PRP8_HUMAN
ID PRP8_HUMAN Reviewed; 2335 AA.
AC Q6P2Q9; O14547; O75965;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Pre-mRNA-processing-splicing factor 8;
DE AltName: Full=220 kDa U5 snRNP-specific protein;
DE AltName: Full=PRP8 homolog;
DE AltName: Full=Splicing factor Prp8;
DE AltName: Full=p220;
GN Name=PRPF8; Synonyms=PRPC8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, SUBUNIT, AND
RP IDENTIFICATION IN U2- AND U12-DEPENDENT SPLICEOSOME COMPLEXES.
RX PubMed=10411133; DOI=10.1017/s1355838299990520;
RA Luo H.R., Moreau G.A., Levin N., Moore M.J.;
RT "The human Prp8 protein is a component of both U2- and U12-dependent
RT spliceosomes.";
RL RNA 5:893-908(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS 68-GLU; LEU-874 AND HIS-1293.
RA Shimada Y., Fujiwara T., Kawai A., Shimizu F., Okuno S., Ozaki K.,
RA Takeda S., Watanabe T., Nagata M., Takahashi E.;
RT "Human homologue of Saccharomyces cerevisiae PRP8, pre-mRNA splicing
RT factor.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-227.
RC TISSUE=Testis;
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 [4]
RP PROTEIN SEQUENCE OF 2-8; 51-58; 218-227; 268-278; 421-428; 453-460;
RP 556-565; 610-623; 643-650; 677-702; 747-758; 822-833; 838-845; 988-995;
RP 999-1032; 1113-1131; 1142-1158; 1225-1231; 1246-1258; 1311-1320; 1345-1354;
RP 1371-1392; 1450-1459; 1464-1491; 1524-1532; 1571-1578; 1642-1649;
RP 1668-1678; 1724-1732; 1736-1744; 1814-1831; 1841-1859; 1902-1908;
RP 1926-1935; 1995-2031; 2035-2045; 2050-2070; 2087-2108; 2114-2121;
RP 2199-2210; 2230-2239; 2250-2266 AND 2288-2302, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP IDENTIFICATION IN U5 SNRNP COMPLEX.
RX PubMed=2532307; DOI=10.1038/342819a0;
RA Anderson G.J., Bach M., Luehrmann R., Beggs J.D.;
RT "Conservation between yeast and man of a protein associated with U5 small
RT nuclear ribonucleoprotein.";
RL Nature 342:819-821(1989).
RN [6]
RP IDENTIFICATION IN U5 SNRNP COMPLEX.
RX PubMed=2527369; DOI=10.1073/pnas.86.16.6038;
RA Bach M., Winkelmann G., Luehrmann R.;
RT "20S small nuclear ribonucleoprotein U5 shows a surprisingly complex
RT protein composition.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6038-6042(1989).
RN [7]
RP IDENTIFICATION IN U5 SNRNP; U5/4/6 SNRNP AND SPLICEOSOME COMPLEXES.
RX PubMed=2479028; DOI=10.1073/pnas.86.22.8742;
RA Pinto A.L., Steitz J.A.;
RT "The mammalian analogue of the yeast PRP8 splicing protein is present in
RT the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8742-8746(1989).
RN [8]
RP IDENTIFICATION IN SPLICEOSOME COMPLEX, AND INTERACTION WITH PRE-MRNA.
RX PubMed=2139226; DOI=10.1073/pnas.87.8.3082;
RA Garcia-Blanco M.A., Anderson G.J., Beggs J., Sharp P.A.;
RT "A mammalian protein of 220 kDa binds pre-mRNAs in the spliceosome: a
RT potential homologue of the yeast PRP8 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3082-3086(1990).
RN [9]
RP IDENTIFICATION IN U5 SNRNP COMPLEX, AND INTERACTION WITH U5 SNRNA.
RX PubMed=8702566; DOI=10.1074/jbc.271.31.19001;
RA Hinz M., Moore M.J., Bindereif A.;
RT "Domain analysis of human U5 RNA. Cap trimethylation, protein binding, and
RT spliceosome assembly.";
RL J. Biol. Chem. 271:19001-19007(1996).
RN [10]
RP INTERACTION WITH PRE-MRNA.
RX PubMed=8608445;
RA Reyes J.L., Kois P., Konforti B.B., Konarska M.M.;
RT "The canonical GU dinucleotide at the 5' splice site is recognized by p220
RT of the U5 snRNP within the spliceosome.";
RL RNA 2:213-225(1996).
RN [11]
RP IDENTIFICATION IN SPLICEOSOME COMPLEX, AND INTERACTION WITH PRE-MRNA.
RX PubMed=9303319; DOI=10.1093/emboj/16.15.4746;
RA Chiara M.D., Palandjian L., Feld Kramer R., Reed R.;
RT "Evidence that U5 snRNP recognizes the 3' splice site for catalytic step II
RT in mammals.";
RL EMBO J. 16:4746-4759(1997).
RN [12]
RP IDENTIFICATION IN U5 SNRP COMPLEX, AND INTERACTION WITH SNRP116 AND
RP SNRNP40.
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 [13]
RP INTERACTION WITH PRE-MRNA.
RX PubMed=10024169; DOI=10.1017/s1355838299981785;
RA Reyes J.L., Gustafson E.H., Luo H.R., Moore M.J., Konarska M.M.;
RT "The C-terminal region of hPrp8 interacts with the conserved GU
RT dinucleotide at the 5' splice site.";
RL RNA 5:167-179(1999).
RN [14]
RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC)
RP WITH SRRM1.
RX PubMed=10809668;
RA Le Hir H., Moore M.J., Maquat L.E.;
RT "Pre-mRNA splicing alters mRNP composition: evidence for stable association
RT of proteins at exon-exon junctions.";
RL Genes Dev. 14:1098-1108(2000).
RN [15]
RP INTERACTION WITH U5 SNRNA.
