ID U5S1_HUMAN Reviewed; 972 AA. AC Q15029; B4DK30; B4DMC0; D3DX58; K7EJ81; Q9BUR0; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 244. DE RecName: Full=116 kDa U5 small nuclear ribonucleoprotein component; DE AltName: Full=Elongation factor Tu GTP-binding domain-containing protein 2; DE AltName: Full=SNU114 homolog; DE Short=hSNU114; DE AltName: Full=U5 snRNP-specific protein, 116 kDa; DE Short=U5-116 kDa; GN Name=EFTUD2; Synonyms=KIAA0031, SNRP116; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., RA Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. The RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of RT randomly sampled cDNA clones from human immature myeloid cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Thalamus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] 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 [6] RP CHARACTERIZATION. RX PubMed=9233818; DOI=10.1093/emboj/16.13.4092; RA Fabrizio P., Laggerbauer B., Lauber J., Lane W.S., Luehrmann R.; RT "An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding RT factor closely related to the ribosomal translocase EF-2."; RL EMBO J. 16:4092-4106(1997). RN [7] RP INTERACTION WITH PRPF8. RX PubMed=9774689; DOI=10.1128/mcb.18.11.6756; RA Achsel T., Ahrens K., Brahms H., Teigelkamp S., Luehrmann R.; RT "The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with RT several U5-specific proteins, including an RNA unwindase, a homologue of RT ribosomal elongation factor EF-2, and a novel WD-40 protein."; RL Mol. Cell. Biol. 18:6756-6766(1998). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL RP C COMPLEX. 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP SUBUNIT. RX PubMed=16723661; DOI=10.1261/rna.55406; RA Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.; RT "The network of protein-protein interactions within the human U4/U6.U5 tri- RT snRNP."; RL RNA 12:1418-1430(2006). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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., 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, AND RP SUBCELLULAR LOCATION. RX PubMed=20858735; DOI=10.1158/1541-7786.mcr-10-0042; RA Gilmore-Hebert M., Ramabhadran R., Stern D.F.; RT "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage RT response pathways."; RL Mol. Cancer Res. 8:1388-1398(2010). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-19, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [15] 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 [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-19, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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., 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 [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [19] RP INTERACTION WITH PIH1D1. RX PubMed=24656813; DOI=10.1016/j.celrep.2014.03.013; RA Horejsi Z., Stach L., Flower T.G., Joshi D., Flynn H., Skehel J.M., RA O'Reilly N.J., Ogrodowicz R.W., Smerdon S.J., Boulton S.J.; RT "Phosphorylation-dependent PIH1D1 interactions define substrate specificity RT of the R2TP cochaperone complex."; RL Cell Rep. 7:19-26(2014). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND THR-86, AND 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 [21] RP FUNCTION, AND INTERACTION WITH UBL5. RX PubMed=25092792; DOI=10.15252/embr.201438679; RA Oka Y., Varmark H., Vitting-Seerup K., Beli P., Waage J., Hakobyan A., RA Mistrik M., Choudhary C., Rohde M., Bekker-Jensen S., Mailand N.; RT "UBL5 is essential for pre-mRNA splicing and sister chromatid cohesion in RT human cells."; RL EMBO Rep. 15:956-964(2014). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [23] RP INTERACTION WITH RPAP3 AND URI1. RX PubMed=28561026; DOI=10.1038/ncomms15615; RA Cloutier P., Poitras C., Durand M., Hekmat O., Fiola-Masson E., RA Bouchard A., Faubert D., Chabot B., Coulombe B.; RT "R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 RT to regulate assembly of U5 small nuclear ribonucleoprotein."; RL Nat. Commun. 