ID PLRG1_HUMAN Reviewed; 514 AA. AC O43660; B3KMK4; Q3KQY5; Q8WUD8; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 196. DE RecName: Full=Pleiotropic regulator 1; GN Name=PLRG1; 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] (ISOFORM 1). RX PubMed=9765207; DOI=10.1101/gad.12.19.3059; RA Nemeth K., Salchert K., Putnoky P., Bhalerao R., Koncz-Kalman Z., RA Stankovic-Stangeland B., Bako L., Mathur J., Oekresz L., Stabel S., RA Geigenberger P., Stitt M., Redei G.P., Schell J., Koncz C.; RT "Pleiotropic control of glucose and hormone responses by PRL1, a nuclear WD RT protein, in Arabidopsis."; RL Genes Dev. 12:3059-3073(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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]. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lung; 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 [5] RP PROTEIN SEQUENCE OF 8-41; 48-62; 69-113; 117-135; 141-180; 199-226; RP 238-250; 258-268; 283-308; 321-355; 377-396; 443-449 AND 488-510, RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND RP INTERACTION WITH CDC5L AND THE SPLICEOSOME. RX PubMed=11101529; DOI=10.1093/emboj/19.23.6569; RA Ajuh P., Kuster B., Panov K., Zomerdijk J.C.B.M., Mann M., Lamond A.I.; RT "Functional analysis of the human CDC5L complex and identification of its RT components by mass spectrometry."; RL EMBO J. 19:6569-6581(2000). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDC5L AND THE RP SPLICEOSOME. RX PubMed=11544257; DOI=10.1074/jbc.m105453200; RA Ajuh P., Sleeman J., Chusainow J., Lamond A.I.; RT "A direct interaction between the carboxyl-terminal region of CDC5L and the RT WD40 domain of PLRG1 is essential for pre-mRNA splicing."; RL J. Biol. Chem. 276:42370-42381(2001). RN [7] RP PROTEIN SEQUENCE OF 81-113 AND 450-476, IDENTIFICATION BY MASS RP SPECTROMETRY, AND INTERACTION WITH THE SPLICEOSOME. RX PubMed=12176931; DOI=10.1101/gr.473902; RA Rappsilber J., Ryder U., Lamond A.I., Mann M.; RT "Large-scale proteomic analysis of the human spliceosome."; RL Genome Res. 12:1231-1245(2002). RN [8] 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 [9] RP IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX, RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION RP WITH CDC5L; PRPF19 AND BCAS2. RX PubMed=20176811; DOI=10.1128/mcb.01505-09; RA Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A., RA Fischle W., Urlaub H., Luhrmann R.; RT "Molecular architecture of the human Prp19/CDC5L complex."; RL Mol. Cell. Biol. 30:2105-2119(2010). RN [10] RP INTERACTION WITH USB1. RX PubMed=23022480; DOI=10.1016/j.celrep.2012.08.031; RA Shchepachev V., Wischnewski H., Missiaglia E., Soneson C., Azzalin C.M.; RT "Mpn1, mutated in poikiloderma with neutropenia protein 1, is a conserved RT 3'-to-5' RNA exonuclease processing U6 small nuclear RNA."; RL Cell Rep. 2:855-865(2012). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-201 AND SER-391, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [12] {ECO:0007744|PDB:4YVD} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 141-514. RA Zeng H., Dong A., Xu C., Tempel W., Li Y., He H., Bountra C., RA Arrowsmith C.H., Edwards A.M., Brown P.J., Min J., Wu H.; RT "Crystal structure of human Pleiotropic Regulator 1 (PRL1)."; RL Submitted (MAR-2015) to the PDB data bank. RN [13] {ECO:0007744|PDB:5XJC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. 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 [14] {ECO:0007744|PDB:5MQF} RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT, RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. 