.1016/0888-7543(95)80203-x;
RA Peelman L., Chardon P., Nunes M., Renard C., Geffrotin C., Vaiman M.,
RA van Zeveren A., Coppieters W., van de Weghe A., Bouquet Y., Choy W.,
RA Strominger J., Spies T.;
RT "The BAT1 gene in the MHC encodes an evolutionarily conserved putative
RT nuclear RNA helicase of the DEAD family.";
RL Genomics 26:210-218(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney epithelium;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-428.
RA Allcock R.J.N., Price P., Gaudieri S., Leelayuwat C., Witt C.S.,
RA Dawkins R.L.;
RT "Homo sapiens BAT1 (BAT1) gene, partial cds; and PERB18 pseudogene,
RT complete sequence.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, INTERACTION WITH U2AF2 AND THE SPLICEOSOME, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9242493; DOI=10.1101/gad.11.14.1864;
RA Fleckner J., Zhang M., Valcarcel J., Green M.R.;
RT "U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-
RT branchpoint interaction.";
RL Genes Dev. 11:1864-1872(1997).
RN [10]
RP FUNCTION, INTERACTION WITH ALYREF/THOC4 AND THE SPLICEOSOME, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11675789; DOI=10.1038/35098106;
RA Luo M.-J., Zhou Z., Magni K., Christoforides C., Rappsilber J., Mann M.,
RA Reed R.;
RT "Pre-mRNA splicing and mRNA export linked by direct interactions between
RT UAP56 and Aly.";
RL Nature 413:644-647(2001).
RN [11]
RP INTERACTION WITH RBM8A; RNPS1; SRRM1 AND ALYREF/THOC4.
RX PubMed=12944400; DOI=10.1074/jbc.m306856200;
RA McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.;
RT "An evolutionarily conserved role for SRm160 in 3'-end processing that
RT functions independently of exon junction complex formation.";
RL J. Biol. Chem. 278:44153-44160(2003).
RN [12]
RP HOMODIMERIZATION, AND INTERACTION WITH ALYREF/THOC4 AND DDX39A.
RX PubMed=14667819; DOI=10.1016/s0888-7543(03)00235-0;
RA Lehner B., Semple J.I., Brown S.E., Counsell D., Campbell R.D.,
RA Sanderson C.M.;
RT "Analysis of a high-throughput yeast two-hybrid system and its use to
RT predict the function of intracellular proteins encoded within the human MHC
RT class III region.";
RL Genomics 83:153-167(2004).
RN [13]
RP IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15833825; DOI=10.1158/0008-5472.can-04-3624;
RA Guo S., Hakimi M.A., Baillat D., Chen X., Farber M.J., Klein-Szanto A.J.,
RA Cooch N.S., Godwin A.K., Shiekhattar R.;
RT "Linking transcriptional elongation and messenger RNA export to metastatic
RT breast cancers.";
RL Cancer Res. 65:3011-3016(2005).
RN [14]
RP IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ALYREF/THOC4, AND
RP DOMAIN.
RX PubMed=15998806; DOI=10.1101/gad.1302205;
RA Masuda S., Das R., Cheng H., Hurt E., Dorman N., Reed R.;
RT "Recruitment of the human TREX complex to mRNA during splicing.";
RL Genes Dev. 19:1512-1517(2005).
RN [15]
RP INTERACTION WITH THOC1, AND SUBCELLULAR LOCATION.
RX PubMed=15870275; DOI=10.1128/mcb.25.10.4023-4033.2005;
RA Li Y., Wang X., Zhang X., Goodrich D.W.;
RT "Human hHpr1/p84/Thoc1 regulates transcriptional elongation and physically
RT links RNA polymerase II and RNA processing factors.";
RL Mol. Cell. Biol. 25:4023-4033(2005).
RN [16]
RP FUNCTION OF THE TREX COMPLEX.
RX PubMed=17190602; DOI=10.1016/j.cell.2006.10.044;
RA Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.;
RT "Human mRNA export machinery recruited to the 5' end of mRNA.";
RL Cell 127:1389-1400(2006).
