GenomeNet

Database: UniProt
Entry: Q13838
LinkDB: Q13838
Original site: Q13838 
ID   DX39B_HUMAN             Reviewed;         428 AA.
AC   Q13838; B0S8C0; O43496; Q0EFA1; Q2L6F9; Q53GL9; Q5RJ64; Q5RJ66;
AC   Q5ST94; Q5STB4; Q5STB5; Q5STB7; Q5STB8; Q5STU4; Q5STU5; Q5STU6;
AC   Q5STU8; Q71V76;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-OCT-2019, entry version 201.
DE   RecName: Full=Spliceosome RNA helicase DDX39B;
DE            EC=3.6.4.13;
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; Synonyms=BAT1, UAP56;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   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.,
RA   Meyer A., Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K.,
RA   Gojobori T., 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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RT   snRNP-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.,
RA   Mann M., Reed R.;
RT   "Pre-mRNA splicing and mRNA export linked by direct interactions
RT   between 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
RT   human MHC 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.,
RA   Klein-Szanto A.J., Cooch N.S., Godwin A.K., Shiekhattar R.;
RT   "Linking transcriptional elongation and messenger RNA export to
RT   metastatic 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,
RP   AND 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
RT   physically 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
RT   with DEXD/H-Box RNA helicase UAP56 to promote cytoplasmic accumulation
RT   of unspliced RNA.";
RL   Mol. Cell. Biol. 26:1631-1643(2006).
RN   [18]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP   94-GLY--THR-96; 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
RT   UAP56, 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
RP   OF 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
RT   mRNAs by RNA helicase UAP56.";
RL   Mol. Cell. Biol. 28:601-608(2008).
RN   [20]
RP   FUNCTION OF THE TREX COMPLEX.
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
RT   virus 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
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a 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,
RT   requires 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
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., 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.,
RA   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation 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.,
RA   Buerckstuemmer T., 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.,
RA   Pavlovic J.;
RT   "Interferon-induced antiviral protein MxA interacts with the cellular
RT   RNA 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
RT   cells 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
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., 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
RT   an 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,
RP   AND 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [36]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND IDENTIFICATION BY
RP   MASS 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
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and 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.,
RA   Dickman M.J., 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
RP   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-
RT   modification 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
RT   factor 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
CC       mRNA. Assembling component of the TREX complex which is thought to
CC       couple mRNA transcription, processing and nuclear export, and
CC       specifically associates with spliced mRNA and not with unspliced
CC       pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-
CC       independent mechanism, binds to mRNA upstream of the exon-junction
CC       complex (EJC) and is recruited in a splicing- and cap-dependent
CC       manner to a region near the 5' end of the mRNA where it functions
CC       in mRNA export to the cytoplasm via the TAP/NFX1 pathway. May
CC       undergo several rounds of ATP hydrolysis during assembly of TREX
CC       to drive subsequent loading of components such as ALYREF/THOC and
CC       CHTOP onto mRNA. The TREX complex is essential for the export of
CC       Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs
CC       and infectious virus production. 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
CC       to recruit export adapter ALYREF/THOC4 to intronless mRNA; its
CC       ATPase activity is cooperatively stimulated by RNA and
CC       ALYREF/THOC4 and ATP hydrolysis is thought to trigger the
CC       dissociation from RNA to allow the association of ALYREF/THOC4 and
CC       the NXF1-NXT1 heterodimer. Involved in transcription elongation
CC       and genome stability.
CC   -!- FUNCTION: Splice factor that is required for the first ATP-
CC       dependent step in spliceosome assembly and for the interaction of
CC       U2 snRNP with the branchpoint. Has both RNA-stimulated ATP
CC       binding/hydrolysis activity and ATP-dependent RNA unwinding
CC       activity. Even with the stimulation of RNA, the ATPase activity is
CC       weak. Can only hydrolyze ATP but not other NTPs. The RNA
CC       stimulation of ATPase activity does not have a strong preference
CC       for the sequence and length of the RNA. However, ssRNA stimulates
CC       the ATPase activity much more strongly than dsRNA. Can unwind 5'
CC       or 3' overhangs or blunt end RNA duplexes in vitro. The ATPase and
CC       helicase activities are not influenced by U2AF2; the effect of
CC       ALYREF/THOC4 is reported conflictingly with [PubMed:23299939]
CC       reporting a stimulatory effect.