RX PubMed=11006293; DOI=10.1074/jbc.m007434200;
RA Urlaub H., Hartmuth K., Kostka S., Grelle G., Luehrmann R.;
RT "A general approach for identification of RNA-protein cross-linking sites
RT within native human spliceosomal small nuclear ribonucleoproteins (snRNPs).
RT Analysis of RNA-protein contacts in native U1 and U4/U6.U5 snRNPs.";
RL J. Biol. Chem. 275:41458-41468(2000).
RN [16]
RP INTERACTION WITH PRE-MRNA, AND IDENTIFICATION IN U5/4/6 SNRNP COMPLEX.
RX PubMed=10983979; DOI=10.1016/s1097-2765(00)00032-0;
RA Maroney P.A., Romfo C.M., Nilsen T.W.;
RT "Functional recognition of 5' splice site by U4/U6.U5 tri-snRNP defines a
RT novel ATP-dependent step in early spliceosome assembly.";
RL Mol. Cell 6:317-328(2000).
RN [17]
RP IDENTIFICATION IN U12-DEPENDENT SPLICEOSOME.
RX PubMed=11971955; DOI=10.1128/mcb.22.10.3219-3229.2002;
RA Schneider C., Will C.L., Makarova O.V., Makarov E.M., Luehrmann R.;
RT "Human U4/U6.U5 and U4atac/U6atac.U5 tri-snRNPs exhibit similar protein
RT compositions.";
RL Mol. Cell. Biol. 22:3219-3229(2002).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [19]
RP REVIEW.
RX PubMed=15840809; DOI=10.1261/rna.2220705;
RA Grainger R.J., Beggs J.D.;
RT "Prp8 protein: at the heart of the spliceosome.";
RL RNA 11:533-557(2005).
RN [20]
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 [21]
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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1463, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [26]
RP FUNCTION, AND INTERACTION WITH PRPF3.
RX PubMed=20595234; DOI=10.1101/gad.1925010;
RA Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D.,
RA Harper J.W., Elledge S.J., Kirschner M.W., Rape M.;
RT "The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control
RT reversible ubiquitination at the spliceosome.";
RL Genes Dev. 24:1434-1447(2010).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [28]
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 [29]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358, AND IDENTIFICATION BY
RP 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 [31]
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 [32]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-1425, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [33]
RP CRYSTALLIZATION, AND INTERACTION WITH AAR2.
RX PubMed=26527271; DOI=10.1107/s2053230x15019202;
RA Santos K., Preussner M., Heroven A.C., Weber G.;
RT "Crystallization and biochemical characterization of the human spliceosomal
RT Aar2-Prp8(RNaseH) complex.";
RL Acta Crystallogr. F 71:1421-1428(2015).
RN [34]
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 [35]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1760-2016, DOMAIN, AND LACK OF
RP METAL-BINDING.
RX PubMed=18843295; DOI=10.1038/emboj.2008.209;
RA Pena V., Rozov A., Fabrizio P., Luehrmann R., Wahl M.C.;
RT "Structure and function of an RNase H domain at the heart of the
RT spliceosome.";
RL EMBO J. 27:2929-2940(2008).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1769-1990, IDENTIFICATION BY MASS
RP SPECTROMETRY, RNA-BINDING, MUTAGENESIS OF VAL-1788 AND THR-1789, AND LACK
RP OF METAL-BINDING SITE.
RX PubMed=18836455; DOI=10.1038/nsmb.1505;
RA Ritchie D.B., Schellenberg M.J., Gesner E.M., Raithatha S.A., Stuart D.T.,
RA Macmillan A.M.;
RT "Structural elucidation of a PRP8 core domain from the heart of the
RT spliceosome.";
RL Nat. Struct. Mol. Biol. 15:1199-1205(2008).
RN [37] {ECO:0007744|PDB:3JCR}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBCELLULAR LOCATION,
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [38] {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 [39] {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 [40] {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 [41] {ECO:0007744|PDB:6FF4, ECO:0007744|PDB:6FF7}
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 [42] {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 [43] {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 [44] {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 [45] {ECO:0007744|PDB:6ICZ, ECO:0007744|PDB:6ID0, ECO:0007744|PDB:6ID1}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.86 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=30728453; DOI=10.1038/s41422-019-0143-x;
RA Zhang X., Zhan X., Yan C., Zhang W., Liu D., Lei J., Shi Y.;
RT "Structures of the human spliceosomes before and after release of the
RT ligated exon.";
RL Cell Res. 29:274-285(2019).
RN [46] {ECO:0007744|PDB:6QDV}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), FUNCTION, SUBCELLULAR
RP 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 [47]
RP VARIANTS RP13 THR-2301; LEU-2304; ARG-2309; PRO-2309; GLY-2310; LYS-2310
RP AND LEU-2314.
RX PubMed=11468273; DOI=10.1093/hmg/10.15.1555;
RA McKie A.B., McHale J.C., Keen T.J., Tarttelin E.E., Goliath R.,
RA van Lith-Verhoeven J.J., Greenberg J., Ramesar R.S., Hoyng C.B.,
RA Cremers F.P., Mackey D.A., Bhattacharya S.S., Bird A.C., Markham A.F.,
RA Inglehearn C.F.;
RT "Mutations in the pre-mRNA splicing factor gene PRPC8 in autosomal dominant
RT retinitis pigmentosa (RP13).";
RL Hum. Mol. Genet. 10:1555-1562(2001).
RN [48]
RP VARIANTS RP13 GLY-2310 AND ASN-2334.
RA De Erkenez A.C., Berson E.L., Dryja T.P.;
RT "Novel mutations in the PRPC8 gene, encoding a pre-mRNA splicing factor in
RT patients with autosomal dominant retinitis pigmentosa.";
RL (er) Invest. Ophthalmol. Vis. Sci. 43:ARVO E-Abstract 791(2002).
RN [49]
RP VARIANT RP13 LYS-2310.