RN [17]
RP INTERACTION WITH HHV-5 PROTEIN UL69.
RX PubMed=16478985; DOI=10.1128/mcb.26.5.1631-1643.2006;
RA Lischka P., Toth Z., Thomas M., Mueller R., Stamminger T.;
RT "The UL69 transactivator protein of human cytomegalovirus interacts with
RT DEXD/H-Box RNA helicase UAP56 to promote cytoplasmic accumulation of
RT unspliced RNA.";
RL Mol. Cell. Biol. 26:1631-1643(2006).
RN [18]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF 94-GLY--THR-96;
RP LYS-95; GLU-197; ASP-199 AND 228-SER--THR-230.
RX PubMed=17562711; DOI=10.1074/jbc.m702304200;
RA Shen J., Zhang L., Zhao R.;
RT "Biochemical characterization of the ATPase and helicase activity of UAP56,
RT an essential pre-mRNA splicing and mRNA export factor.";
RL J. Biol. Chem. 282:22544-22550(2007).
RN [19]
RP FUNCTION, INTERACTION WITH ALYREF, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP LYS-95.
RX PubMed=17984224; DOI=10.1128/mcb.01341-07;
RA Taniguchi I., Ohno M.;
RT "ATP-dependent recruitment of export factor Aly/REF onto intronless mRNAs
RT by RNA helicase UAP56.";
RL Mol. Cell. Biol. 28:601-608(2008).
RN [20]
RP FUNCTION OF THE TREX COMPLEX (MICROBIAL INFECTION).
RX PubMed=18974867; DOI=10.1371/journal.ppat.1000194;
RA Boyne J.R., Colgan K.J., Whitehouse A.;
RT "Recruitment of the complete hTREX complex is required for Kaposi's
RT sarcoma-associated herpesvirus intronless mRNA nuclear export and virus
RT replication.";
RL PLoS Pathog. 4:E1000194-E1000194(2008).
RN [21]
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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP INTERACTION WITH FYTTD1.
RX PubMed=19836239; DOI=10.1016/j.cub.2009.09.041;
RA Hautbergue G.M., Hung M.L., Walsh M.J., Snijders A.P., Chang C.T.,
RA Jones R., Ponting C.P., Dickman M.J., Wilson S.A.;
RT "UIF, a new mRNA export adaptor that works together with REF/ALY, requires
RT FACT for recruitment to mRNA.";
RL Curr. Biol. 19:1918-1924(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [25]
RP FUNCTION, AND INTERACTION WITH ALYREF AND SARNP.
RX PubMed=20844015; DOI=10.1101/gad.1898610;
RA Dufu K., Livingstone M.J., Seebacher J., Gygi S.P., Wilson S.A., Reed R.;
RT "ATP is required for interactions between UAP56 and two conserved mRNA
RT export proteins, Aly and CIP29, to assemble the TREX complex.";
RL Genes Dev. 24:2043-2053(2010).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND THR-172, AND
RP IDENTIFICATION BY 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 [27]
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 [28]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MX1.
RX PubMed=21859714; DOI=10.1074/jbc.m111.251843;
RA Wisskirchen C., Ludersdorfer T.H., Mueller D.A., Moritz E., Pavlovic J.;
RT "Interferon-induced antiviral protein MxA interacts with the cellular RNA
RT helicases UAP56 and URH49.";
RL J. Biol. Chem. 286:34743-34751(2011).
RN [29]
RP FUNCTION.
RX PubMed=22144908; DOI=10.1371/journal.pgen.1002386;
RA Dominguez-Sanchez M.S., Barroso S., Gomez-Gonzalez B., Luna R.,
RA Aguilera A.;
RT "Genome instability and transcription elongation impairment in human cells
RT depleted of THO/TREX.";
RL PLoS Genet. 7:E1002386-E1002386(2011).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [31]
RP INTERACTION WITH POLDIP3.
RX PubMed=22928037; DOI=10.1371/journal.pone.0043804;
RA Folco E.G., Lee C.S., Dufu K., Yamazaki T., Reed R.;
RT "The proteins PDIP3 and ZC11A associate with the human TREX complex in an
RT ATP-dependent manner and function in mRNA export.";
RL PLoS ONE 7:E43804-E43804(2012).