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. Component of the
CC       transcription/export (TREX) complex at least composed of
CC       ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex;
CC       TREX seems to have dynamic structure involving ATP-dependent
CC       remodeling; in the complex bridges ALYREF/THOC4 and the THO
CC       complex, and, in a ATP-dependent manner, ALYREF/THOC4 and
CC       SARNP/CIP29. Component of the spliceosome. Interacts directly with
CC       U2AF2. Interacts with RBM8A, RNPS1 and SRRM1, FYTTD1/UIF, THOC1,
CC       MX1 and POLDIP3. Interacts with human cytomegalovirus/HHV-5
CC       protein UL69. Interacts with LUZP4. {ECO:0000269|PubMed:11675789,
CC       ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:14667819,
CC       ECO:0000269|PubMed:15585580, ECO:0000269|PubMed:15833825,
CC       ECO:0000269|PubMed:15870275, ECO:0000269|PubMed:15998806,
CC       ECO:0000269|PubMed:16478985, 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   -!- INTERACTION:
CC       Self; NbExp=9; IntAct=EBI-348622, EBI-348622;
CC       Q86V81:ALYREF; NbExp=4; IntAct=EBI-348622, EBI-347640;
CC       Q9Y3Y2:CHTOP; NbExp=7; IntAct=EBI-348622, EBI-347794;
CC       O00148:DDX39A; NbExp=9; IntAct=EBI-348622, EBI-348253;
CC       P78317:RNF4; NbExp=4; IntAct=EBI-348622, EBI-2340927;
CC       P82979:SARNP; NbExp=5; IntAct=EBI-348622, EBI-347495;
CC       O00560:SDCBP; NbExp=4; IntAct=EBI-348622, EBI-727004;
CC       P26368-2:U2AF2; NbExp=4; IntAct=EBI-348622, EBI-11097439;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm.
CC       Note=Can translocate to the cytoplasm in the presence of MX1. TREX
CC       complex assembly seems to occur in regions surrounding nuclear
CC       speckles known 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         Note=No experimental confirmation available.;
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
CC       subfamily. {ECO:0000305}.
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   PDBsum; 1T5I; -.
DR   PDBsum; 1T6N; -.
DR   PDBsum; 1XTI; -.
DR   PDBsum; 1XTJ; -.
DR   PDBsum; 1XTK; -.
DR   SMR; Q13838; -.
DR   BioGrid; 113649; 204.
DR   CORUM; Q13838; -.
DR   IntAct; Q13838; 67.
DR   MINT; Q13838; -.
DR   STRING; 9606.ENSP00000379475; -.
DR   DrugBank; DB11638; Artenimol.
DR   DrugBank; DB02325; Isopropyl alcohol.
DR   TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR   iPTMnet; 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   DNASU; 7919; -.
