PRP4_HUMAN
ID PRP4_HUMAN Reviewed; 522 AA.
AC O43172; O43445; O43864; Q5T1M8; Q96DG2; Q96IK4;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=U4/U6 small nuclear ribonucleoprotein Prp4;
DE AltName: Full=PRP4 homolog;
DE Short=hPrp4;
DE AltName: Full=U4/U6 snRNP 60 kDa protein;
DE AltName: Full=WD splicing factor Prp4;
GN Name=PRPF4; Synonyms=PRP4;
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 [GENOMIC DNA] (ISOFORM 2), SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9257651;
RA Lauber J., Plessel G., Prehn S., Will C.L., Fabrizio P., Groning K.,
RA Lane W.S., Luehrmann R.;
RT "The human U4/U6 snRNP contains 60 and 90kD proteins that are structurally
RT homologous to the yeast splicing factors Prp4p and Prp3p.";
RL RNA 3:926-941(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 28-38; 58-85;
RP 95-106; 193-200 AND 457-472, INTERACTION WITH U4/U5/U6 SNRNPS, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9404889;
RA Horowitz D.S., Kobayashi R., Krainer A.R.;
RT "A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a
RT complex associated with U4/U6 snRNPs.";
RL RNA 3:1374-1387(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH PRPF3 AND U4/U5/U6
RP SNRNPS, AND SUBCELLULAR LOCATION.
RX PubMed=9328476; DOI=10.1093/hmg/6.12.2117;
RA Wang A., Forman-Kay J., Luo Y., Luo M., Chow Y.-H., Plumb J., Friesen J.D.,
RA Tsui L.-C., Heng H.H.Q., Woolford J.L. Jr., Hu J.;
RT "Identification and characterization of human genes encoding Hprp3p and
RT Hprp4p, interacting components of the spliceosome.";
RL Hum. Mol. Genet. 6:2117-2126(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Ovary;
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 [7]
RP INTERACTION WITH PRPF18.
RX PubMed=9000057; DOI=10.1101/gad.11.1.139;
RA Horowitz D.S., Krainer A.R.;
RT "A human protein required for the second step of pre-mRNA splicing is
RT functionally related to a yeast splicing factor.";
RL Genes Dev. 11:139-151(1997).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, 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 [10]
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 [11]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 107-137 IN COMPLEX WITH PPIH.
RX PubMed=12875835; DOI=10.1016/s0022-2836(03)00684-3;
RA Reidt U., Wahl M.C., Fasshauer D., Horowitz D.S., Luehrmann R., Ficner R.;
RT "Crystal structure of a complex between human spliceosomal cyclophilin H
RT and a U4/U6 snRNP-60K peptide.";
RL J. Mol. Biol. 331:45-56(2003).
RN [13] {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 [14] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [15]
RP INVOLVEMENT IN RP70, AND VARIANT RP70 LEU-315.
RX PubMed=24419317; DOI=10.1093/hmg/ddu005;
RA Chen X., Liu Y., Sheng X., Tam P.O., Zhao K., Chen X., Rong W., Liu Y.,
RA Liu X., Pan X., Chen L.J., Zhao Q., Vollrath D., Pang C.P., Zhao C.;
RT "PRPF4 mutations cause autosomal dominant retinitis pigmentosa.";
RL Hum. Mol. Genet. 23:2926-2939(2014).
RN [16]
RP VARIANT RP70 HIS-192, CHARACTERIZATION OF VARIANT RP70 HIS-192, INTERACTION
RP WITH PRPF3 AND PPIH, MUTAGENESIS OF ARG-192, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25383878; DOI=10.1371/journal.pone.0111754;
RA Linder B., Hirmer A., Gal A., Ruether K., Bolz H.J., Winkler C.,
RA Laggerbauer B., Fischer U.;
RT "Identification of a PRPF4 loss-of-function variant that abrogates U4/U6.U5
RT tri-snRNP integration and is associated with retinitis pigmentosa.";
RL PLoS ONE 9:E111754-E111754(2014).
CC -!- FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5
CC tri-snRNP complex that is involved in spliceosome assembly, and as
CC component of the precatalytic spliceosome (spliceosome B complex).
CC {ECO:0000269|PubMed:25383878, ECO:0000269|PubMed:28781166}.
CC -!- SUBUNIT: Component of the precatalytic spliceosome (spliceosome B
CC complex) (PubMed:28781166). Component of the U4/U6-U5 tri-snRNP
CC complex, a building block of the precatalytic spliceosome (spliceosome
CC B complex) (PubMed:9257651, PubMed:9404889, PubMed:9328476,
CC PubMed:28781166, PubMed:26912367). The U4/U6-U5 tri-snRNP complex is
CC composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6,
CC PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2,
CC SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1
CC and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8
CC (PubMed:16723661, PubMed:26912367). Interacts directly with PRPF18,
CC PPIH and PRPF3 (PubMed:9404889, PubMed:9328476, PubMed:9000057,
CC PubMed:12875835, PubMed:25383878). Part of a heteromeric complex
CC containing PPIH, PRPF3 and PRPF4 that is stable in the absence of RNA
CC (PubMed:9404889). Interacts with ERCC6 (PubMed:26030138).
