PUF5_CAEEL
ID PUF5_CAEEL Reviewed; 553 AA.
AC Q20757;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Pumilio domain-containing protein 5 {ECO:0000303|PubMed:17234175};
GN Name=puf-5 {ECO:0000312|EMBL:CAA90254.1, ECO:0000312|WormBase:F54C9.8};
GN ORFNames=F54C9.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17234175; DOI=10.1016/j.ydbio.2006.12.004;
RA Lublin A.L., Evans T.C.;
RT "The RNA-binding proteins PUF-5, PUF-6, and PUF-7 reveal multiple systems
RT for maternal mRNA regulation during C. elegans oogenesis.";
RL Dev. Biol. 303:635-649(2007).
RN [2] {ECO:0000312|EMBL:CAA90254.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA90254.1};
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 [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18695046; DOI=10.1083/jcb.200802128;
RA Noble S.L., Allen B.L., Goh L.K., Nordick K., Evans T.C.;
RT "Maternal mRNAs are regulated by diverse P body-related mRNP granules
RT during early Caenorhabditis elegans development.";
RL J. Cell Biol. 182:559-572(2008).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=18579869; DOI=10.1261/rna.1095908;
RA Stumpf C.R., Kimble J., Wickens M.;
RT "A Caenorhabditis elegans PUF protein family with distinct RNA binding
RT specificity.";
RL RNA 14:1550-1557(2008).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22542599; DOI=10.1016/j.ydbio.2012.03.019;
RA Hubstenberger A., Cameron C., Shtofman R., Gutman S., Evans T.C.;
RT "A network of PUF proteins and Ras signaling promote mRNA repression and
RT oogenesis in C. elegans.";
RL Dev. Biol. 366:218-231(2012).
CC -!- FUNCTION: RNA-binding protein that binds to the consensus sequence 5'-
CC CUCUGUAUCUUGU-3' in mRNA 3'-UTRs and modulates mRNA expression and
CC stability. Functions redundantly with puf-6 and puf-7 in oocyte
CC formation and organization, early embryonic cell divisions, and
CC repression of expression of glp-1 and other maternal mRNAs in late
CC oogenesis. {ECO:0000269|PubMed:17234175, ECO:0000269|PubMed:18579869,
CC ECO:0000269|PubMed:18695046, ECO:0000269|PubMed:22542599}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17234175,
CC ECO:0000269|PubMed:18695046}. Cytoplasm, P-body. Note=Localizes to
CC perinuclear and cytoplasmic P granules. {ECO:0000269|PubMed:17234175,
CC ECO:0000269|PubMed:18695046}.
CC -!- TISSUE SPECIFICITY: Detected in differentiating oocytes with highest
CC levels observed in developing ooctyes in the distal portion of the
CC proximal gonad. {ECO:0000269|PubMed:17234175}.
CC -!- DEVELOPMENTAL STAGE: Expressed during a specific period of late
CC oogenesis, from late meiotic pachytene to late diakinesis. Repressed
CC prior to terminal oocyte differentiation.
CC {ECO:0000269|PubMed:17234175}.
CC -!- DISRUPTION PHENOTYPE: Production of viable embryos and predominantly
CC normal oocytes with a low percentage showing misorganization. Does not
CC affect germline development in adult hermaphrodites. Impaired
CC repression of glp-1 and fog-1. Simultaneous knockdown of puf-5, puf-6
CC and puf-7 results in abnormally small oocytes, disorganization of
CC oocyte nuclei and cells, inefficient yolk uptake by oocytes, embryonic
CC arrest with impaired eggshell formation and cytokinesis defects,
CC impaired repression of glp-1 in late oogenesis, and mislocalization of
CC rme-2 to the cytoplasm instead of the plasma membrane.
CC {ECO:0000269|PubMed:17234175, ECO:0000269|PubMed:18695046,
CC ECO:0000269|PubMed:22542599}.
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DR EMBL; Z49967; CAA90254.1; -; Genomic_DNA.
DR PIR; T22634; T22634.
