GenomeNet

Database: UniProt
Entry: Q15029
LinkDB: Q15029
Original site: Q15029 
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   29-SEP-2021, entry version 232.
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};
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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   SMR; Q15029; -.
DR   BioGRID; 114749; 1372.
DR   CORUM; Q15029; -.
DR   IntAct; Q15029; 89.
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; 240 antibodies.
DR   DNASU; 9343; -.
DR   Ensembl; ENST00000402521; ENSP00000385873; ENSG00000108883. [Q15029-2]
DR   Ensembl; ENST00000426333; ENSP00000392094; ENSG00000108883. [Q15029-1]
DR   Ensembl; ENST00000591382; ENSP00000467805; ENSG00000108883. [Q15029-1]
DR   Ensembl; ENST00000592576; ENSP00000465058; ENSG00000108883. [Q15029-3]
DR   GeneID; 9343; -.
DR   KEGG; hsa:9343; -.
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; WGDIFYN; -.
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   BioGRID-ORCS; 9343; 783 hits in 1022 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 skeletal muscle tissue and 210 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; 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:0035690; P:cellular response to drug; 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; Isopeptide bond; Mental retardation; 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   NP_BIND         136..143
FT                   /note="GTP"
FT                   /evidence="ECO:0000255"
FT   NP_BIND         204..208
FT                   /note="GTP"
FT                   /evidence="ECO:0000255"
FT   NP_BIND         258..261
FT                   /note="GTP"
FT                   /evidence="ECO:0000255"
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   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   TURN            160..163
FT                   /evidence="ECO:0007829|PDB:6ICZ"
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:6ID0"
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:6ICZ"
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:6FF4"
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   STRAND          512..520
FT                   /evidence="ECO:0007829|PDB:6FF4"
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:6ICZ"
FT   STRAND          588..596
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           597..599
FT                   /evidence="ECO:0007829|PDB:6ID0"
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   STRAND          949..953
FT                   /evidence="ECO:0007829|PDB:6FF4"
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
//
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