PIE1_CAEEL
ID PIE1_CAEEL Reviewed; 335 AA.
AC Q94131; E9P8A6; Q9XTT5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Pharynx and intestine in excess protein 1;
DE Short=Protein pie-1;
GN Name=pie-1 {ECO:0000312|WormBase:Y49E10.14a};
GN Synonyms=pic-1 {ECO:0000312|WormBase:Y49E10.14a};
GN ORFNames=Y49E10.14 {ECO:0000312|WormBase:Y49E10.14a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=8751440; DOI=10.1038/382710a0;
RA Mello C.C., Schubert C., Draper B., Zhang W., Lobel R., Priess J.R.;
RT "The PIE-1 protein and germline specification in C. elegans embryos.";
RL Nature 382:710-712(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=1623520; DOI=10.1016/0092-8674(92)90542-k;
RA Mello C.C., Draper B.W., Krause M., Weintraub H., Priess J.R.;
RT "The pie-1 and mex-1 genes and maternal control of blastomere identity in
RT early C. elegans embryos.";
RL Cell 70:163-176(1992).
RN [4]
RP CHARACTERIZATION.
RX PubMed=8751441; DOI=10.1038/382713a0;
RA Seydoux G., Mello C.C., Pettitt J., Wood W.B., Priess J.R., Fire A.;
RT "Repression of gene expression in the embryonic germ lineage of C.
RT elegans.";
RL Nature 382:713-716(1996).
RN [5]
RP FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=JJ532;
RX PubMed=10983990; DOI=10.1016/s1097-2765(00)00043-5;
RA Reese K.J., Dunn M.A., Waddle J.A., Seydoux G.;
RT "Asymmetric segregation of PIE-1 in C. elegans is mediated by two
RT complementary mechanisms that act through separate PIE-1 protein domains.";
RL Mol. Cell 6:445-455(2000).
RN [6]
RP FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 69-ARG--LEU-72.
RC STRAIN=JJ532;
RX PubMed=11316796; DOI=10.1101/gad.876201;
RA Tenenhaus C., Subramaniam K., Dunn M.A., Seydoux G.;
RT "PIE-1 is a bifunctional protein that regulates maternal and zygotic gene
RT expression in the embryonic germ line of Caenorhabditis elegans.";
RL Genes Dev. 15:1031-1040(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH HDA-1; LET-418 AND MEP-1.
RX PubMed=12507426; DOI=10.1016/s0092-8674(02)01202-3;
RA Unhavaithaya Y., Shin T.H., Miliaras N., Lee J., Oyama T., Mello C.C.;
RT "MEP-1 and a homolog of the NURD complex component Mi-2 act together to
RT maintain germline-soma distinctions in C. elegans.";
RL Cell 111:991-1002(2002).
RN [8]
RP FUNCTION, AND INTERACTION WITH CIT-1.1.
RX PubMed=12651893; DOI=10.1101/gad.1068203;
RA Zhang F., Barboric M., Blackwell T.K., Peterlin B.M.;
RT "A model of repression: CTD analogs and PIE-1 inhibit transcriptional
RT elongation by P-TEFb.";
RL Genes Dev. 17:748-758(2003).
RN [9]
RP FUNCTION, INTERACTION WITH CIT-1.1, AND SUBCELLULAR LOCATION.
RX PubMed=18202370; DOI=10.1534/genetics.107.083212;
RA Ghosh D., Seydoux G.;
RT "Inhibition of transcription by the Caenorhabditis elegans germline protein
RT PIE-1: genetic evidence for distinct mechanisms targeting initiation and
RT elongation.";
RL Genetics 178:235-243(2008).
RN [10]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=30279189; DOI=10.1534/g3.118.200744;
RA Gauvin T.J., Han B., Sun M.J., Griffin E.E.;
RT "PIE-1 Translation in the Germline Lineage Contributes to PIE-1 Asymmetry
RT in the Early Caenorhabditis elegans Embryo.";
RL G3 (Bethesda) 8:3791-3801(2018).
CC -!- FUNCTION: Maternally provided PIE-1 is required for germline cell fate
CC determination. Functions as a repressor of RNA polymerase II-dependent
CC gene expression in the developing germline. Required for expression of
CC nos-2 in P4 germline blastomere cells. Inhibits the histone deacetylase
CC activity of hda-1. Represses transcriptional activation of cdk-9 and
CC cit-1.1, which are members of the P-TEFb complex.
CC {ECO:0000269|PubMed:10983990, ECO:0000269|PubMed:11316796,
CC ECO:0000269|PubMed:12507426, ECO:0000269|PubMed:12651893,
CC ECO:0000269|PubMed:1623520, ECO:0000269|PubMed:18202370}.
CC -!- SUBUNIT: Interacts with hda-1, let-418 and mep-1. Interacts (via C
CC terminus) with cit-1.1 (via C terminus). {ECO:0000269|PubMed:12507426,
CC ECO:0000269|PubMed:12651893, ECO:0000269|PubMed:18202370}.
CC -!- INTERACTION:
CC Q94131; Q22805: CELE_T26A8.4; NbExp=3; IntAct=EBI-300501, EBI-2415565;
CC Q94131; O17695: hda-1; NbExp=3; IntAct=EBI-300501, EBI-318045;
CC Q94131; Q21502: mep-1; NbExp=3; IntAct=EBI-300501, EBI-319858;
CC Q94131; P34482: zif-1; NbExp=2; IntAct=EBI-300501, EBI-300497;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30279189}. Cytoplasm
CC {ECO:0000269|PubMed:30279189}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Cytoplasm, cytoskeleton, spindle.