8:15615-15615(2017). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-64, 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 [25] RP INTERACTION WITH NRDE2. RX PubMed=30538148; DOI=10.1261/rna.069773.118; RA Jiao A.L., Perales R., Umbreit N.T., Haswell J.R., Piper M.E., Adams B.D., RA Pellman D., Kennedy S., Slack F.J.; RT "Human nuclear RNAi-defective 2 (NRDE2) is an essential RNA splicing RT factor."; RL RNA 25:352-363(2019). RN [26] RP INTERACTION WITH FAM50A. RX PubMed=32703943; DOI=10.1038/s41467-020-17452-6; RA Lee Y.R., Khan K., Armfield-Uhas K., Srikanth S., Thompson N.A., Pardo M., RA Yu L., Norris J.W., Peng Y., Gripp K.W., Aleck K.A., Li C., Spence E., RA Choi T.I., Kwon S.J., Park H.M., Yu D., Do Heo W., Mooney M.R., Baig S.M., RA Wentzensen I.M., Telegrafi A., McWalter K., Moreland T., Roadhouse C., RA Ramsey K., Lyons M.J., Skinner C., Alexov E., Katsanis N., Stevenson R.E., RA Choudhary J.S., Adams D.J., Kim C.H., Davis E.E., Schwartz C.E.; RT "Mutations in FAM50A suggest that Armfield XLID syndrome is a RT spliceosomopathy."; RL Nat. Commun. 11:3698-3698(2020). RN [27] {ECO:0007744|PDB:3JCR} RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), IDENTIFICATION BY MASS RP SPECTROMETRY, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=26912367; DOI=10.1126/science.aad2085; RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H., RA Luhrmann R., Stark H.; RT "Molecular architecture of the human U4/U6.U5 tri-snRNP."; RL Science 351:1416-1420(2016). RN [28] {ECO:0007744|PDB:5XJC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. 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 [29] {ECO:0007744|PDB:5O9Z} RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011; RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N., RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.; RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for RT Activation."; RL Cell 170:701-713(2017). RN [30] {ECO:0007744|PDB:5MQF} RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. 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). RN [31] {ECO:0007744|PDB:6FF4} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=29361316; DOI=10.1016/j.cell.2018.01.010; RA Haselbach D., Komarov I., Agafonov D.E., Hartmuth K., Graf B., Dybkov O., RA Urlaub H., Kastner B., Luhrmann R., Stark H.; RT "Structure and Conformational Dynamics of the Human Spliceosomal Bact RT Complex."; RL Cell 172:454-464(2018). RN [32] {ECO:0007744|PDB:6AH0, ECO:0007744|PDB:6AHD} RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=30315277; DOI=10.1038/s41422-018-0094-7; RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.; RT "Structures of the human pre-catalytic spliceosome and its precursor RT spliceosome."; RL Cell Res. 28:1129-1140(2018). RN [33] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57, ECO:0007744|PDB:5Z58} RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=29360106; DOI=10.1038/cr.2018.14; RA Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.; RT "Structure of the human activated spliceosome in three conformational RT states."; RL Cell Res. 28:307-322(2018). RN [34] {ECO:0007744|PDB:5YZG} RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=29301961; DOI=10.1126/science.aar6401; RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.; RT "Structure of a human catalytic step I spliceosome."; RL Science 359:537-545(2018). RN [35] {ECO:0007744|PDB:6QDV} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 56-955, FUNCTION, RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=30705154; DOI=10.1126/science.aaw5569; RA Fica S.M., Oubridge C., Wilkinson M.E., Newman A.J., Nagai K.; RT "A human postcatalytic spliceosome structure reveals essential roles of RT metazoan factors for exon ligation."; RL Science 363:710-714(2019). RN [36] RP VARIANTS MFDM TRP-262; ARG-476 AND ARG-637. RX PubMed=22305528; DOI=10.1016/j.ajhg.2011.12.023; RA Lines M.A., Huang L., Schwartzentruber J., Douglas S.L., Lynch D.C., RA Beaulieu C., Guion-Almeida M.L., Zechi-Ceide R.M., Gener B., RA Gillessen-Kaesbach G., Nava C., Baujat G., Horn D., Kini U., Caliebe A., RA Alanay Y., Utine G.E., Lev D., Kohlhase J., Grix A.W., Lohmann D.R., RA Hehr U., Bohm D., Majewski J., Bulman D.E., Wieczorek D., Boycott K.M.; RT "Haploinsufficiency of a spliceosomal GTPase encoded by EFTUD2 causes RT mandibulofacial dysostosis with microcephaly."; RL Am. J. Hum. Genet. 