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PLP1_CAEEL
ID   PLP1_CAEEL              Reviewed;         226 AA.
AC   Q94230;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Transcriptional activator plp-1 {ECO:0000305};
DE   AltName: Full=Pur-alpha-like protein 1 {ECO:0000303|PubMed:16267406};
GN   Name=plp-1 {ECO:0000303|PubMed:16267406, ECO:0000312|WormBase:F45E4.2};
GN   ORFNames=F45E4.2 {ECO:0000312|WormBase:F45E4.2};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16267406;
RA   Im S.H., Lee J.;
RT   "PLP-1 binds nematode double-stranded telomeric DNA.";
RL   Mol. Cells 20:297-302(2005).
RN   [3] {ECO:0000305}
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=19084000; DOI=10.1016/j.ydbio.2008.11.015;
RA   Witze E.S., Field E.D., Hunt D.F., Rothman J.H.;
RT   "C. elegans pur alpha, an activator of end-1, synergizes with the Wnt
RT   pathway to specify endoderm.";
RL   Dev. Biol. 327:12-23(2009).
RN   [4] {ECO:0000305}
RP   DISRUPTION PHENOTYPE.
RX   PubMed=25439098; DOI=10.1016/j.ajhg.2014.09.014;
RA   Lalani S.R., Zhang J., Schaaf C.P., Brown C.W., Magoulas P., Tsai A.C.,
RA   El-Gharbawy A., Wierenga K.J., Bartholomew D., Fong C.T.,
RA   Barbaro-Dieber T., Kukolich M.K., Burrage L.C., Austin E., Keller K.,
RA   Pastore M., Fernandez F., Lotze T., Wilfong A., Purcarin G., Zhu W.,
RA   Craigen W.J., McGuire M., Jain M., Cooney E., Azamian M., Bainbridge M.N.,
RA   Muzny D.M., Boerwinkle E., Person R.E., Niu Z., Eng C.M., Lupski J.R.,
RA   Gibbs R.A., Beaudet A.L., Yang Y., Wang M.C., Xia F.;
RT   "Mutations in PURA cause profound neonatal hypotonia, seizures, and
RT   encephalopathy in 5q31.3 microdeletion syndrome.";
RL   Am. J. Hum. Genet. 95:579-583(2014).
CC   -!- FUNCTION: Probable transcription activator (PubMed:19084000). Binds
CC       telomeric DNA containing repeats of the sequence, 5'-TTAGGC-3'
CC       (PubMed:16267406). Binds to end-1 promoter, activating end-1
CC       expression, which is required for endoderm specification during
CC       embryonic development (PubMed:19084000). {ECO:0000269|PubMed:16267406,
CC       ECO:0000269|PubMed:19084000}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19084000}. Chromosome
CC       {ECO:0000269|PubMed:16267406, ECO:0000269|PubMed:19084000}.
CC       Note=localizes to nuclei of interphase cells throughout early
CC       embryogenesis. Localizes to the nucleus in a lit-1 dependent manner.
CC       Transiently asymmetrically localizes during telophase of the dividing
CC       EMS cell with higher levels in the future E cell nucleus and low or
CC       undetectable levels in that of the MS cell.
CC       {ECO:0000269|PubMed:19084000}.
CC   -!- DEVELOPMENTAL STAGE: First expressed in blastomeres at the two cell
CC       stage of embryogenesis (PubMed:19084000). Also expressed in germline-
CC       specific P granules of early embryos (PubMed:19084000).
CC       {ECO:0000269|PubMed:19084000}.
CC   -!- DISRUPTION PHENOTYPE: Sterile due to lack of oocytes (PubMed:25439098).
CC       Defective locomotion, marked by a 3-fold reduction in speed
CC       (PubMed:25439098). RNAi-mediated knockdown causes embryonic lethality
CC       (PubMed:19084000). RNAi-mediated knockdown substantially reduces
CC       expression of end-1 (PubMed:19084000). RNAi-mediated knockdown
CC       abolishes formation of endoderm in 3% of embryos and in 35% of embryos
CC       on a mom-5 mutant background (PubMed:19084000).
CC       {ECO:0000269|PubMed:19084000, ECO:0000269|PubMed:25439098}.
CC   -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
CC       {ECO:0000305}.
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DR   EMBL; BX284604; CCD63777.1; -; Genomic_DNA.
DR   PIR; T25756; T25756.
DR   RefSeq; NP_501241.1; NM_068840.4.
DR   AlphaFoldDB; Q94230; -.
DR   SMR; Q94230; -.
DR   IntAct; Q94230; 2.
DR   STRING; 6239.F45E4.2; -.
DR   EPD; Q94230; -.
DR   PaxDb; Q94230; -.
DR   PeptideAtlas; Q94230; -.
DR   EnsemblMetazoa; F45E4.2.1; F45E4.2.1; WBGene00004046.
DR   GeneID; 177540; -.
DR   KEGG; cel:CELE_F45E4.2; -.
DR   UCSC; F45E4.2.1; c. elegans.
DR   CTD; 177540; -.
DR   WormBase; F45E4.2; CE10494; WBGene00004046; plp-1.
DR   eggNOG; KOG3074; Eukaryota.
DR   GeneTree; ENSGT00950000183162; -.
DR   HOGENOM; CLU_057873_1_1_1; -.
DR   InParanoid; Q94230; -.
DR   OMA; TRGRYIK; -.
DR   OrthoDB; 1248813at2759; -.
DR   PhylomeDB; Q94230; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00004046; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0043186; C:P granule; IDA:WormBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:WormBase.
DR   GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:WormBase.
DR   GO; GO:0032422; F:purine-rich negative regulatory element binding; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR   GO; GO:0007281; P:germ cell development; IMP:WormBase.
DR   GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR006628; PUR-bd_fam.
DR   PANTHER; PTHR12611; PTHR12611; 1.
DR   Pfam; PF04845; PurA; 1.
DR   SMART; SM00712; PUR; 3.
PE   1: Evidence at protein level;
KW   Activator; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..226
FT                   /note="Transcriptional activator plp-1"
FT                   /id="PRO_0000451293"
SQ   SEQUENCE   226 AA;  25515 MW;  A91A8ADABA72CD67 CRC64;
     MSDGSVERGT KRAEDSLATH QLTVQYKRYY IDVNENTRGR YIKIAELGTN YKSRIILSIV
     AAKAIVSEIS KMLALIDEPS TGEHAPKESS LIKSETLNVD GRKFYVDLKE NVRGRFLRIA
     QMPMNPRQTR QQIAIPSDGI AEIHKVLTEY LAKFGEGHEQ ENTNTPKITA ENKSFLFHSG
     KNDRGEFVRI SEIKLNSGYR NAITVPMSAL VDFRKELDNI IANQGK
 
 
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