CC {ECO:0000269|PubMed:12875835, ECO:0000269|PubMed:16723661,
CC ECO:0000269|PubMed:25383878, ECO:0000269|PubMed:26030138,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166,
CC ECO:0000269|PubMed:9000057, ECO:0000269|PubMed:9257651,
CC ECO:0000269|PubMed:9328476, ECO:0000269|PubMed:9404889}.
CC -!- INTERACTION:
CC O43172; Q92917: GPKOW; NbExp=2; IntAct=EBI-718395, EBI-746309;
CC O43172; O43447: PPIH; NbExp=5; IntAct=EBI-718395, EBI-1055615;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25383878,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166,
CC ECO:0000269|PubMed:9257651, ECO:0000269|PubMed:9328476,
CC ECO:0000269|PubMed:9404889}. Nucleus speckle {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43172-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43172-2; Sequence=VSP_006785;
CC -!- DISEASE: Retinitis pigmentosa 70 (RP70) [MIM:615922]: 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:24419317,
CC ECO:0000269|PubMed:25383878}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AF001687; AAB87640.1; -; Genomic_DNA.
DR EMBL; AF016369; AAC51925.1; -; mRNA.
DR EMBL; U82756; AAC02261.1; -; mRNA.
DR EMBL; AL449305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87362.1; -; Genomic_DNA.
DR EMBL; BC001588; AAH01588.1; -; mRNA.
DR EMBL; BC007424; AAH07424.1; -; mRNA.
DR CCDS; CCDS59142.1; -. [O43172-2]
DR CCDS; CCDS6791.1; -. [O43172-1]
DR RefSeq; NP_001231855.1; NM_001244926.1. [O43172-2]
DR RefSeq; NP_004688.2; NM_004697.4. [O43172-1]
DR PDB; 1MZW; X-ray; 2.00 A; B=107-137.
DR PDB; 3JCR; EM; 7.00 A; L=1-522.
DR PDB; 5O9Z; EM; 4.50 A; F=1-522.
DR PDB; 6AH0; EM; 5.70 A; K=1-522.
DR PDB; 6AHD; EM; 3.80 A; 7=421-443.
DR PDB; 6QW6; EM; 2.92 A; 4B=1-522.
DR PDB; 6QX9; EM; 3.28 A; 4B=1-522.
DR PDBsum; 1MZW; -.
DR PDBsum; 3JCR; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR AlphaFoldDB; O43172; -.
DR SMR; O43172; -.
DR BioGRID; 114576; 219.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; O43172; -.
DR IntAct; O43172; 108.
DR MINT; O43172; -.
DR STRING; 9606.ENSP00000363313; -.
DR BindingDB; O43172; -.
DR DrugCentral; O43172; -.
DR GlyGen; O43172; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43172; -.
DR PhosphoSitePlus; O43172; -.
DR SwissPalm; O43172; -.
DR BioMuta; PRPF4; -.
DR EPD; O43172; -.
DR jPOST; O43172; -.
DR MassIVE; O43172; -.
DR MaxQB; O43172; -.
DR PaxDb; O43172; -.
DR PeptideAtlas; O43172; -.
DR PRIDE; O43172; -.
DR ProteomicsDB; 48788; -. [O43172-1]
DR ProteomicsDB; 48789; -. [O43172-2]
DR Antibodypedia; 15276; 138 antibodies from 23 providers.
DR DNASU; 9128; -.
DR Ensembl; ENST00000374198.5; ENSP00000363313.4; ENSG00000136875.13. [O43172-2]
DR Ensembl; ENST00000374199.9; ENSP00000363315.4; ENSG00000136875.13. [O43172-1]
DR GeneID; 9128; -.
DR KEGG; hsa:9128; -.
DR MANE-Select; ENST00000374198.5; ENSP00000363313.4; NM_001244926.2; NP_001231855.1. [O43172-2]
DR UCSC; uc004bgx.4; human. [O43172-1]
DR CTD; 9128; -.
DR DisGeNET; 9128; -.
DR GeneCards; PRPF4; -.
DR HGNC; HGNC:17349; PRPF4.
DR HPA; ENSG00000136875; Low tissue specificity.
DR MalaCards; PRPF4; -.
DR MIM; 607795; gene.
DR MIM; 615922; phenotype.
DR neXtProt; NX_O43172; -.
DR OpenTargets; ENSG00000136875; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA38448; -.
DR VEuPathDB; HostDB:ENSG00000136875; -.
DR eggNOG; KOG0272; Eukaryota.
DR GeneTree; ENSGT00940000156006; -.
DR HOGENOM; CLU_000288_57_20_1; -.
DR InParanoid; O43172; -.
DR OMA; LNEPICY; -.
DR OrthoDB; 1076587at2759; -.
DR PhylomeDB; O43172; -.
DR TreeFam; TF314922; -.
DR PathwayCommons; O43172; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O43172; -.
DR BioGRID-ORCS; 9128; 757 hits in 1085 CRISPR screens.
DR EvolutionaryTrace; O43172; -.