RN [32]
RP FUNCTION, AND INTERACTION WITH CHTOP.
RX PubMed=23299939; DOI=10.1038/emboj.2012.342;
RA Chang C.T., Hautbergue G.M., Walsh M.J., Viphakone N., van Dijk T.B.,
RA Philipsen S., Wilson S.A.;
RT "Chtop is a component of the dynamic TREX mRNA export complex.";
RL EMBO J. 32:473-486(2013).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-41 AND THR-172, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [34]
RP FUNCTION.
RX PubMed=23222130; DOI=10.1093/nar/gks1188;
RA Chi B., Wang Q., Wu G., Tan M., Wang L., Shi M., Chang X., Cheng H.;
RT "Aly and THO are required for assembly of the human TREX complex and
RT association of TREX components with the spliced mRNA.";
RL Nucleic Acids Res. 41:1294-1306(2013).
RN [35]
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 [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [37]
RP INTERACTION WITH LUZP4.
RX PubMed=25662211; DOI=10.1093/nar/gkv070;
RA Viphakone N., Cumberbatch M.G., Livingstone M.J., Heath P.R., Dickman M.J.,
RA Catto J.W., Wilson S.A.;
RT "Luzp4 defines a new mRNA export pathway in cancer cells.";
RL Nucleic Acids Res. 43:2353-2366(2015).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND IDENTIFICATION BY MASS
RP 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 [39]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 44-428 IN COMPLEX WITH ADP,
RP FUNCTION, AND MUTAGENESIS OF CYS-198.
RX PubMed=15585580; DOI=10.1073/pnas.0408172101;
RA Shi H., Cordin O., Minder C.M., Linder P., Xu R.-M.;
RT "Crystal structure of the human ATP-dependent splicing and export factor
RT UAP56.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17628-17633(2004).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 34-428, AND DIMERIZATION.
RX PubMed=15296731; DOI=10.1016/j.str.2004.06.006;
RA Zhao R., Shen J., Green M.R., MacMorris M., Blumenthal T.;
RT "Crystal structure of UAP56, a DExD/H-box protein involved in pre-mRNA
RT splicing and mRNA export.";
RL Structure 12:1373-1381(2004).
CC -!- FUNCTION: Involved in nuclear export of spliced and unspliced mRNA.
CC Assembling component of the TREX complex which is thought to couple
CC mRNA transcription, processing and nuclear export, and specifically
CC associates with spliced mRNA and not with unspliced pre-mRNA. TREX is
CC recruited to spliced mRNAs by a transcription-independent mechanism,
CC binds to mRNA upstream of the exon-junction complex (EJC) and is
CC recruited in a splicing- and cap-dependent manner to a region near the
CC 5' end of the mRNA where it functions in mRNA export to the cytoplasm
CC via the TAP/NFX1 pathway. May undergo several rounds of ATP hydrolysis
CC during assembly of TREX to drive subsequent loading of components such
CC as ALYREF/THOC and CHTOP onto mRNA. Also associates with pre-mRNA
CC independent of ALYREF/THOC4 and the THO complex. Involved in the
CC nuclear export of intronless mRNA; the ATP-bound form is proposed to
CC recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase
CC activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP
CC hydrolysis is thought to trigger the dissociation from RNA to allow the
CC association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in
CC transcription elongation and genome stability.
CC {ECO:0000269|PubMed:11675789, ECO:0000269|PubMed:15585580,
CC ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806,
CC ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17562711,
CC ECO:0000269|PubMed:17984224, ECO:0000269|PubMed:20844015,
CC ECO:0000269|PubMed:22144908, ECO:0000269|PubMed:23222130,
CC ECO:0000269|PubMed:23299939, ECO:0000269|PubMed:9242493}.
CC -!- FUNCTION: Splice factor that is required for the first ATP-dependent
CC step in spliceosome assembly and for the interaction of U2 snRNP with
CC the branchpoint. Has both RNA-stimulated ATP binding/hydrolysis
CC activity and ATP-dependent RNA unwinding activity. Even with the
CC stimulation of RNA, the ATPase activity is weak. Can only hydrolyze ATP
CC but not other NTPs. The RNA stimulation of ATPase activity does not
CC have a strong preference for the sequence and length of the RNA.