RX PubMed=11910553; DOI=10.1076/opge.23.1.1.2206;
RA van Lith-Verhoeven J.J., van der Velde-Visser S.D., Sohocki M.M.,
RA Deutman A.F., Brink H.M., Cremers F.P., Hoyng C.B.;
RT "Clinical characterization, linkage analysis, and PRPC8 mutation analysis
RT of a family with autosomal dominant retinitis pigmentosa type 13 (RP13).";
RL Ophthalmic Genet. 23:1-12(2002).
RN [50]
RP VARIANT RP13 GLY-2310.
RX PubMed=12714658; DOI=10.1167/iovs.02-0871;
RA Martinez-Gimeno M., Gamundi M.J., Hernan I., Maseras M., Milla E.,
RA Ayuso C., Garcia-Sandoval B., Beneyto M., Vilela C., Baiget M.,
RA Antinolo G., Carballo M.;
RT "Mutations in the pre-mRNA splicing-factor genes PRPF3, PRPF8, and PRPF31
RT in Spanish families with autosomal dominant retinitis pigmentosa.";
RL Invest. Ophthalmol. Vis. Sci. 44:2171-2177(2003).
RN [51]
RP CHARACTERIZATION OF VARIANTS RP13 LEU-2304; PRO-2309; ARG-2309; GLY-2310;
RP LYS-2310 AND LEU-2314, AND INTERACTION WITH EFTUD2 AND SNRNP200.
RX PubMed=17317632; DOI=10.1016/j.molcel.2007.01.023;
RA Pena V., Liu S., Bujnicki J.M., Luehrmann R., Wahl M.C.;
RT "Structure of a multipartite protein-protein interaction domain in splicing
RT factor Prp8 and its link to retinitis pigmentosa.";
RL Mol. Cell 25:615-624(2007).
CC -!- FUNCTION: Plays role in pre-mRNA splicing as core component of
CC precatalytic, catalytic and postcatalytic spliceosomal complexes, both
CC of the predominant U2-type spliceosome and the minor U12-type
CC spliceosome (PubMed:10411133, PubMed:11971955, PubMed:28502770,
CC PubMed:28781166, PubMed:28076346, PubMed:29361316, PubMed:30315277,
CC PubMed:29360106, PubMed:29301961, PubMed:30728453, PubMed:30705154).
CC Functions as a scaffold that mediates the ordered assembly of
CC spliceosomal proteins and snRNAs. Required for the assembly of the
CC U4/U6-U5 tri-snRNP complex, a building block of the spliceosome.
CC Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs
CC at splice sites on pre-mRNA substrates, so that splicing can occur.
CC Interacts with both the 5' and the 3' splice site.
CC {ECO:0000269|PubMed:10411133, ECO:0000269|PubMed:11971955,
CC ECO:0000269|PubMed:20595234, 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, ECO:0000269|PubMed:30728453,
CC ECO:0000303|PubMed:15840809}.
CC -!- SUBUNIT: Part of the U5 snRNP complex (PubMed:2532307, PubMed:2527369).
CC Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and
CC U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200,
CC TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39
CC (PubMed:2479028, PubMed:16723661, PubMed:26912367). Component of the
CC U5.U4atac/U6atac snRNP complexes in U12-dependent spliceosomes
CC (PubMed:11971955). Core component of U2-type precatalytic, catalytic
CC and postcatalytic spliceosomal complexes (PubMed:10411133,
CC PubMed:28502770, PubMed:28781166, PubMed:28076346, PubMed:29361316,
CC PubMed:30315277, PubMed:29360106, PubMed:29301961, PubMed:30728453,
CC PubMed:30705154). Found in a mRNA splicing-dependent exon junction
CC complex (EJC) with SRRM1. Interacts with U5 snRNP proteins SNRP116 and
CC SNRNP40. Interacts with EFTUD2 and SNRNP200. Interacts (via the MPN
CC (JAB/Mov34) domain) with PRPF3 ('Lys-63'-linked polyubiquitinated); may
CC stabilize the U4/U6-U5 tri-snRNP complex. Interacts (via RNase H
CC homology domain) with AAR2 (PubMed:26527271). Interacts with RPAP3 and
CC URI1 in a ZNHIT2-dependent manner (PubMed:28561026).
CC {ECO:0000269|PubMed:10024169, ECO:0000269|PubMed:10411133,
CC ECO:0000269|PubMed:10809668, ECO:0000269|PubMed:10983979,
CC ECO:0000269|PubMed:11006293, ECO:0000269|PubMed:11971955,
CC ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:17317632,
CC ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:2139226,
CC ECO:0000269|PubMed:2479028, ECO:0000269|PubMed:2527369,
CC ECO:0000269|PubMed:2532307, ECO:0000269|PubMed:26527271,
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:30705154,
CC ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:8608445,
CC ECO:0000269|PubMed:8702566, ECO:0000269|PubMed:9303319,
CC ECO:0000269|PubMed:9774689}.