DR GeneWiki; PRPF4; -.
DR GenomeRNAi; 9128; -.
DR Pharos; O43172; Tchem.
DR PRO; PR:O43172; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O43172; protein.
DR Bgee; ENSG00000136875; Expressed in secondary oocyte and 201 other tissues.
DR ExpressionAtlas; O43172; baseline and differential.
DR Genevisible; O43172; HS.
DR GO; GO:0015030; C:Cajal body; IDA:BHF-UCL.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; NAS:UniProtKB.
DR GO; GO:0097525; C:spliceosomal snRNP complex; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0071001; C:U4/U6 snRNP; IDA:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:CAFA.
DR GO; GO:0030621; F:U4 snRNA binding; IBA:GO_Central.
DR GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; NAS:UniProtKB.
DR DisProt; DP01751; -.
DR Gene3D; 2.130.10.10; -; 3.
DR Gene3D; 4.10.280.110; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR014906; PRP4-like.
DR InterPro; IPR036285; PRP4-like_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08799; PRP4; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00500; SFM; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF158230; SSF158230; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Disease variant; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Retinitis pigmentosa; Spliceosome; WD repeat.
FT CHAIN 1..522
FT /note="U4/U6 small nuclear ribonucleoprotein Prp4"
FT /id="PRO_0000051149"
FT REPEAT 229..268
FT /note="WD 1"
FT REPEAT 271..318
FT /note="WD 2"
FT REPEAT 321..360
FT /note="WD 3"
FT REPEAT 363..402
FT /note="WD 4"
FT REPEAT 405..444
FT /note="WD 5"
FT REPEAT 447..487
FT /note="WD 6"
FT REPEAT 490..521
FT /note="WD 7"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 10
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9328476"
FT /id="VSP_006785"
FT VARIANT 192
FT /note="R -> H (in RP70; does not affect nuclear speck
FT localization; disrupts interaction with PRPF3; does not
FT affect interaction with PPIH; does not integrated in
FT spliceosomal snRNP complex; dbSNP:rs41296057)"
FT /evidence="ECO:0000269|PubMed:25383878"
FT /id="VAR_074029"
FT VARIANT 315
FT /note="P -> L (in RP70; dbSNP:rs587777599)"
FT /evidence="ECO:0000269|PubMed:24419317"
FT /id="VAR_071872"
FT MUTAGEN 192
FT /note="R->E: Decreases PRPF3 binding."
FT /evidence="ECO:0000269|PubMed:25383878"
FT MUTAGEN 192
FT /note="R->K: Decreases PRPF3 binding."
FT /evidence="ECO:0000269|PubMed:25383878"
FT MUTAGEN 192
FT /note="R->W: Decreases PRPF3 binding."
FT /evidence="ECO:0000269|PubMed:25383878"
FT CONFLICT 78..103
FT /note="HISERQAEVLAEFERRKRARQINVST -> ISASDRQKYWLSLREGSEPGRS
FT MFPP (in Ref. 3; AAC02261)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="H -> R (in Ref. 2; AAC51925)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="V -> L (in Ref. 1; AAB87640)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="R -> K (in Ref. 1; AAB87640)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="G -> D (in Ref. 1; AAB87640)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="Missing (in Ref. 3; AAC02261)"
FT /evidence="ECO:0000305"
FT CONFLICT 275..282
FT /note="NVGAIVFH -> KKEQLHSI (in Ref. 3; AAC02261)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="G -> D (in Ref. 1; AAB87640)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="A -> P (in Ref. 1; AAB87640)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="C -> Y (in Ref. 1; AAB87640)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="A -> L (in Ref. 1; AAB87640)"
FT /evidence="ECO:0000305"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:1MZW"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1MZW"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:1MZW"
SQ SEQUENCE 522 AA; 58449 MW; 08975A26D0B21857 CRC64;
MASSRASSTQ ATKTKAPDDL VAPVVKKPHI YYGSLEEKER ERLAKGESGI LGKDGLKAGI
EAGNINITSG EVFEIEEHIS ERQAEVLAEF ERRKRARQIN VSTDDSEVKA CLRALGEPIT
LFGEGPAERR ERLRNILSVV GTDALKKTKK DDEKSKKSKE EYQQTWYHEG PNSLKVARLW
IANYSLPRAM KRLEEARLHK EIPETTRTSQ MQELHKSLRS LNNFCSQIGD DRPISYCHFS
PNSKMLATAC WSGLCKLWSV PDCNLLHTLR GHNTNVGAIV FHPKSTVSLD PKDVNLASCA
ADGSVKLWSL DSDEPVADIE GHTVRVARVM WHPSGRFLGT TCYDRSWRLW DLEAQEEILH
QEGHSMGVYD IAFHQDGSLA GTGGLDAFGR VWDLRTGRCI MFLEGHLKEI YGINFSPNGY
HIATGSGDNT CKVWDLRQRR CVYTIPAHQN LVTGVKFEPI HGNFLLTGAY DNTAKIWTHP
GWSPLKTLAG HEGKVMGLDI SSDGQLIATC SYDRTFKLWM AE