90:369-377(2012). RN [37] {ECO:0007744|PDB:7DVQ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), FUNCTION, AND SUBUNIT. RX PubMed=33509932; DOI=10.1126/science.abg0879; RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.; RT "Structure of the activated human minor spliceosome."; RL Science 371:0-0(2021). CC -!- FUNCTION: Required for pre-mRNA splicing as component of the CC spliceosome, including pre-catalytic, catalytic and post-catalytic CC spliceosomal complexes (PubMed:28502770, PubMed:28781166, CC PubMed:28076346, PubMed:29361316, PubMed:30315277, PubMed:29360106, CC PubMed:29301961, PubMed:30705154, PubMed:25092792). Component of the U5 CC snRNP and the U4/U6-U5 tri-snRNP complex, a building block of the CC spliceosome (PubMed:16723661). As a component of the minor spliceosome, CC involved in the splicing of U12-type introns in pre-mRNAs (Probable). CC {ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:25092792, CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:29301961, CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, CC ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30705154, CC ECO:0000305|PubMed:33509932}. CC -!- SUBUNIT: Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex, CC a building block of the spliceosome (PubMed:26912367, PubMed:16723661). CC The U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs CC and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, CC SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39 CC (PubMed:16723661, PubMed:26912367). Component of the pre-catalytic, CC catalytic and post-catalytic spliceosome complexes (PubMed:28502770, CC PubMed:28781166, PubMed:28076346, PubMed:29361316, PubMed:30315277, CC PubMed:29360106, PubMed:29301961, PubMed:30705154). Component of the CC minor spliceosome, which splices U12-type introns. Within this complex, CC interacts with CRIPT (PubMed:33509932). Interacts with ERBB4 and PRPF8. CC Interacts with PIH1D1 (PubMed:24656813). Interacts with RPAP3 and URI1 CC in a ZNHIT2-dependent manner (PubMed:28561026). Interacts with NRDE2 CC (PubMed:30538148). Interacts with FAM50A (PubMed:32703943). Interacts CC with UBL5 (PubMed:25092792). {ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:20858735, CC ECO:0000269|PubMed:24656813, ECO:0000269|PubMed:25092792, CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28561026, CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:29301961, CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, CC ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30538148, CC ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:32703943, CC ECO:0000269|PubMed:33509932, ECO:0000269|PubMed:9774689}. CC -!- INTERACTION: CC Q15029; P04792: HSPB1; NbExp=2; IntAct=EBI-357897, EBI-352682; CC Q15029; Q13123: IK; NbExp=2; IntAct=EBI-357897, EBI-713456; CC Q15029; P01106: MYC; NbExp=5; IntAct=EBI-357897, EBI-447544; CC Q15029; Q6P2Q9: PRPF8; NbExp=6; IntAct=EBI-357897, EBI-538479; CC Q15029; Q15427: SF3B4; NbExp=2; IntAct=EBI-357897, EBI-348469; CC Q15029; Q96DI7: SNRNP40; NbExp=2; IntAct=EBI-357897, EBI-538492; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20858735, CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277, CC ECO:0000269|PubMed:30705154}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q15029-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15029-2; Sequence=VSP_044282; CC Name=3; CC IsoId=Q15029-3; Sequence=VSP_055175; CC -!