CC -!- INTERACTION:
CC Q6P2Q9; P54253: ATXN1; NbExp=6; IntAct=EBI-538479, EBI-930964;
CC Q6P2Q9; O75934: BCAS2; NbExp=2; IntAct=EBI-538479, EBI-1050106;
CC Q6P2Q9; O95905: ECD; NbExp=3; IntAct=EBI-538479, EBI-2557598;
CC Q6P2Q9; Q15029: EFTUD2; NbExp=6; IntAct=EBI-538479, EBI-357897;
CC Q6P2Q9; Q92917: GPKOW; NbExp=2; IntAct=EBI-538479, EBI-746309;
CC Q6P2Q9; Q15365: PCBP1; NbExp=2; IntAct=EBI-538479, EBI-946095;
CC Q6P2Q9; Q9UMS4: PRPF19; NbExp=2; IntAct=EBI-538479, EBI-395746;
CC Q6P2Q9; O94906: PRPF6; NbExp=4; IntAct=EBI-538479, EBI-536755;
CC Q6P2Q9; Q13435: SF3B2; NbExp=3; IntAct=EBI-538479, EBI-749111;
CC Q6P2Q9; Q15427: SF3B4; NbExp=2; IntAct=EBI-538479, EBI-348469;
CC Q6P2Q9; O95391: SLU7; NbExp=2; IntAct=EBI-538479, EBI-750559;
CC Q6P2Q9; O75643: SNRNP200; NbExp=3; IntAct=EBI-538479, EBI-1045395;
CC Q6P2Q9; O75643-1: SNRNP200; NbExp=2; IntAct=EBI-538479, EBI-5456052;
CC Q6P2Q9; Q96DI7: SNRNP40; NbExp=4; IntAct=EBI-538479, EBI-538492;
CC Q6P2Q9; Q13148: TARDBP; NbExp=3; IntAct=EBI-538479, EBI-372899;
CC Q6P2Q9; Q9BRX9: WDR83; NbExp=2; IntAct=EBI-538479, EBI-7705033;
CC Q6P2Q9; Q96NB3: ZNF830; NbExp=2; IntAct=EBI-538479, EBI-3920997;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26912367,
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:0000269|PubMed:30728453}. Nucleus speckle {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10411133}.
CC -!- DOMAIN: The MPN (JAB/Mov34) domain has structural similarity with
CC deubiquitinating enzymes, but lacks the residues that would bind the
CC catalytic metal ion. {ECO:0000250}.
CC -!- DOMAIN: Contains a region with structural similarity to reverse
CC transcripase, presenting the classical thumb, fingers and palm
CC architecture, but lacks enzyme activity, since the essential metal-
CC binding residues are not conserved. {ECO:0000250}.
CC -!- DOMAIN: Contains a region with structural similarity to type-2
CC restriction endonucleases, but the residues that would bind catalytic
CC metal ions in endonucleases are instead involved in hydrogen bonds that
CC stabilize the protein structure. {ECO:0000250}.
CC -!- DOMAIN: Contains a region with structural similarity to RNase H, but
CC lacks RNase H activity. {ECO:0000250}.
CC -!- DISEASE: Retinitis pigmentosa 13 (RP13) [MIM:600059]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:11468273,
CC ECO:0000269|PubMed:11910553, ECO:0000269|PubMed:12714658,
CC ECO:0000269|PubMed:17317632, ECO:0000269|Ref.48}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
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DR EMBL; AF092565; AAC61776.1; -; mRNA.
DR EMBL; AB007510; BAA22563.1; -; mRNA.
DR EMBL; BC064370; AAH64370.1; -; mRNA.
DR CCDS; CCDS11010.1; -.
DR RefSeq; NP_006436.3; NM_006445.3.
DR PDB; 3E9L; X-ray; 1.95 A; A=1760-2016.
DR PDB; 3ENB; X-ray; 1.85 A; A/B=1769-1990.
DR PDB; 3JCR; EM; 7.00 A; A=1-2335.
DR PDB; 3LRU; X-ray; 1.85 A; A/B=1831-1990.
DR PDB; 4JK7; X-ray; 1.40 A; A/B=1769-1990.
DR PDB; 4JK8; X-ray; 1.15 A; A/B=1769-1990.
DR PDB; 4JK9; X-ray; 1.50 A; A/B=1769-1990.
DR PDB; 4JKA; X-ray; 1.32 A; A/B=1769-1990.
DR PDB; 4JKB; X-ray; 1.30 A; A/B=1769-1990.
DR PDB; 4JKC; X-ray; 1.50 A; A/B=1769-1990.
DR PDB; 4JKD; X-ray; 1.55 A; A/B=1769-1990.
DR PDB; 4JKE; X-ray; 1.65 A; A/B=1769-1990.
DR PDB; 4JKF; X-ray; 1.95 A; A/B=1769-1990.
DR PDB; 4JKG; X-ray; 1.80 A; A/B=1769-1990.
DR PDB; 4JKH; X-ray; 1.80 A; A/B=1769-1990.
DR PDB; 4KIT; X-ray; 3.60 A; C=2064-2335.
DR PDB; 5MQF; EM; 5.90 A; A=1-2335.
DR PDB; 5O9Z; EM; 4.50 A; A=1-2335.
DR PDB; 5XJC; EM; 3.60 A; A=1-2335.
DR PDB; 5YZG; EM; 4.10 A; A=1-2335.
DR PDB; 5Z56; EM; 5.10 A; A=1-2335.
DR PDB; 5Z57; EM; 6.50 A; A=1-2335.
DR PDB; 5Z58; EM; 4.90 A; A=1-2335.
DR PDB; 6AH0; EM; 5.70 A; A=1-2335.
DR PDB; 6AHD; EM; 3.80 A; A=1-2335.
DR PDB; 6FF4; EM; 16.00 A; A=1-2335.
DR PDB; 6FF7; EM; 4.50 A; A=1-2335.
DR PDB; 6ICZ; EM; 3.00 A; A=1-2335.
DR PDB; 6ID0; EM; 2.90 A; A=1-2335.
DR PDB; 6ID1; EM; 2.86 A; A=1-2335.
DR PDB; 6QDV; EM; 3.30 A; A=1-2335.
DR PDB; 6QW6; EM; 2.92 A; 5A=25-2335.
DR PDB; 6QX9; EM; 3.28 A; 5A=25-2335.
DR PDB; 6S8Q; X-ray; 2.39 A; J=2064-2320.
DR PDB; 6S9I; X-ray; 2.60 A; J=2064-2320.
DR PDB; 6ZYM; EM; 3.40 A; A=1-1755.
DR PDB; 7A5P; EM; 5.00 A; A=1-2335.
DR PDB; 7AAV; EM; 4.20 A; A=1-2335.
DR PDB; 7ABF; EM; 3.90 A; A=1-2335.
DR PDB; 7ABG; EM; 7.80 A; A=1-2335.
