U5S1_HUMAN
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 03-AUG-2022, entry version 235.
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 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 [22]
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 [23]
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 [24]
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 [25]
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 [26] {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 [27] {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 [28] {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 [29] {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 [30] {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 [31] {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 [32] {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 [33] {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 [34] {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 [35]
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).
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). Component of the U5 snRNP and the
CC U4/U6-U5 tri-snRNP complex, a building block of the spliceosome
CC (PubMed:16723661). {ECO:0000269|PubMed:16723661,
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 -!- 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). Interacts with
CC ERBB4 and PRPF8. Interacts with PIH1D1 (PubMed:24656813). Interacts
CC with RPAP3 and URI1 in a ZNHIT2-dependent manner (PubMed:28561026).
CC Interacts with NRDE2 (PubMed:30538148). Interacts with FAM50A
CC (PubMed:32703943). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:20858735,
CC ECO:0000269|PubMed:24656813, ECO:0000269|PubMed:26912367,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:28561026, 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:30538148, ECO:0000269|PubMed:30705154,
CC ECO:0000269|PubMed:32703943, 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 ---------------------------------------------------------------------------
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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 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 AlphaFoldDB; Q15029; -.
DR SMR; Q15029; -.
DR BioGRID; 114749; 1391.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; Q15029; -.
DR IntAct; Q15029; 94.
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; Q15029; -.
DR PeptideAtlas; Q15029; -.
DR PRIDE; Q15029; -.
DR ProteomicsDB; 4423; -.
DR ProteomicsDB; 60379; -. [Q15029-1]
DR Antibodypedia; 17535; 248 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 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; GPDEMGP; -.
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 BioGRID-ORCS; 9343; 790 hits in 1081 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 179 other tissues.
DR ExpressionAtlas; Q15029; baseline and differential.
DR Genevisible; Q15029; HS.
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:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
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; IEA:InterPro.
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; cd04167; Snu114p; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
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