- DISEASE: Mandibulofacial dysostosis with microcephaly (MFDM) CC [MIM:610536]: A rare syndrome characterized by progressive CC microcephaly, midface and malar hypoplasia, micrognathia, microtia, CC dysplastic ears, preauricular skin tags, significant developmental CC delay, and speech delay. Many patients have major sequelae, including CC choanal atresia that results in respiratory difficulties, conductive CC hearing loss, and cleft palate. {ECO:0000269|PubMed:22305528}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-G/EF-2 CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA04699.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D21163; BAA04699.2; ALT_INIT; mRNA. DR EMBL; AK296367; BAG59042.1; -; mRNA. DR EMBL; AK297392; BAG59832.1; -; mRNA. DR EMBL; AK316098; BAH14469.1; -; mRNA. DR EMBL; AC015936; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471178; EAW51573.1; -; Genomic_DNA. DR EMBL; CH471178; EAW51574.1; -; Genomic_DNA. DR EMBL; BC002360; AAH02360.1; -; mRNA. DR CCDS; CCDS11489.1; -. [Q15029-1] DR CCDS; CCDS45707.1; -. [Q15029-2] DR CCDS; CCDS59295.1; -. [Q15029-3] DR RefSeq; NP_001136077.1; NM_001142605.1. [Q15029-2] DR RefSeq; NP_001245282.1; NM_001258353.1. [Q15029-1] DR RefSeq; NP_001245283.1; NM_001258354.1. [Q15029-3] DR RefSeq; NP_004238.3; NM_004247.3. [Q15029-1] DR PDB; 3JCR; EM; 7.00 A; B=1-972. DR PDB; 5MQF; EM; 5.90 A; B=1-972. DR PDB; 5O9Z; EM; 4.50 A; B=1-972. DR PDB; 5XJC; EM; 3.60 A; C=1-972. DR PDB; 5YZG; EM; 4.10 A; C=1-972. DR PDB; 5Z56; EM; 5.10 A; C=1-972. DR PDB; 5Z57; EM; 6.50 A; C=1-972. DR PDB; 5Z58; EM; 4.90 A; C=1-972. DR PDB; 6AH0; EM; 5.70 A; C=1-972. DR PDB; 6AHD; EM; 3.80 A; C=1-972. DR PDB; 6FF4; EM; 16.00 A; B=1-972. DR PDB; 6FF7; EM; 4.50 A; B=1-972. DR PDB; 6ICZ; EM; 3.00 A; C=1-972. DR PDB; 6ID0; EM; 2.90 A; C=1-972. DR PDB; 6ID1; EM; 2.86 A; C=1-972. DR PDB; 6QDV; EM; 3.30 A; C=56-955. DR PDB; 6QW6; EM; 2.92 A; 5C=104-956. DR PDB; 6QX9; EM; 3.28 A; 5C=104-957. DR PDB; 6ZYM; EM; 3.40 A; B=1-952. DR PDB; 7AAV; EM; 4.20 A; r=1-972. DR PDB; 7ABF; EM; 3.90 A; r=1-972. DR PDB; 7ABG; EM; 7.80 A; r=1-972. DR PDB; 7ABI; EM; 8.00 A; r=1-972. DR PDB; 7DVQ; EM; 2.89 A; C=1-972. DR PDB; 7QTT; EM; 3.10 A; b=1-972. DR PDB; 7W59; EM; 3.60 A; C=1-972. DR PDB; 7W5A; EM; 3.60 A; C=1-972. DR PDB; 7W5B; EM; 4.30 A; C=1-972. DR PDB; 8C6J; EM; 2.80 A; C=1-972. DR PDB; 8CH6; EM; 5.90 A; b=1-972. DR PDBsum; 3JCR; -. DR PDBsum; 5MQF; -. DR PDBsum; 5O9Z; -. DR PDBsum; 5XJC; -. DR PDBsum; 5YZG; -. DR PDBsum; 5Z56; -. DR PDBsum; 5Z57; -. DR PDBsum; 5Z58; -. DR PDBsum; 6AH0; -. DR PDBsum; 6AHD; -. DR PDBsum; 6FF4; -. DR PDBsum; 6FF7; -. DR PDBsum; 6ICZ; -. DR PDBsum; 6ID0; -. DR PDBsum; 6ID1; -. DR PDBsum; 6QDV; -. DR PDBsum; 6QW6; -. DR PDBsum; 6QX9; -. DR PDBsum; 6ZYM; -. DR PDBsum; 7AAV; -. DR PDBsum; 7ABF; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABI; -. DR PDBsum; 7DVQ; -. DR PDBsum; 7QTT; -. DR PDBsum; 7W59; -. DR PDBsum; 7W5A; -. DR PDBsum; 7W5B; -. DR PDBsum; 8C6J; -. DR PDBsum; 8CH6; -. DR AlphaFoldDB; Q15029; -. DR EMDB; EMD-11569; -. DR EMDB; EMD-11693; -. DR EMDB; EMD-11694; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-14146; -. DR EMDB; EMD-16452; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-30875; -. DR EMDB; EMD-32317; -. DR EMDB; EMD-32319; -. DR EMDB; EMD-32321; -. DR EMDB; EMD-3545; -. DR EMDB; EMD-3766; -. DR EMDB; EMD-4255; -. DR EMDB; EMD-4525; -. DR EMDB; EMD-4658; -. DR EMDB; EMD-4665; -. DR EMDB; EMD-6721; -. DR EMDB; EMD-6864; -. DR EMDB; EMD-6889; -. DR EMDB; EMD-6890; -. DR EMDB; EMD-6891; -. DR EMDB; EMD-9621; -. DR EMDB; EMD-9624; -. DR EMDB; EMD-9645; -. DR EMDB; EMD-9646; -. DR EMDB; EMD-9647; -. DR SMR; Q15029; -. DR BioGRID; 114749; 1442. DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex. DR CORUM; Q15029; -. DR IntAct; Q15029; 101. DR MINT; Q15029; -. DR STRING; 9606.ENSP00000392094; -. DR GlyGen; Q15029; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q15029; -. DR MetOSite; Q15029; -. DR PhosphoSitePlus; Q15029; -. DR SwissPalm; Q15029; -. DR BioMuta; EFTUD2; -. DR DMDM; 18202501; -. DR EPD; Q15029; -. DR