DR PDB; 7ABI; EM; 8.00 A; A=1-2335.
DR PDB; 7BDI; X-ray; 2.80 A; J=2064-2320.
DR PDB; 7BDJ; X-ray; 2.59 A; J=2064-2320.
DR PDB; 7BDK; X-ray; 2.52 A; J=2064-2320.
DR PDB; 7BDL; X-ray; 2.69 A; J=2064-2320.
DR PDB; 7DVQ; EM; 2.89 A; A=1-2335.
DR PDB; 7OS2; EM; 2.76 A; J=2064-2335.
DR PDB; 7PX3; EM; 3.05 A; J=2064-2320.
DR PDBsum; 3E9L; -.
DR PDBsum; 3ENB; -.
DR PDBsum; 3JCR; -.
DR PDBsum; 3LRU; -.
DR PDBsum; 4JK7; -.
DR PDBsum; 4JK8; -.
DR PDBsum; 4JK9; -.
DR PDBsum; 4JKA; -.
DR PDBsum; 4JKB; -.
DR PDBsum; 4JKC; -.
DR PDBsum; 4JKD; -.
DR PDBsum; 4JKE; -.
DR PDBsum; 4JKF; -.
DR PDBsum; 4JKG; -.
DR PDBsum; 4JKH; -.
DR PDBsum; 4KIT; -.
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; 6S8Q; -.
DR PDBsum; 6S9I; -.
DR PDBsum; 6ZYM; -.
DR PDBsum; 7A5P; -.
DR PDBsum; 7AAV; -.
DR PDBsum; 7ABF; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7BDI; -.
DR PDBsum; 7BDJ; -.
DR PDBsum; 7BDK; -.
DR PDBsum; 7BDL; -.
DR PDBsum; 7DVQ; -.
DR PDBsum; 7OS2; -.
DR PDBsum; 7PX3; -.
DR AlphaFoldDB; Q6P2Q9; -.
DR SMR; Q6P2Q9; -.
DR BioGRID; 115842; 696.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; Q6P2Q9; -.
DR DIP; DIP-29614N; -.
DR IntAct; Q6P2Q9; 118.
DR MINT; Q6P2Q9; -.
DR STRING; 9606.ENSP00000460348; -.
DR CarbonylDB; Q6P2Q9; -.
DR GlyGen; Q6P2Q9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6P2Q9; -.
DR MetOSite; Q6P2Q9; -.
DR PhosphoSitePlus; Q6P2Q9; -.
DR SwissPalm; Q6P2Q9; -.
DR BioMuta; PRPF8; -.
DR DMDM; 67460824; -.
DR EPD; Q6P2Q9; -.
DR jPOST; Q6P2Q9; -.
DR MassIVE; Q6P2Q9; -.
DR MaxQB; Q6P2Q9; -.
DR PaxDb; Q6P2Q9; -.
DR PeptideAtlas; Q6P2Q9; -.
DR PRIDE; Q6P2Q9; -.
DR ProteomicsDB; 66917; -.
DR Antibodypedia; 4094; 169 antibodies from 31 providers.
DR DNASU; 10594; -.
DR Ensembl; ENST00000304992.11; ENSP00000304350.6; ENSG00000174231.17.
DR Ensembl; ENST00000572621.5; ENSP00000460348.1; ENSG00000174231.17.
DR Ensembl; ENST00000614672.2; ENSP00000479194.1; ENSG00000274442.2.
DR Ensembl; ENST00000634039.1; ENSP00000488611.1; ENSG00000274442.2.
DR GeneID; 10594; -.
DR KEGG; hsa:10594; -.
DR MANE-Select; ENST00000304992.11; ENSP00000304350.6; NM_006445.4; NP_006436.3.
DR UCSC; uc002fte.3; human.
DR CTD; 10594; -.
DR DisGeNET; 10594; -.
DR GeneCards; PRPF8; -.
DR GeneReviews; PRPF8; -.
DR HGNC; HGNC:17340; PRPF8.
DR HPA; ENSG00000174231; Low tissue specificity.
DR MalaCards; PRPF8; -.
DR MIM; 600059; phenotype.
DR MIM; 607300; gene.
DR neXtProt; NX_Q6P2Q9; -.
DR OpenTargets; ENSG00000174231; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA33815; -.
DR VEuPathDB; HostDB:ENSG00000174231; -.
DR eggNOG; KOG1795; Eukaryota.
DR GeneTree; ENSGT00390000015210; -.
DR HOGENOM; CLU_000380_3_0_1; -.
DR InParanoid; Q6P2Q9; -.
DR OMA; VCMRREK; -.
DR OrthoDB; 156083at2759; -.
DR PhylomeDB; Q6P2Q9; -.
DR TreeFam; TF105613; -.
DR PathwayCommons; Q6P2Q9; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; Q6P2Q9; -.
DR BioGRID-ORCS; 10594; 799 hits in 1089 CRISPR screens.
DR ChiTaRS; PRPF8; human.
DR EvolutionaryTrace; Q6P2Q9; -.
DR GeneWiki; PRPF8; -.
DR GenomeRNAi; 10594; -.
DR Pharos; Q6P2Q9; Tbio.
DR PRO; PR:Q6P2Q9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6P2Q9; protein.
DR Bgee; ENSG00000174231; Expressed in adenohypophysis and 92 other tissues.
DR ExpressionAtlas; Q6P2Q9; baseline and differential.
DR Genevisible; Q6P2Q9; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; 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:0005682; C:U5 snRNP; IBA:GO_Central.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR GO; GO:0030623; F:U5 snRNA binding; IBA:GO_Central.
DR GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:UniProtKB.
DR CDD; cd13838; RNase_H_like_Prp8_IV; 1.
DR Gene3D; 1.20.80.40; -; 1.
DR Gene3D; 3.30.420.230; -; 1.
DR Gene3D; 3.30.43.40; -; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR012591; PRO8NT.
DR InterPro; IPR012592; PROCN.