CC However, ssRNA stimulates the ATPase activity much more strongly than
CC dsRNA. Can unwind 5' or 3' overhangs or blunt end RNA duplexes in
CC vitro. The ATPase and helicase activities are not influenced by U2AF2;
CC the effect of ALYREF/THOC4 is reported conflictingly with
CC [PubMed:23299939] reporting a stimulatory effect.
CC {ECO:0000269|PubMed:23299939, ECO:0000269|PubMed:9242493}.
CC -!- FUNCTION: (Microbial infection) The TREX complex is essential for the
CC export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless
CC mRNAs and infectious virus production. {ECO:0000269|PubMed:18974867}.
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:0000269|PubMed:17984224};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.3 uM for ATP {ECO:0000269|PubMed:17562711};
CC Vmax=0.126 uM/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:17562711};
CC -!- SUBUNIT: Homodimer, and heterodimer with DDX39A (PubMed:11675789,
CC PubMed:15833825, PubMed:14667819). Component of the
CC transcription/export (TREX) complex at least composed of ALYREF/THOC4,
CC DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have
CC dynamic structure involving ATP-dependent remodeling; in the complex
CC bridges ALYREF/THOC4 and the THO complex, and, in a ATP-dependent
CC manner, ALYREF/THOC4 and SARNP/CIP29 (PubMed:11675789, PubMed:15833825,
CC PubMed:14667819, PubMed:15998806, PubMed:17984224, PubMed:20844015,
CC PubMed:23299939). Component of the spliceosome. Interacts directly with
CC U2AF2 (PubMed:9242493). Interacts with RBM8A, RNPS1 and SRRM1,
CC FYTTD1/UIF, THOC1, MX1 and POLDIP3 (PubMed:12944400, PubMed:15870275,
CC PubMed:19836239, PubMed:21859714, PubMed:22928037). Interacts with
CC LUZP4 (PubMed:25662211). {ECO:0000269|PubMed:11675789,
CC ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:14667819,
CC ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15870275,
CC ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17984224,
CC ECO:0000269|PubMed:19836239, ECO:0000269|PubMed:20844015,
CC ECO:0000269|PubMed:21859714, ECO:0000269|PubMed:22928037,
CC ECO:0000269|PubMed:23299939, ECO:0000269|PubMed:25662211,
CC ECO:0000269|PubMed:9242493}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human
CC cytomegalovirus/HHV-5 protein UL69. {ECO:0000269|PubMed:16478985}.
CC -!- INTERACTION:
CC Q13838; Q86V81: ALYREF; NbExp=4; IntAct=EBI-348622, EBI-347640;
CC Q13838; Q9Y3Y2: CHTOP; NbExp=7; IntAct=EBI-348622, EBI-347794;
CC Q13838; Q9Y3Y2-3: CHTOP; NbExp=5; IntAct=EBI-348622, EBI-11984237;
CC Q13838; O00148: DDX39A; NbExp=4; IntAct=EBI-348622, EBI-348253;
CC Q13838; Q13838: DDX39B; NbExp=4; IntAct=EBI-348622, EBI-348622;
CC Q13838; Q96QD9: FYTTD1; NbExp=3; IntAct=EBI-348622, EBI-724553;
CC Q13838; Q9P127: LUZP4; NbExp=3; IntAct=EBI-348622, EBI-10198848;
CC Q13838; P78317: RNF4; NbExp=3; IntAct=EBI-348622, EBI-2340927;
CC Q13838; P82979: SARNP; NbExp=4; IntAct=EBI-348622, EBI-347495;
CC Q13838; O00560: SDCBP; NbExp=3; IntAct=EBI-348622, EBI-727004;
CC Q13838; P09012: SNRPA; NbExp=3; IntAct=EBI-348622, EBI-607085;
CC Q13838; P26368-2: U2AF2; NbExp=3; IntAct=EBI-348622, EBI-11097439;
CC Q13838; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-348622, EBI-10180829;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm. Note=Can
CC translocate to the cytoplasm in the presence of MX1. TREX complex
CC assembly seems to occur in regions surrounding nuclear speckles known
CC as perispeckles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13838-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13838-2; Sequence=VSP_026347;
CC -!- DOMAIN: The helicase C-terminal domain mediates interaction with
CC ALYREF/THOC4. {ECO:0000269|PubMed:15998806}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.