jPOST; Q15029; -. DR MassIVE; Q15029; -. DR MaxQB; Q15029; -. DR PaxDb; 9606-ENSP00000392094; -. DR PeptideAtlas; Q15029; -. DR PRIDE; Q15029; -. DR ProteomicsDB; 4423; -. DR ProteomicsDB; 60379; -. [Q15029-1] DR Pumba; Q15029; -. DR Antibodypedia; 17535; 271 antibodies from 30 providers. DR DNASU; 9343; -. DR Ensembl; ENST00000402521.7; ENSP00000385873.2; ENSG00000108883.13. [Q15029-2] DR Ensembl; ENST00000426333.7; ENSP00000392094.1; ENSG00000108883.13. [Q15029-1] DR Ensembl; ENST00000591382.5; ENSP00000467805.1; ENSG00000108883.13. [Q15029-1] DR Ensembl; ENST00000592576.5; ENSP00000465058.1; ENSG00000108883.13. [Q15029-3] DR GeneID; 9343; -. DR KEGG; hsa:9343; -. DR MANE-Select; ENST00000426333.7; ENSP00000392094.1; NM_004247.4; NP_004238.3. DR UCSC; uc002ihn.3; human. [Q15029-1] DR AGR; HGNC:30858; -. DR CTD; 9343; -. DR DisGeNET; 9343; -. DR GeneCards; EFTUD2; -. DR GeneReviews; EFTUD2; -. DR HGNC; HGNC:30858; EFTUD2. DR HPA; ENSG00000108883; Low tissue specificity. DR MalaCards; EFTUD2; -. DR MIM; 603892; gene. DR MIM; 610536; phenotype. DR neXtProt; NX_Q15029; -. DR OpenTargets; ENSG00000108883; -. DR Orphanet; 79113; Mandibulofacial dysostosis-microcephaly syndrome. DR PharmGKB; PA142671915; -. DR VEuPathDB; HostDB:ENSG00000108883; -. DR eggNOG; KOG0468; Eukaryota. DR GeneTree; ENSGT00940000155685; -. DR HOGENOM; CLU_002794_11_2_1; -. DR InParanoid; Q15029; -. DR OMA; YIFRPIR; -. DR OrthoDB; 166721at2759; -. DR PhylomeDB; Q15029; -. DR TreeFam; TF105703; -. DR PathwayCommons; Q15029; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway. DR SignaLink; Q15029; -. DR SIGNOR; Q15029; -. DR BioGRID-ORCS; 9343; 822 hits in 1159 CRISPR screens. DR ChiTaRS; EFTUD2; human. DR GeneWiki; EFTUD2; -. DR GenomeRNAi; 9343; -. DR Pharos; Q15029; Tbio. DR PRO; PR:Q15029; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q15029; Protein. DR Bgee; ENSG00000108883; Expressed in bone marrow cell and 181 other cell types or tissues. DR ExpressionAtlas; Q15029; baseline and differential. DR GO; GO:0015030; C:Cajal body; IDA:BHF-UCL. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB. DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:CAFA. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0030623; F:U5 snRNA binding; IBA:GO_Central. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl. DR CDD; cd04098; eEF2_C_snRNP; 1. DR CDD; cd04090; EF2_II_snRNP; 1. DR CDD; cd01683; EF2_IV_snRNP; 1. DR CDD; cd16264; snRNP_III; 1. DR CDD; cd04167; Snu114p; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 1. DR InterPro; IPR041095; EFG_II. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR000640; EFG_V-like. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR031950; EFTUD2_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR044121; Snu114_GTP-bd. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV. DR InterPro; IPR035655; U5-116kDa_C. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR42908:SF6; 116 KDA U5 SMALL NUCLEAR RIBONUCLEOPROTEIN COMPONENT; 1. DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF14492; EFG_III; 1. DR Pfam; PF03764; EFG_IV; 1. DR Pfam; PF16004; EFTUD2; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SMART; SM00889; EFG_IV; 1. DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS51722; G_TR_2; 1. DR Genevisible; Q15029; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Disease variant; KW GTP-binding; Intellectual disability; Isopeptide bond; mRNA processing; KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Spliceosome; Ubl conjugation. FT CHAIN 1..972 FT /note="116 kDa U5 small nuclear ribonucleoprotein FT component" FT /id="PRO_0000091563" FT DOMAIN 127..409 FT /note="tr-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 1..