DR InterPro; IPR012984; PROCT.
DR InterPro; IPR027652; PRP8.
DR InterPro; IPR021983; PRP8_domainIV.
DR InterPro; IPR043173; Prp8_domainIV_fingers.
DR InterPro; IPR043172; Prp8_domainIV_palm.
DR InterPro; IPR019581; Prp8_U5-snRNA-bd.
DR InterPro; IPR042516; Prp8_U5-snRNA-bd_sf.
DR InterPro; IPR019580; Prp8_U6-snRNA-bd.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR019582; RRM_spliceosomal_PrP8.
DR PANTHER; PTHR11140; PTHR11140; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF08082; PRO8NT; 1.
DR Pfam; PF08083; PROCN; 1.
DR Pfam; PF08084; PROCT; 1.
DR Pfam; PF12134; PRP8_domainIV; 1.
DR Pfam; PF10598; RRM_4; 1.
DR Pfam; PF10597; U5_2-snRNA_bdg; 1.
DR Pfam; PF10596; U6-snRNA_bdg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant;
KW Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Retinitis pigmentosa; Ribonucleoprotein; RNA-binding;
KW Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..2335
FT /note="Pre-mRNA-processing-splicing factor 8"
FT /id="PRO_0000097040"
FT DOMAIN 2103..2234
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 812..1303
FT /note="Reverse transcriptase homology domain"
FT REGION 1304..1577
FT /note="Linker"
FT REGION 1513..1526
FT /note="Important for branch point selection"
FT /evidence="ECO:0000250"
FT REGION 1581..1752
FT /note="Restriction endonuclease homology domain"
FT REGION 1669..2034
FT /note="Involved in interaction with pre-mRNA 5' splice
FT site"
FT REGION 1767..2020
FT /note="RNase H homology domain"
FT REGION 2301..2335
FT /note="Required for interaction with EFTUD2 and SNRNP200"
FT /evidence="ECO:0000269|PubMed:17317632"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1425
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1463
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 68
FT /note="K -> E (in dbSNP:rs1043391)"
FT /id="VAR_022622"
FT VARIANT 227
FT /note="R -> H (in dbSNP:rs11559304)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_022623"
FT VARIANT 874
FT /note="P -> L (in dbSNP:rs1043396)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022624"
FT VARIANT 1293
FT /note="N -> H (in dbSNP:rs1043399)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022625"
FT VARIANT 2301
FT /note="P -> T (in RP13; no effect on interaction with
FT SNRNP200 and EFTUD2; dbSNP:rs121434239)"
FT /evidence="ECO:0000269|PubMed:11468273"
FT /id="VAR_022626"
FT VARIANT 2304
FT /note="F -> L (in RP13; dbSNP:rs121434240)"
FT /evidence="ECO:0000269|PubMed:11468273,
FT ECO:0000269|PubMed:17317632"
FT /id="VAR_022627"
FT VARIANT 2309
FT /note="H -> P (in RP13; no effect on interaction with
FT SNRNP200 and EFTUD2; dbSNP:rs121434236)"
FT /evidence="ECO:0000269|PubMed:11468273,
FT ECO:0000269|PubMed:17317632"
FT /id="VAR_022628"
FT VARIANT 2309
FT /note="H -> R (in RP13; no effect on interaction with
FT SNRNP200 and EFTUD2; dbSNP:rs121434236)"
FT /evidence="ECO:0000269|PubMed:11468273,
FT ECO:0000269|PubMed:17317632"
FT /id="VAR_022629"
FT VARIANT 2310
FT /note="R -> G (in RP13; reduces interaction with SNRNP200
FT and EFTUD2)"
FT /evidence="ECO:0000269|PubMed:11468273,
FT ECO:0000269|PubMed:12714658, ECO:0000269|PubMed:17317632,
FT ECO:0000269|Ref.48"
FT /id="VAR_022630"
FT VARIANT 2310
FT /note="R -> K (in RP13; reduces interaction with SNRNP200
FT and EFTUD2; dbSNP:rs121434238)"
FT /evidence="ECO:0000269|PubMed:11468273,
FT ECO:0000269|PubMed:11910553, ECO:0000269|PubMed:17317632"
FT /id="VAR_022631"
FT VARIANT 2314
FT /note="F -> L (in RP13; reduces interaction with EFTUD2,
FT but not with SNRNP200)"
FT /evidence="ECO:0000269|PubMed:11468273,
FT ECO:0000269|PubMed:17317632"
FT /id="VAR_022632"
FT VARIANT 2334
FT /note="Y -> N (in RP13)"
FT /evidence="ECO:0000269|Ref.48"
FT /id="VAR_022633"
FT MUTAGEN 1788
FT /note="V->D: Strongly reduced interaction with RNA."
FT /evidence="ECO:0000269|PubMed:18836455"
FT MUTAGEN 1789
FT /note="T->P: Strongly reduced interaction with RNA."