CC {ECO:0000305}.
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DR EMBL; Z37166; CAA85523.1; -; mRNA.
DR EMBL; BT009909; AAP88911.1; -; mRNA.
DR EMBL; AK222912; BAD96632.1; -; mRNA.
DR EMBL; AB088115; BAC54953.1; -; Genomic_DNA.
DR EMBL; AB103621; BAF31287.1; -; Genomic_DNA.
DR EMBL; AB202112; BAE78637.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63306.1; -; Genomic_DNA.
DR EMBL; AL662801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX001040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03404.1; -; Genomic_DNA.
DR EMBL; BC000361; AAH00361.1; -; mRNA.
DR EMBL; BC013006; AAH13006.1; -; mRNA.
DR EMBL; AF029061; AAB94615.1; -; Genomic_DNA.
DR EMBL; AF029062; AAC63046.1; -; Genomic_DNA.
DR CCDS; CCDS4697.1; -. [Q13838-1]
DR PIR; I37201; I37201.
DR RefSeq; NP_004631.1; NM_004640.6. [Q13838-1]
DR RefSeq; NP_542165.1; NM_080598.5. [Q13838-1]
DR PDB; 1T5I; X-ray; 1.90 A; A=259-428.
DR PDB; 1T6N; X-ray; 1.94 A; A/B=34-251.
DR PDB; 1XTI; X-ray; 1.95 A; A=46-428.
DR PDB; 1XTJ; X-ray; 2.70 A; A=44-423.
DR PDB; 1XTK; X-ray; 2.40 A; A=45-428.
DR PDB; 7APK; EM; 3.30 A; H/P/h/p=1-428.
DR PDBsum; 1T5I; -.
DR PDBsum; 1T6N; -.
DR PDBsum; 1XTI; -.
DR PDBsum; 1XTJ; -.
DR PDBsum; 1XTK; -.
DR PDBsum; 7APK; -.
DR AlphaFoldDB; Q13838; -.
DR SMR; Q13838; -.
DR BioGRID; 113649; 397.
DR CORUM; Q13838; -.
DR IntAct; Q13838; 79.
DR MINT; Q13838; -.
DR STRING; 9606.ENSP00000379475; -.
DR DrugBank; DB11638; Artenimol.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR GlyGen; Q13838; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13838; -.
DR MetOSite; Q13838; -.
DR PhosphoSitePlus; Q13838; -.
DR SwissPalm; Q13838; -.
DR BioMuta; DDX39B; -.
DR DMDM; 2500529; -.
DR EPD; Q13838; -.
DR jPOST; Q13838; -.
DR MassIVE; Q13838; -.
DR MaxQB; Q13838; -.
DR PaxDb; Q13838; -.
DR PeptideAtlas; Q13838; -.
DR PRIDE; Q13838; -.
DR ProteomicsDB; 59701; -. [Q13838-1]
DR ProteomicsDB; 59702; -. [Q13838-2]
DR Antibodypedia; 27068; 364 antibodies from 28 providers.
DR DNASU; 7919; -.