DR RefSeq; NP_495814.1; NM_063413.3.
DR AlphaFoldDB; Q20757; -.
DR SMR; Q20757; -.
DR BioGRID; 39701; 1.
DR STRING; 6239.F54C9.8; -.
DR EPD; Q20757; -.
DR PaxDb; Q20757; -.
DR PeptideAtlas; Q20757; -.
DR EnsemblMetazoa; F54C9.8.1; F54C9.8.1; WBGene00004241.
DR GeneID; 174373; -.
DR KEGG; cel:CELE_F54C9.8; -.
DR UCSC; F54C9.8; c. elegans.
DR CTD; 174373; -.
DR WormBase; F54C9.8; CE02258; WBGene00004241; puf-5.
DR eggNOG; KOG1488; Eukaryota.
DR GeneTree; ENSGT00970000196107; -.
DR HOGENOM; CLU_028494_0_0_1; -.
DR InParanoid; Q20757; -.
DR OMA; MDISAHF; -.
DR OrthoDB; 1364009at2759; -.
DR PhylomeDB; Q20757; -.
DR PRO; PR:Q20757; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004241; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0040019; P:positive regulation of embryonic development; IGI:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR Pfam; PF00806; PUF; 7.
DR SMART; SM00025; Pumilio; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50302; PUM; 8.
DR PROSITE; PS50303; PUM_HD; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Developmental protein;
KW Differentiation; Oogenesis; Reference proteome; Repeat; RNA-binding;
KW Translation regulation.
FT CHAIN 1..553
FT /note="Pumilio domain-containing protein 5"
FT /id="PRO_0000424283"
FT REPEAT 146..184
FT /note="Pumilio 1"
FT /evidence="ECO:0000255"
FT REPEAT 185..223
FT /note="Pumilio 2"
FT /evidence="ECO:0000255"
FT REPEAT 224..260
FT /note="Pumilio 3"
FT /evidence="ECO:0000255"
FT REPEAT 261..296
FT /note="Pumilio 4"
FT /evidence="ECO:0000255"
FT REPEAT 297..335
FT /note="Pumilio 5"
FT /evidence="ECO:0000255"
FT REPEAT 347..384
FT /note="Pumilio 6"
FT /evidence="ECO:0000255"
FT REPEAT 386..421
FT /note="Pumilio 7"
FT /evidence="ECO:0000255"
FT REPEAT 432..472
FT /note="Pumilio 8"
FT /evidence="ECO:0000255"
FT REGION 499..514
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:O44169"
SQ SEQUENCE 553 AA; 62575 MW; BA5FFB24F4E2DC1F CRC64;
MSDSTGRINS KASDSSSISD HQTADLSIFN GSFDGGAFSS SNIPLFNFMG TGNQRFQYSP
HPFAKSSDPC RLAALTPSTP KGPLNLTPAD FGLADFSVGN ESFADFTANN TSFVGNVQSN
VRSTRLLPAW AVDNSGNIRD DLTLQDVVSN GSLIDFAMDR TGVKFLERHF PEDHDNEMHF
VLFDKLTEQG AVFTSLCRSA AGNFIIQKFV EHATLDEQER LVRKMCDNGL IEMCLDKFAC
RVVQMSIQKF DVSIAMKLVE KISSLDFLPL CTDQCAIHVL QKVVKLLPIS AWSFFVKFLC
RDDNLMTVCQ DKYGCRLVQQ TIDKLSDNPK LHCFNTRLQL LHGLMTSVAR NCFRLSSNEF
ANYVVQYVIK SSGVMEMYRD TIIEKCLLRN ILSMSQDKYA SHVVEGAFLF APPLLLSEMM
DEIFDGYVKD QETNRDALDI LLFHQYGNYV VQQMISICIS ALLGKEERKM VASEMRLYAK
WFDRIKNRVN RHSGRLERFS SGKKIIESLQ KLNVPMTMTN EPMPYWAMPT PLMDISAHFM
NKLNFQKNSV FDE