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 14..49 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 136..143 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT BINDING 204..208 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT BINDING 258..261 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:22223895" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 86 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT CROSSLNK 64 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 64 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..35 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044282" FT VAR_SEQ 143..152 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055175" FT VARIANT 262 FT /note="R -> W (in MFDM; dbSNP:rs387906877)" FT /evidence="ECO:0000269|PubMed:22305528" FT /id="VAR_067580" FT VARIANT 476 FT /note="C -> R (in MFDM)" FT /evidence="ECO:0000269|PubMed:22305528" FT /id="VAR_067581" FT VARIANT 637 FT /note="L -> R (in MFDM; dbSNP:rs387906879)" FT /evidence="ECO:0000269|PubMed:22305528" FT /id="VAR_067582" FT VARIANT 773 FT /note="G -> V (in dbSNP:rs1056505)" FT /id="VAR_014931" FT CONFLICT 321 FT /note="G -> V (in Ref. 5; AAH02360)" FT /evidence="ECO:0000305" FT CONFLICT 619 FT /note="T -> S (in Ref. 2; BAG59832)" FT /evidence="ECO:0000305" FT CONFLICT 955 FT /note="D -> G (in Ref. 2; BAG59832)" FT /evidence="ECO:0000305" FT TURN 60..62 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 69..73 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 75..81 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:6ZYM" FT HELIX 117..123 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 126..141 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 142..153 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 174..177 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 185..190 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 198..204 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 212..221 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 223..230 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 231..233 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 237..248 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 252..258 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 261..264 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 265..267 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 271..292 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 302..305 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 307..310 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 312..315 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 320..330 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 336..341 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 343..346 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 351..354 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 355..360 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 361..364 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 368..386 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 388..391 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 392..396 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 397..400 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 407..409 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 412..424 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 428..435 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 440..444 FT /evidence="ECO:0007829|PDB:6ID0" FT HELIX 445..452 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 453..455 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 459..461 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 462..467 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 470..473 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 475..483 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 485..488 FT /evidence="ECO:0007829|PDB:6ICZ" FT STRAND 490..499 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 501..504 FT /evidence="ECO:0007829|PDB:6ZYM" FT STRAND 506..510 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 516..518 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 523..526 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 