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}.
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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 Genevisible; O43660; HS.
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.
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
//