CC Cytoplasmic granule. Note=Initially associates with both centrosomes of
CC the mitotic spindle. Rapidly disappears from the centrosome destined
CC for the somatic daughter and persists in the centrosome of the daughter
CC that becomes the next germline blastomere. Accumulates in larger
CC cytoplasmic granules (P granules), which are visible around the nuclei
CC in the micrographs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y49E10.14a};
CC IsoId=Q94131-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y49E10.14b};
CC IsoId=Q94131-2; Sequence=VSP_044040;
CC -!- DEVELOPMENTAL STAGE: Expressed in 1, 2 and 4-cell embryos (at protein
CC level) (PubMed:10983990, PubMed:30279189). Expression increases between
CC P0 (the zygote) and P2 blastomeres due to its asymmetric segregation in
CC P1 and P2 blastomeres, its degradation in somatic cells and its
CC translation in the P lineage (at protein level) (PubMed:30279189).
CC {ECO:0000269|PubMed:10983990, ECO:0000269|PubMed:30279189}.
CC -!- DOMAIN: The C3H1-type 1 domain is required for degradation in somatic
CC blastomeres.
CC -!- DOMAIN: The C3H1-type 2 domain targets the protein to P granules, is
CC involved in germ cell positioning in embryos and is required for
CC default nos-2 expression.
CC -!- DISRUPTION PHENOTYPE: Disrupts blastomere cell fate. Excessive
CC pharyngeal cells produced during embryogenesis. Reduced expression of
CC nos-2 in P4 germline blastomeres and absence of nos-2 protein.
CC {ECO:0000269|PubMed:11316796}.
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DR EMBL; U62896; AAB17868.1; -; mRNA.
DR EMBL; BX284603; CAB11564.2; -; Genomic_DNA.
DR EMBL; BX284603; CBZ39492.1; -; Genomic_DNA.
DR PIR; S71796; S71796.
DR PIR; T27052; T27052.
DR RefSeq; NP_001255166.1; NM_001268237.1. [Q94131-1]
DR RefSeq; NP_001255167.1; NM_001268238.1. [Q94131-2]
DR AlphaFoldDB; Q94131; -.
DR BioGRID; 41846; 54.
DR DIP; DIP-25777N; -.
DR IntAct; Q94131; 27.
DR STRING; 6239.Y49E10.14a.2; -.
DR EPD; Q94131; -.
DR PaxDb; Q94131; -.
DR PeptideAtlas; Q94131; -.
DR PRIDE; Q94131; -.
DR EnsemblMetazoa; Y49E10.14a.1; Y49E10.14a.1; WBGene00004027. [Q94131-1]
DR EnsemblMetazoa; Y49E10.14b.1; Y49E10.14b.1; WBGene00004027. [Q94131-2]
DR GeneID; 176667; -.
DR KEGG; cel:CELE_Y49E10.14; -.
DR UCSC; Y49E10.14.1; c. elegans. [Q94131-1]
DR CTD; 176667; -.
DR WormBase; Y49E10.14a; CE28134; WBGene00004027; pie-1. [Q94131-1]
DR WormBase; Y49E10.14b; CE45773; WBGene00004027; pie-1. [Q94131-2]
DR eggNOG; KOG1677; Eukaryota.
DR HOGENOM; CLU_772173_0_0_1; -.
DR InParanoid; Q94131; -.
DR OMA; CPARIQN; -.
DR OrthoDB; 544208at2759; -.
DR PhylomeDB; Q94131; -.
DR SignaLink; Q94131; -.
DR PRO; PR:Q94131; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004027; Expressed in germ line (C elegans) and 13 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0001709; P:cell fate determination; IMP:WormBase.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:WormBase.
DR GO; GO:0001704; P:formation of primary germ layer; IMP:WormBase.
DR GO; GO:0031064; P:negative regulation of histone deacetylation; IDA:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:WormBase.
DR InterPro; IPR045877; ZFP36-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12547; PTHR12547; 2.
DR Pfam; PF00642; zf-CCCH; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..335
FT /note="Pharynx and intestine in excess protein 1"
FT /id="PRO_0000089176"
FT ZN_FING 98..126
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 184..211
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 130..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..291
FT /note="Required for inhibition of Ser-2 phosphorylation"
FT COMPBIAS 130..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..211
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_044040"
FT MUTAGEN 69..72
FT /note="REAL->AEAA: Disrupts efficient nucleus localization
FT and transcriptional repression in germline blastomeres."
FT /evidence="ECO:0000269|PubMed:11316796"
SQ SEQUENCE 335 AA; 38364 MW; 31513EE4E72B4880 CRC64;
MAQTKPIAEQ MAALNNSDDT SFAADRSNSL LNATCPARIQ NSVDQRKINR SFNDSLSSGY
SGKWLRPKRE ALKITPLAQI DEAPATKRHS SAKDKHTEYK TRLCDAFRRE GYCPYNDNCT
YAHGQDELRV PRRRQEYYSR DPPRERRDSR SRRDDVDTTI NRSSSSASKH HDENRRPSNN
HGSSNRRQIC HNFERGNCRY GPRCRFIHVE QMQHFNANAT VYAPPSSDCP PPIAYYHHHP
QHQQQFLPFP MPYFLAPPPQ AQQGAPFPVQ YIPQQHDLMN SQPMYAPMAP TYYYQPINSN
GMPMMDVTID PNATGGAFEV FPDGFFSQPP PTIIS