FT /evidence="ECO:0000269|PubMed:18836455"
FT CONFLICT 184
FT /note="D -> N (in Ref. 2; BAA22563)"
FT /evidence="ECO:0000305"
FT CONFLICT 492..493
FT /note="VG -> GW (in Ref. 2; BAA22563)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="M -> V (in Ref. 2; BAA22563)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="A -> T (in Ref. 2; BAA22563)"
FT /evidence="ECO:0000305"
FT CONFLICT 997
FT /note="L -> V (in Ref. 2; BAA22563)"
FT /evidence="ECO:0000305"
FT CONFLICT 1390
FT /note="A -> S (in Ref. 2; BAA22563)"
FT /evidence="ECO:0000305"
FT CONFLICT 1867
FT /note="G -> D (in Ref. 2; BAA22563)"
FT /evidence="ECO:0000305"
FT HELIX 27..44
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6ZYM"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 137..156
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 197..208
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:6ZYM"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:6FF4"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:6ID0"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 441..459
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 472..476
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 479..488
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 489..510
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:6FF4"
FT STRAND 524..528
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 532..537
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 542..565
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 572..583
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 585..588
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 599..616
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 631..661
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 677..696
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 706..721
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 729..731
FT /evidence="ECO:0007829|PDB:6ZYM"
FT HELIX 733..763
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 769..796
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 804..819
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 835..847
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 849..851
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 858..872
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 874..886
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 894..900
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 902..910
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 913..932
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 940..942
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 948..960
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 963..966
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 969..971
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 972..980
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 982..987
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 990..1000
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1003..1013
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1016..1019
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1022..1025
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1027..1029
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1037..1053
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1055..1062
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1065..1067
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1077..1080
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1083..1091
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1094..1102
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1103..1116
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1123..1125
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1132..1134
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1136..1138
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1144..1158
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1159..1161
FT /evidence="ECO:0007829|PDB:6FF4"
FT TURN 1163..1165
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1170..1172
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1174..1178
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1185..1188
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1190..1202
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1203..1205
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 1209..1212
FT /evidence="ECO:0007829|PDB:6FF4"
FT STRAND 1213..1217
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1219..1221
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1223..1232
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1234..1248
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1249..1251
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1254..1257
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1258..1273
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1275..1280
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1282..1303
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1308..1310
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 1314..1317
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1320..1322
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1331..1333
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 1337..1339
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1340..1345
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1350..1356
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1360..1362
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 1368..1371
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1375..1398
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1405..1410
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1411..1413
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1415..1418
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1419..1423
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1425..1428
FT /evidence="ECO:0007829|PDB:6ZYM"
FT HELIX 1430..1432
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1436..1441
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1442..1446
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1447..1449
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 1452..1455
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 1458..1460
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1469..1478
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1480..1485
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1486..1489
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1490..1493
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1498..1500
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 1501..1503
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1507..1509
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1512..1515
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1520..1522
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1523..1527
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1529..1531
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1532..1537
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1539..1542
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1545..1547
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1550..1555
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 1556..1558
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 1561..1564
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 1569..1576
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1578..1580
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1581..1597