DR   Ensembl; ENST00000383508; ENSP00000373000; ENSG00000215425. [Q13838-1]
DR   Ensembl; ENST00000396172; ENSP00000379475; ENSG00000198563. [Q13838-1]
DR   Ensembl; ENST00000400295; ENSP00000383151; ENSG00000215425. [Q13838-1]
DR   Ensembl; ENST00000400296; ENSP00000383152; ENSG00000215425. [Q13838-1]
DR   Ensembl; ENST00000412106; ENSP00000393712; ENSG00000225073. [Q13838-1]
DR   Ensembl; ENST00000412330; ENSP00000398775; ENSG00000225859. [Q13838-1]
DR   Ensembl; ENST00000413678; ENSP00000391463; ENSG00000229496. [Q13838-1]
DR   Ensembl; ENST00000414440; ENSP00000411853; ENSG00000229496. [Q13838-1]
DR   Ensembl; ENST00000415689; ENSP00000390999; ENSG00000225073. [Q13838-1]
DR   Ensembl; ENST00000416863; ENSP00000407419; ENSG00000229496. [Q13838-1]
DR   Ensembl; ENST00000430784; ENSP00000399030; ENSG00000235439. [Q13838-1]
DR   Ensembl; ENST00000431360; ENSP00000404695; ENSG00000235439. [Q13838-1]
DR   Ensembl; ENST00000441425; ENSP00000388880; ENSG00000230624. [Q13838-1]
DR   Ensembl; ENST00000445218; ENSP00000411136; ENSG00000225859. [Q13838-1]
DR   Ensembl; ENST00000448296; ENSP00000405560; ENSG00000225859. [Q13838-1]
DR   Ensembl; ENST00000453138; ENSP00000387994; ENSG00000230624. [Q13838-1]
DR   Ensembl; ENST00000456476; ENSP00000400326; ENSG00000225073. [Q13838-1]
DR   Ensembl; ENST00000456666; ENSP00000394160; ENSG00000230624. [Q13838-1]
DR   Ensembl; ENST00000458640; ENSP00000416269; ENSG00000198563. [Q13838-1]
DR   GeneID; 7919; -.
DR   KEGG; hsa:7919; -.
DR   UCSC; uc003ntt.4; human. [Q13838-1]
DR   CTD; 7919; -.
DR   DisGeNET; 7919; -.
DR   GeneCards; DDX39B; -.
DR   HGNC; HGNC:13917; DDX39B.
DR   HPA; CAB034012; -.
DR   HPA; HPA055334; -.
DR   HPA; HPA058450; -.
DR   MIM; 142560; gene.
DR   neXtProt; NX_Q13838; -.
DR   OpenTargets; ENSG00000198563; -.
DR   PharmGKB; PA25262; -.
DR   eggNOG; KOG0329; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   GeneTree; ENSGT00940000160110; -.
DR   InParanoid; Q13838; -.
DR   KO; K12812; -.
DR   OMA; VCADEAP; -.
DR   OrthoDB; 779000at2759; -.
DR   PhylomeDB; Q13838; -.
DR   TreeFam; TF300442; -.
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   EvolutionaryTrace; Q13838; -.
DR   GeneWiki; BAT1; -.
DR   GenomeRNAi; 7919; -.
DR   Pharos; Q13838; -.
DR   PRO; PR:Q13838; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000198563; Expressed in 90 organ(s), highest expression level in left lobe of thyroid gland.
DR   ExpressionAtlas; Q13838; baseline and differential.
DR   Genevisible; Q13838; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043008; F:ATP-dependent protein binding; IDA:BHF-UCL.
DR   GO; GO:0016887; F:ATPase activity; EXP:Reactome.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR   GO; GO:0008186; F:RNA-dependent ATPase 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:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
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:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
DR   GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IMP:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR   GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
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   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;
KW   Complete proteome; Cytoplasm; Helicase; Hydrolase; Isopeptide bond;
KW   mRNA processing; mRNA splicing; mRNA transport; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Spliceosome;
KW   Transport; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:19413330,
FT                                ECO:0000244|PubMed:22223895}.
FT   CHAIN         2    428       Spliceosome RNA helicase DDX39B.
FT                                /FTId=PRO_0000055071.
FT   DOMAIN       76    249       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      261    422       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      89     96       ATP.
FT   MOTIF        45     73       Q motif.
FT   MOTIF       196    199       DECD box.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:19413330,
FT                                ECO:0000244|PubMed:22223895}.
FT   MOD_RES      36     36       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES      38     38       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES      41     41       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     172    172       Phosphothreonine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   CROSSLNK     36     36       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ     114    114       V -> VYLGRVLGRGFWLGLV (in isoform 2).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_026347.
FT   MUTAGEN      94     96       GKT->AAA: Loss of ATPase and helicase
FT                                activity. {ECO:0000269|PubMed:17562711}.