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 [15] {ECO:0007744|PDB:7DVQ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), FUNCTION, AND SUBUNIT. RX PubMed=33509932; DOI=10.1126/science.abg0879; RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.; RT "Structure of the activated human minor spliceosome."; RL Science 371:0-0(2021). CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome CC (PubMed:28502770, PubMed:28076346). Component of the PRP19-CDC5L CC complex that forms an integral part of the spliceosome and is required CC for activating pre-mRNA splicing (PubMed:11101529, PubMed:11544257). As CC a component of the minor spliceosome, involved in the splicing of U12- CC type introns in pre-mRNAs (Probable). {ECO:0000269|PubMed:11101529, CC ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000305|PubMed:33509932}. CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:12176931, CC PubMed:28502770, PubMed:28076346). Component of the PRP19-CDC5L CC splicing complex composed of a core complex comprising a homotetramer CC of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably CC associated proteins CTNNBL1, CWC15 and HSPA8 (PubMed:11101529, CC PubMed:20176811). Interacts (via its WD40 repeat domain) directly with CC CDC5L (via its C-terminal); the interaction is required for mRNA CC splicing but not for spliceosome assembly (PubMed:11544257). Component CC of the minor spliceosome, which splices U12-type introns. Within this CC complex, interacts with CRIPT (PubMed:33509932). Also interacts CC directly in the complex with BCAS2 and PRPF19 (PubMed:20176811). CC Interacts with USB1 (PubMed:23022480). {ECO:0000269|PubMed:11101529, CC ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:12176931, CC ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:23022480, CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, CC ECO:0000269|PubMed:33509932}. CC -!- INTERACTION: CC O43660; O75934: BCAS2; NbExp=2; IntAct=EBI-1051504, EBI-1050106; CC O43660; Q99459: CDC5L; NbExp=8; IntAct=EBI-1051504, EBI-374880; CC O43660; P52272: HNRNPM; NbExp=5; IntAct=EBI-1051504, EBI-486809; CC O43660-2; P54253: ATXN1; NbExp=3; IntAct=EBI-11743883, EBI-930964; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11101529, CC ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770}. Nucleus speckle CC {ECO:0000269|PubMed:11544257}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O43660-1; Sequence=Displayed; CC Name=2; CC IsoId=O43660-2; Sequence=VSP_008804; CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice CC site. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the WD repeat PRL1/PRL2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF044333; AAD09407.1; -; mRNA. DR EMBL; AK002108; BAG51016.1; -; mRNA. DR EMBL; CH471056; EAX04941.1; -; Genomic_DNA. DR EMBL; BC020786; AAH20786.1; -; mRNA. DR EMBL; BC106004; AAI06005.1; -; mRNA. DR CCDS; CCDS34083.1; -. [O43660-1] DR CCDS; CCDS56341.1; -. [O43660-2] DR RefSeq; NP_001188493.1; NM_001201564.1. [O43660-2] DR RefSeq; NP_002660.1; NM_002669.3. [O43660-1] DR PDB; 4YVD; X-ray; 1.70 A; A=141-514. DR PDB; 5MQF; EM; 5.90 A; D=1-514. DR PDB; 5XJC; EM; 3.60 A; T=1-514. DR PDB; 5YZG; EM; 4.10 A; T=1-514. DR PDB; 5Z56; EM; 5.10 A; T=1-514. DR PDB; 5Z57; EM; 6.50 A; T=1-514. DR PDB; 5Z58; EM; 4.90 A; T=1-514. DR PDB; 6FF4; EM; 16.00 A; D=1-514. DR PDB; 6FF7; EM; 4.50 A; D=1-514. DR PDB; 6ICZ; EM; 3.00 A; T=1-514. DR PDB; 6ID0; EM; 2.90 A; T=1-514. DR PDB; 6ID1; EM; 2.86 A; T=1-514. DR PDB; 6QDV; EM; 3.30 A; J=185-504. DR PDB; 6ZYM; EM; 3.40 A; D=1-514. DR PDB; 7AAV; EM; 4.20 A; G=1-514. DR PDB; 7ABF; EM; 3.90 A; G=1-514. DR PDB; 7ABG; EM; 7.80 A; G=1-514. DR PDB; 7ABI; EM; 8.00 A; G=1-514. DR PDB; 7DH6; X-ray; 2.58 A; A/B/C/D=140-514. DR PDB; 7DVQ; EM; 2.89 A; T=1-514. DR PDB; 7QTT; EM; 3.10 A; O=1-514. DR PDB; 7W59; EM; 3.60 A; T=1-514. DR PDB; 7W5A; EM; 3.60 A; T=1-514. DR PDB; 7W5B; EM; 4.30 A; T=1-514. DR PDB; 