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1601..1603
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1606..1611
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 1617..1620
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1628..1631
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1632..1635
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 1642..1644
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1656..1658
FT /evidence="ECO:0007829|PDB:6FF4"
FT STRAND 1660..1667
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1671..1673
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1676..1687
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1688..1693
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1696..1698
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 1701..1706
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1707..1710
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1711..1717
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1720..1722
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1723..1733
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 1734..1736
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1738..1751
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1753..1757
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 1761..1763
FT /evidence="ECO:0007829|PDB:3E9L"
FT TURN 1765..1767
FT /evidence="ECO:0007829|PDB:3E9L"
FT HELIX 1768..1772
FT /evidence="ECO:0007829|PDB:3E9L"
FT STRAND 1773..1775
FT /evidence="ECO:0007829|PDB:4JK8"
FT STRAND 1777..1781
FT /evidence="ECO:0007829|PDB:4JK8"
FT STRAND 1785..1792
FT /evidence="ECO:0007829|PDB:4JK8"
FT STRAND 1794..1796
FT /evidence="ECO:0007829|PDB:3E9L"
FT STRAND 1798..1803
FT /evidence="ECO:0007829|PDB:4JK8"
FT STRAND 1805..1810
FT /evidence="ECO:0007829|PDB:4JK8"
FT TURN 1812..1814
FT /evidence="ECO:0007829|PDB:4JK8"
FT STRAND 1816..1822
FT /evidence="ECO:0007829|PDB:4JK8"
FT HELIX 1824..1827
FT /evidence="ECO:0007829|PDB:4JK8"
FT HELIX 1833..1851
FT /evidence="ECO:0007829|PDB:4JK8"
FT HELIX 1854..1856
FT /evidence="ECO:0007829|PDB:4JK8"
FT STRAND 1859..1865
FT /evidence="ECO:0007829|PDB:4JK8"
FT HELIX 1866..1868
FT /evidence="ECO:0007829|PDB:4JK8"
FT HELIX 1869..1875
FT /evidence="ECO:0007829|PDB:4JK8"
FT TURN 1876..1878
FT /evidence="ECO:0007829|PDB:4JK8"
FT STRAND 1883..1886
FT /evidence="ECO:0007829|PDB:4JK8"
FT HELIX 1893..1898
FT /evidence="ECO:0007829|PDB:4JK8"
FT HELIX 1900..1908
FT /evidence="ECO:0007829|PDB:4JK8"
FT STRAND 1913..1918
FT /evidence="ECO:0007829|PDB:4JK8"
FT TURN 1919..1922
FT /evidence="ECO:0007829|PDB:4JK8"
FT HELIX 1923..1925
FT /evidence="ECO:0007829|PDB:4JK8"
FT HELIX 1929..1945
FT /evidence="ECO:0007829|PDB:4JK8"
FT HELIX 1947..1953
FT /evidence="ECO:0007829|PDB:4JK8"
FT STRAND 1957..1959
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 1966..1968
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 1973..1989
FT /evidence="ECO:0007829|PDB:4JK8"
FT HELIX 1999..2001
FT /evidence="ECO:0007829|PDB:3E9L"
FT HELIX 2004..2012
FT /evidence="ECO:0007829|PDB:3E9L"
FT HELIX 2072..2080
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 2081..2088
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2089..2092
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2095..2097
FT /evidence="ECO:0007829|PDB:7PX3"
FT STRAND 2099..2101
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 2103..2107
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 2108..2116
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2120..2122
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2125..2131
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2139..2146
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2149..2152
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 2167..2169
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2172..2183
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 2190..2202
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 2208..2210
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2212..2217
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2222..2230
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 2232..2240
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2245..2247
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 2253..2255
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2256..2259
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2261..2267
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2270..2277
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2282..2284
FT /evidence="ECO:0007829|PDB:7PX3"
FT HELIX 2285..2287
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2296..2298
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 2307..2309
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 2311..2315
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 2316..2318
FT /evidence="ECO:0007829|PDB:7BDK"
FT HELIX 2321..2325
FT /evidence="ECO:0007829|PDB:7DVQ"
SQ SEQUENCE 2335 AA; 273600 MW; E823A15C60EA61C9 CRC64;
MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK FGFVDAQKED
MPPEHVRKII RDHGDMTNRK FRHDKRVYLG ALKYMPHAVL KLLENMPMPW EQIRDVPVLY
HITGAISFVN EIPWVIEPVY ISQWGSMWIM MRREKRDRRH FKRMRFPPFD DEEPPLDYAD
NILDVEPLEA IQLELDPEED APVLDWFYDH QPLRDSRKYV NGSTYQRWQF TLPMMSTLYR
LANQLLTDLV DDNYFYLFDL KAFFTSKALN MAIPGGPKFE PLVRDINLQD EDWNEFNDIN
KIIIRQPIRT EYKIAFPYLY NNLPHHVHLT WYHTPNVVFI KTEDPDLPAF YFDPLINPIS
HRHSVKSQEP LPDDDEEFEL PEFVEPFLKD TPLYTDNTAN GIALLWAPRP FNLRSGRTRR
ALDIPLVKNW YREHCPAGQP VKVRVSYQKL LKYYVLNALK HRPPKAQKKR YLFRSFKATK
FFQSTKLDWV EVGLQVCRQG YNMLNLLIHR KNLNYLHLDY NFNLKPVKTL TTKERKKSRF
GNAFHLCREV LRLTKLVVDS HVQYRLGNVD AFQLADGLQY IFAHVGQLTG MYRYKYKLMR
QIRMCKDLKH LIYYRFNTGP VGKGPGCGFW AAGWRVWLFF MRGITPLLER WLGNLLARQF
EGRHSKGVAK TVTKQRVESH FDLELRAAVM HDILDMMPEG IKQNKARTIL QHLSEAWRCW
KANIPWKVPG LPTPIENMIL RYVKAKADWW TNTAHYNRER IRRGATVDKT VCKKNLGRLT
RLYLKAEQER QHNYLKDGPY ITAEEAVAVY TTTVHWLESR RFSPIPFPPL SYKHDTKLLI
LALERLKEAY SVKSRLNQSQ REELGLIEQA YDNPHEALSR IKRHLLTQRA FKEVGIEFMD
LYSHLVPVYD VEPLEKITDA YLDQYLWYEA DKRRLFPPWI KPADTEPPPL LVYKWCQGIN
NLQDVWETSE GECNVMLESR FEKMYEKIDL TLLNRLLRLI VDHNIADYMT AKNNVVINYK
DMNHTNSYGI IRGLQFASFI VQYYGLVMDL LVLGLHRASE MAGPPQMPND FLSFQDIATE
AAHPIRLFCR YIDRIHIFFR FTADEARDLI QRYLTEHPDP NNENIVGYNN KKCWPRDARM
RLMKHDVNLG RAVFWDIKNR LPRSVTTVQW ENSFVSVYSK DNPNLLFNMC GFECRILPKC
RTSYEEFTHK DGVWNLQNEV TKERTAQCFL RVDDESMQRF HNRVRQILMA SGSTTFTKIV
NKWNTALIGL MTYFREAVVN TQELLDLLVK CENKIQTRIK IGLNSKMPSR FPPVVFYTPK
ELGGLGMLSM GHVLIPQSDL RWSKQTDVGI THFRSGMSHE EDQLIPNLYR YIQPWESEFI
DSQRVWAEYA LKRQEAIAQN RRLTLEDLED SWDRGIPRIN TLFQKDRHTL AYDKGWRVRT
DFKQYQVLKQ NPFWWTHQRH DGKLWNLNNY RTDMIQALGG VEGILEHTLF KGTYFPTWEG
LFWEKASGFE ESMKWKKLTN AQRSGLNQIP NRRFTLWWSP TINRANVYVG FQVQLDLTGI
FMHGKIPTLK ISLIQIFRAH LWQKIHESIV MDLCQVFDQE LDALEIETVQ KETIHPRKSY
KMNSSCADIL LFASYKWNVS RPSLLADSKD VMDSTTTQKY WIDIQLRWGD YDSHDIERYA
RAKFLDYTTD NMSIYPSPTG VLIAIDLAYN LHSAYGNWFP GSKPLIQQAM AKIMKANPAL
YVLRERIRKG LQLYSSEPTE PYLSSQNYGE LFSNQIIWFV DDTNVYRVTI HKTFEGNLTT
KPINGAIFIF NPRTGQLFLK IIHTSVWAGQ KRLGQLAKWK TAEEVAALIR SLPVEEQPKQ
IIVTRKGMLD PLEVHLLDFP NIVIKGSELQ LPFQACLKVE KFGDLILKAT EPQMVLFNLY
DDWLKTISSY TAFSRLILIL RALHVNNDRA KVILKPDKTT ITEPHHIWPT LTDEEWIKVE
VQLKDLILAD YGKKNNVNVA SLTQSEIRDI ILGMEISAPS QQRQQIAEIE KQTKEQSQLT
ATQTRTVNKH GDEIITSTTS NYETQTFSSK TEWRVRAISA ANLHLRTNHI YVSSDDIKET
GYTYILPKNV LKKFICISDL RAQIAGYLYG VSPPDNPQVK EIRCIVMVPQ WGTHQTVHLP
GQLPQHEYLK EMEPLGWIHT QPNESPQLSP QDVTTHAKIM ADNPSWDGEK TIIITCSFTP
GSCTLTAYKL TPSGYEWGRQ NTDKGNNPKG YLPSHYERVQ MLLSDRFLGF FMVPAQSSWN
YNFMGVRHDP NMKYELQLAN PKEFYHEVHR PSHFLNFALL QEGEVYSADR EDLYA