DR Ensembl; ENST00000383508.6; ENSP00000373000.2; ENSG00000215425.11. [Q13838-1]
DR Ensembl; ENST00000396172.6; ENSP00000379475.1; ENSG00000198563.14. [Q13838-1]
DR Ensembl; ENST00000400295.5; ENSP00000383151.1; ENSG00000215425.11. [Q13838-1]
DR Ensembl; ENST00000400296.5; ENSP00000383152.1; ENSG00000215425.11. [Q13838-1]
DR Ensembl; ENST00000412106.5; ENSP00000393712.1; ENSG00000225073.10. [Q13838-1]
DR Ensembl; ENST00000412330.5; ENSP00000398775.1; ENSG00000225859.10. [Q13838-1]
DR Ensembl; ENST00000413678.5; ENSP00000391463.1; ENSG00000229496.10. [Q13838-1]
DR Ensembl; ENST00000414440.5; ENSP00000411853.1; ENSG00000229496.10. [Q13838-1]
DR Ensembl; ENST00000415689.5; ENSP00000390999.1; ENSG00000225073.10. [Q13838-1]
DR Ensembl; ENST00000416863.5; ENSP00000407419.1; ENSG00000229496.10. [Q13838-1]
DR Ensembl; ENST00000430784.5; ENSP00000399030.1; ENSG00000235439.10. [Q13838-1]
DR Ensembl; ENST00000431360.5; ENSP00000404695.1; ENSG00000235439.10. [Q13838-1]
DR Ensembl; ENST00000441425.5; ENSP00000388880.1; ENSG00000230624.10. [Q13838-1]
DR Ensembl; ENST00000445218.5; ENSP00000411136.1; ENSG00000225859.10. [Q13838-1]
DR Ensembl; ENST00000448296.5; ENSP00000405560.1; ENSG00000225859.10. [Q13838-1]
DR Ensembl; ENST00000453138.5; ENSP00000387994.1; ENSG00000230624.10. [Q13838-1]
DR Ensembl; ENST00000456476.5; ENSP00000400326.1; ENSG00000225073.10. [Q13838-1]
DR Ensembl; ENST00000456666.5; ENSP00000394160.1; ENSG00000230624.10. [Q13838-1]
DR Ensembl; ENST00000458640.5; ENSP00000416269.1; ENSG00000198563.14. [Q13838-1]
DR GeneID; 7919; -.
DR KEGG; hsa:7919; -.
DR MANE-Select; ENST00000396172.6; ENSP00000379475.1; NM_004640.7; NP_004631.1.
DR UCSC; uc003ntt.4; human. [Q13838-1]
DR CTD; 7919; -.
DR DisGeNET; 7919; -.
DR GeneCards; DDX39B; -.
DR HGNC; HGNC:13917; DDX39B.
DR HPA; ENSG00000198563; Low tissue specificity.
DR MIM; 142560; gene.
DR neXtProt; NX_Q13838; -.
DR OpenTargets; ENSG00000198563; -.
DR PharmGKB; PA25262; -.
DR VEuPathDB; HostDB:ENSG00000198563; -.
DR eggNOG; KOG0329; Eukaryota.
DR GeneTree; ENSGT00940000160110; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q13838; -.
DR OMA; IKPICRK; -.
DR PhylomeDB; Q13838; -.
DR TreeFam; TF300442; -.
DR PathwayCommons; Q13838; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR SABIO-RK; Q13838; -.
DR SignaLink; Q13838; -.
DR SIGNOR; Q13838; -.
DR BioGRID-ORCS; 7919; 440 hits in 1090 CRISPR screens.
DR EvolutionaryTrace; Q13838; -.
DR GeneWiki; BAT1; -.
DR GenomeRNAi; 7919; -.
DR Pharos; Q13838; Tbio.
DR PRO; PR:Q13838; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q13838; protein.
DR Bgee; ENSG00000198563; Expressed in granulocyte and 177 other tissues.
DR ExpressionAtlas; Q13838; baseline and differential.
DR Genevisible; Q13838; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IDA:BHF-UCL.
DR GO; GO:0000346; C:transcription export complex; IDA:UniProtKB.
DR GO; GO:0005687; C:U4 snRNP; IDA:BHF-UCL.
DR GO; GO:0005688; C:U6 snRNP; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; EXP:Reactome.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:UniProtKB.
DR GO; GO:0043008; F:ATP-dependent protein binding; IDA:BHF-UCL.
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; IDA:UniProtKB.
DR GO; GO:0030621; F:U4 snRNA binding; IDA:BHF-UCL.
DR GO; GO:0017070; F:U6 snRNA binding; IDA:BHF-UCL.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IGI:UniProtKB.