8C6J; EM; 2.80 A; J=1-514. DR PDB; 8CH6; EM; 5.90 A; O=1-514. DR PDBsum; 4YVD; -. DR PDBsum; 5MQF; -. DR PDBsum; 5XJC; -. DR PDBsum; 5YZG; -. DR PDBsum; 5Z56; -. DR PDBsum; 5Z57; -. DR PDBsum; 5Z58; -. DR PDBsum; 6FF4; -. DR PDBsum; 6FF7; -. DR PDBsum; 6ICZ; -. DR PDBsum; 6ID0; -. DR PDBsum; 6ID1; -. DR PDBsum; 6QDV; -. DR PDBsum; 6ZYM; -. DR PDBsum; 7AAV; -. DR PDBsum; 7ABF; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABI; -. DR PDBsum; 7DH6; -. DR PDBsum; 7DVQ; -. DR PDBsum; 7QTT; -. DR PDBsum; 7W59; -. DR PDBsum; 7W5A; -. DR PDBsum; 7W5B; -. DR PDBsum; 8C6J; -. DR PDBsum; 8CH6; -. DR AlphaFoldDB; O43660; -. DR EMDB; EMD-11569; -. DR EMDB; EMD-11693; -. DR EMDB; EMD-11694; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-14146; -. DR EMDB; EMD-16452; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-30875; -. DR EMDB; EMD-32317; -. DR EMDB; EMD-32319; -. DR EMDB; EMD-32321; -. DR EMDB; EMD-3545; -. DR EMDB; EMD-4255; -. DR EMDB; EMD-4525; -. DR EMDB; EMD-6721; -. DR EMDB; EMD-6864; -. DR EMDB; EMD-6889; -. DR EMDB; EMD-6890; -. DR EMDB; EMD-6891; -. DR EMDB; EMD-9645; -. DR EMDB; EMD-9646; -. DR EMDB; EMD-9647; -. DR SMR; O43660; -. DR BioGRID; 111370; 201. DR ComplexPortal; CPX-5824; PRP19-CDC5L complex. DR CORUM; O43660; -. DR IntAct; O43660; 71. DR MINT; O43660; -. DR STRING; 9606.ENSP00000424417; -. DR GlyCosmos; O43660; 1 site, 1 glycan. DR GlyGen; O43660; 4 sites, 2 O-linked glycans (4 sites). DR iPTMnet; O43660; -. DR MetOSite; O43660; -. DR PhosphoSitePlus; O43660; -. DR SwissPalm; O43660; -. DR BioMuta; PLRG1; -. DR EPD; O43660; -. DR jPOST; O43660; -. DR MassIVE; O43660; -. DR MaxQB; O43660; -. DR PaxDb; 9606-ENSP00000424417; -. DR PeptideAtlas; O43660; -. DR ProteomicsDB; 49091; -. [O43660-1] DR ProteomicsDB; 49092; -. [O43660-2] DR Pumba; O43660; -. DR Antibodypedia; 16702; 281 antibodies from 30 providers. DR DNASU; 5356; -. DR Ensembl; ENST00000302078.9; ENSP00000303191.5; ENSG00000171566.12. [O43660-2] DR Ensembl; ENST00000499023.7; ENSP00000424417.1; ENSG00000171566.12. [O43660-1] DR GeneID; 5356; -. DR KEGG; hsa:5356; -. DR MANE-Select; ENST00000499023.7; ENSP00000424417.1; NM_002669.4; NP_002660.1. DR UCSC; uc003iny.4; human. [O43660-1] DR AGR; HGNC:9089; -. DR CTD; 5356; -. DR DisGeNET; 5356; -. DR GeneCards; PLRG1; -. DR HGNC; HGNC:9089; PLRG1. DR HPA; ENSG00000171566; Low tissue specificity. DR MIM; 605961; gene. DR neXtProt; NX_O43660; -. DR OpenTargets; ENSG00000171566; -. DR PharmGKB; PA33416; -. DR VEuPathDB; HostDB:ENSG00000171566; -. DR eggNOG; KOG0285; Eukaryota. DR GeneTree; ENSGT00940000155316; -. DR HOGENOM; CLU_000288_72_2_1; -. DR InParanoid; O43660; -. DR OMA; FAMCFDQ; -. DR OrthoDB; 118158at2759; -. DR PhylomeDB; O43660; -. DR TreeFam; TF105684; -. DR PathwayCommons; O43660; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; O43660; -. DR SIGNOR; O43660; -. DR BioGRID-ORCS; 5356; 744 hits in 1154 CRISPR screens. DR ChiTaRS; PLRG1; human. DR GeneWiki; PLRG1; -. DR GenomeRNAi; 5356; -. DR Pharos; O43660; Tbio. DR PRO; PR:O43660; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; O43660; Protein. DR Bgee; ENSG00000171566; Expressed in secondary oocyte and 185 other cell types or tissues. DR ExpressionAtlas; O43660; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000974; C:Prp19 complex; IPI:ComplexPortal. DR GO; GO:0005681; C:spliceosomal complex; IPI:ComplexPortal. DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl. DR CDD; cd00200; WD40; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR045241; Prp46/PLRG1-like. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19923:SF0; PLEIOTROPIC REGULATOR 1; 1. DR PANTHER; PTHR19923; WD40 REPEAT PROTEINPRL1/PRL2-RELATED; 1. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; O43660; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Spliceosome; WD repeat. FT CHAIN 1..514 FT /note="Pleiotropic regulator 1" FT /id="PRO_0000051133" FT REPEAT 202..241 FT /note="WD 1" FT REPEAT 244..283 FT /note="WD 2" FT REPEAT 286..325 FT /note="WD 3" FT REPEAT 328..367 FT /note="WD 4" FT REPEAT 370..410 FT /note="WD 5" FT REPEAT 411..449 FT /note="WD 6" FT REPEAT 460..499 FT /note="WD 7" FT REGION 135..160 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 119 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 201 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 391 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 96..104 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_008804" FT STRAND 194..200 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 207..212 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 216..223 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 228..232 FT /evidence="ECO:0007829|PDB:4YVD" FT TURN 233..235 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 238..242 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 249..254 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 256..265 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 270..274 FT /evidence="ECO:0007829|PDB:4YVD" FT TURN 275..278 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 279..283 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 291..296 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 298..307 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 310..316 FT /evidence="ECO:0007829|PDB:4YVD" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 322..327 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 333..338 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 340..343 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 345..349 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 354..358 FT /evidence="ECO:0007829|PDB:4YVD" FT TURN 359..362 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 363..368 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 377..380 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 384..390 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 395..399 FT /evidence="ECO:0007829|PDB:4YVD" FT TURN 400..403 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 404..409 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 416..421 FT /evidence="ECO:0007829|PDB:4YVD" FT TURN 423..425 FT /evidence="ECO:0007829|PDB:6ID0" FT STRAND 426..431 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 436..440 FT /evidence="ECO:0007829|PDB:4YVD" FT TURN 441..443 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 446..450 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 456..458 FT /evidence="ECO:0007829|PDB:6ID0" FT HELIX 460..462 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 465..470 FT /evidence="ECO:0007829|PDB:4YVD" FT STRAND 472..475 FT /evidence="ECO:0007829|PDB:6FF4" FT STRAND 476..481 FT /evidence="ECO:0007829|PDB:4YVD" FT TURN 482..484 FT /evidence="ECO:0007829|PDB:6ICZ" FT STRAND 486..491 FT /evidence="ECO:0007829|PDB:4YVD" FT TURN 497..499 FT /evidence="ECO:0007829|PDB:7DVQ" SQ SEQUENCE 514 AA; 57194 MW; 8C914CAF5F7887BD CRC64; MVEEVQKHSV HTLVFRSLKR THDMFVADNG KPVPLDEESH KRKMAIKLRN EYGPVLHMPT SKENLKEKGP QNATDSYVHK QYPANQGQEV EYFVAGTHPY PPGPGVALTA DTKIQRMPSE SAAQSLAVAL PLQTKADANR TAPSGSEYRH PGASDRPQPT AMNSIVMETG NTKNSALMAK KAPTMPKPQW HPPWKLYRVI SGHLGWVRCI AVEPGNQWFV TGSADRTIKI WDLASGKLKL SLTGHISTVR GVIVSTRSPY LFSCGEDKQV KCWDLEYNKV IRHYHGHLSA VYGLDLHPTI DVLVTCSRDS TARIWDVRTK ASVHTLSGHT NAVATVRCQA AEPQIITGSH DTTIRLWDLV AGKTRVTLTN HKKSVRAVVL HPRHYTFASG SPDNIKQWKF PDGSFIQNLS GHNAIINTLT VNSDGVLVSG ADNGTMHLWD WRTGYNFQRV HAAVQPGSLD SESGIFACAF DQSESRLLTA EADKTIKVYR EDDTATEETH PVSWKPEIIK RKRF //