FT   MUTAGEN      95     95       K->A: Loss of ATPase and helicase
FT                                activity. {ECO:0000269|PubMed:17562711,
FT                                ECO:0000269|PubMed:17984224}.
FT   MUTAGEN     197    197       E->A: Loss of ATPase and helicase
FT                                activity. {ECO:0000269|PubMed:17562711}.
FT   MUTAGEN     198    198       C->A: No effect on ATPase activity.
FT                                {ECO:0000269|PubMed:15585580}.
FT   MUTAGEN     199    199       D->A: Increased ATPase activity and loss
FT                                of helicase activity.
FT                                {ECO:0000269|PubMed:17562711}.
FT   MUTAGEN     228    230       SAT->AAA: Decreased ATPase activity and
FT                                loss of helicase activity.
FT                                {ECO:0000269|PubMed:17562711}.
FT   CONFLICT    289    289       Q -> R (in Ref. 3; BAD96632).
FT                                {ECO:0000305}.
FT   HELIX        47     50       {ECO:0000244|PDB:1XTI}.
FT   HELIX        54     62       {ECO:0000244|PDB:1T6N}.
FT   HELIX        70     80       {ECO:0000244|PDB:1T6N}.
FT   STRAND       85     88       {ECO:0000244|PDB:1T6N}.
FT   HELIX        95    106       {ECO:0000244|PDB:1T6N}.
FT   STRAND      116    119       {ECO:0000244|PDB:1T6N}.
FT   HELIX       123    136       {ECO:0000244|PDB:1T6N}.
FT   TURN        137    139       {ECO:0000244|PDB:1T6N}.
FT   STRAND      145    149       {ECO:0000244|PDB:1T6N}.
FT   HELIX       154    163       {ECO:0000244|PDB:1T6N}.
FT   STRAND      167    171       {ECO:0000244|PDB:1T6N}.
FT   HELIX       173    181       {ECO:0000244|PDB:1T6N}.
FT   STRAND      183    185       {ECO:0000244|PDB:1XTJ}.
FT   STRAND      192    197       {ECO:0000244|PDB:1T6N}.
FT   HELIX       198    202       {ECO:0000244|PDB:1T6N}.
FT   HELIX       205    216       {ECO:0000244|PDB:1T6N}.
FT   STRAND      220    229       {ECO:0000244|PDB:1T6N}.
FT   TURN        233    235       {ECO:0000244|PDB:1T6N}.
FT   HELIX       236    240       {ECO:0000244|PDB:1T6N}.
FT   STRAND      247    250       {ECO:0000244|PDB:1T6N}.
FT   STRAND      263    268       {ECO:0000244|PDB:1T5I}.
FT   HELIX       271    273       {ECO:0000244|PDB:1T5I}.
FT   HELIX       274    284       {ECO:0000244|PDB:1T5I}.
FT   STRAND      288    293       {ECO:0000244|PDB:1T5I}.
FT   HELIX       297    309       {ECO:0000244|PDB:1T5I}.
FT   STRAND      314    317       {ECO:0000244|PDB:1T5I}.
FT   STRAND      319    321       {ECO:0000244|PDB:1XTK}.
FT   HELIX       323    334       {ECO:0000244|PDB:1T5I}.
FT   STRAND      335    337       {ECO:0000244|PDB:1XTJ}.
FT   STRAND      339    345       {ECO:0000244|PDB:1T5I}.
FT   HELIX       353    355       {ECO:0000244|PDB:1T5I}.
FT   STRAND      357    363       {ECO:0000244|PDB:1T5I}.
FT   HELIX       368    378       {ECO:0000244|PDB:1T5I}.
FT   HELIX       380    382       {ECO:0000244|PDB:1T5I}.
FT   STRAND      386    391       {ECO:0000244|PDB:1T5I}.
FT   HELIX       394    407       {ECO:0000244|PDB:1T5I}.
FT   STRAND      411    413       {ECO:0000244|PDB:1T5I}.
FT   STRAND      417    419       {ECO:0000244|PDB:1XTJ}.
FT   HELIX       420    422       {ECO:0000244|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
//
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