DR GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IMP:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IMP:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
DR GO; GO:0010501; P:RNA secondary structure unwinding; IDA:BHF-UCL.
DR GO; GO:0008380; P:RNA splicing; IDA:BHF-UCL.
DR GO; GO:0000245; P:spliceosomal complex assembly; IDA:BHF-UCL.
DR GO; GO:0046784; P:viral mRNA export from host cell nucleus; IDA:UniProtKB.
DR DisProt; DP02724; -.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Helicase; Hydrolase; Isopeptide bond; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Spliceosome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..428
FT /note="Spliceosome RNA helicase DDX39B"
FT /id="PRO_0000055071"
FT DOMAIN 76..249
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 261..422
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..73
FT /note="Q motif"
FT MOTIF 196..199
FT /note="DECD box"
FT COMPBIAS 1..22
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 36
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 172
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 114
FT /note="V -> VYLGRVLGRGFWLGLV (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026347"
FT MUTAGEN 94..96
FT /note="GKT->AAA: Loss of ATPase and helicase activity."
FT /evidence="ECO:0000269|PubMed:17562711"
FT MUTAGEN 95
FT /note="K->A: Loss of ATPase and helicase activity."
FT /evidence="ECO:0000269|PubMed:17562711,
FT ECO:0000269|PubMed:17984224"
FT MUTAGEN 197
FT /note="E->A: Loss of ATPase and helicase activity."
FT /evidence="ECO:0000269|PubMed:17562711"
FT MUTAGEN 198
FT /note="C->A: No effect on ATPase activity."
FT /evidence="ECO:0000269|PubMed:15585580"
FT MUTAGEN 199
FT /note="D->A: Increased ATPase activity and loss of helicase
FT activity."
FT /evidence="ECO:0000269|PubMed:17562711"
FT MUTAGEN 228..230
FT /note="SAT->AAA: Decreased ATPase activity and loss of
FT helicase activity."
FT /evidence="ECO:0000269|PubMed:17562711"
FT CONFLICT 289
FT /note="Q -> R (in Ref. 3; BAD96632)"
FT /evidence="ECO:0000305"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1XTI"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:1T6N"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:1T6N"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1T6N"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:1T6N"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1T6N"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:1T6N"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1T6N"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1T6N"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:1T6N"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:1T6N"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:1T6N"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1XTJ"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1T6N"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:1T6N"
FT HELIX 205..216
FT /evidence="ECO:0007829|PDB:1T6N"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:1T6N"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1T6N"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:1T6N"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1T6N"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:1T5I"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1T5I"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:1T5I"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:1T5I"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:1T5I"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1T5I"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1XTK"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:1T5I"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1XTJ"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:1T5I"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1T5I"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:1T5I"
FT HELIX 368..378
FT /evidence="ECO:0007829|PDB:1T5I"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:1T5I"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:1T5I"
FT HELIX 394..407
FT /evidence="ECO:0007829|PDB:1T5I"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:1T5I"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:1XTJ"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:1XTI"
SQ SEQUENCE 428 AA; 48991 MW; 7A55167BF576FB6F CRC64;
MAENDVDNEL LDYEDDEVET AAGGDGAEAP AKKDVKGSYV SIHSSGFRDF LLKPELLRAI
VDCGFEHPSE VQHECIPQAI LGMDVLCQAK SGMGKTAVFV LATLQQLEPV TGQVSVLVMC
HTRELAFQIS KEYERFSKYM PNVKVAVFFG GLSIKKDEEV LKKNCPHIVV GTPGRILALA
RNKSLNLKHI KHFILDECDK MLEQLDMRRD VQEIFRMTPH EKQVMMFSAT LSKEIRPVCR
KFMQDPMEIF VDDETKLTLH GLQQYYVKLK DNEKNRKLFD LLDVLEFNQV VIFVKSVQRC
IALAQLLVEQ NFPAIAIHRG MPQEERLSRY QQFKDFQRRI LVATNLFGRG MDIERVNIAF
NYDMPEDSDT YLHRVARAGR FGTKGLAITF VSDENDAKIL NDVQDRFEVN ISELPDEIDI
SSYIEQTR