530..533 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 534..536 FT /evidence="ECO:0007829|PDB:6ID0" FT STRAND 538..540 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 542..544 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 549..554 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 556..558 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 560..562 FT /evidence="ECO:0007829|PDB:6ZYM" FT STRAND 563..566 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 568..570 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 588..596 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 597..599 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 600..613 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 618..621 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 623..625 FT /evidence="ECO:0007829|PDB:6ICZ" FT STRAND 627..633 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 634..646 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 653..655 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 663..666 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 674..677 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 679..681 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 684..690 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 694..700 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 701..705 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 707..709 FT /evidence="ECO:0007829|PDB:6ZYM" FT HELIX 711..722 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 726..729 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 737..740 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 742..747 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 752..754 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 756..776 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 778..780 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 786..795 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 801..803 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 804..821 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 825..838 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 840..851 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 852..854 FT /evidence="ECO:0007829|PDB:6FF4" FT STRAND 857..859 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 869..879 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 883..890 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 891..893 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 895..906 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 920..922 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 926..928 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 929..940 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 949..952 FT /evidence="ECO:0007829|PDB:7DVQ" SQ SEQUENCE 972 AA; 109436 MW; 862BD6CA7993F118 CRC64; MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEMDDDD DDDDVGDHDD DHPGMEVVLH EDKKYYPTAE EVYGPEVETI VQEEDTQPLT EPIIKPVKTK KFTLMEQTLP VTVYEMDFLA DLMDNSELIR NVTLCGHLHH GKTCFVDCLI EQTHPEIRKR YDQDLCYTDI LFTEQERGVG IKSTPVTVVL PDTKGKSYLF NIMDTPGHVN FSDEVTAGLR ISDGVVLFID AAEGVMLNTE RLIKHAVQER LAVTVCINKI DRLILELKLP PTDAYYKLRH IVDEVNGLIS MYSTDENLIL SPLLGNVCFS SSQYSICFTL GSFAKIYADT FGDINYQEFA KRLWGDIYFN PKTRKFTKKA PTSSSQRSFV EFILEPLYKI LAQVVGDVDT SLPRTLDELG IHLTKEELKL NIRPLLRLVC KKFFGEFTGF VDMCVQHIPS PKVGAKPKIE HTYTGGVDSD LGEAMSDCDP DGPLMCHTTK MYSTDDGVQF HAFGRVLSGT IHAGQPVKVL GENYTLEDEE DSQICTVGRL WISVARYHIE VNRVPAGNWV LIEGVDQPIV KTATITEPRG NEEAQIFRPL KFNTTSVIKI AVEPVNPSEL PKMLDGLRKV NKSYPSLTTK VEESGEHVIL GTGELYLDCV MHDLRKMYSE IDIKVADPVV TFCETVVETS SLKCFAETPN KKNKITMIAE PLEKGLAEDI ENEVVQITWN RKKLGEFFQT KYDWDLLAAR SIWAFGPDAT GPNILVDDTL PSEVDKALLG SVKDSIVQGF QWGTREGPLC DELIRNVKFK ILDAVVAQEP LHRGGGQIIP TARRVVYSAF LMATPRLMEP YYFVEVQAPA DCVSAVYTVL ARRRGHVTQD APIPGSPLYT IKAFIPAIDS FGFETDLRTH TQGQAFSLSV FHHWQIVPGD PLDKSIVIRP LEPQPAPHLA REFMIKTRRR KGLSEDVSIS KFFDDPMLLE LAKQDVVLNY PM //