14332_CAEEL
ID 14332_CAEEL Reviewed; 248 AA.
AC Q20655;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=14-3-3-like protein 2;
GN Name=ftt-2 {ECO:0000312|WormBase:F52D10.3a};
GN ORFNames=F52D10.3 {ECO:0000312|WormBase:F52D10.3a};
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 [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 [2]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DAF-16 AND
RP SIR-2.1, AND SUBCELLULAR LOCATION.
RX PubMed=16777605; DOI=10.1016/j.cell.2006.04.036;
RA Berdichevsky A., Viswanathan M., Horvitz H.R., Guarente L.;
RT "C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and
RT extend life span.";
RL Cell 125:1165-1177(2006).
RN [3]
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ASP-240.
RX PubMed=17371877; DOI=10.1074/jbc.m611051200;
RA Taylor R.C., Brumatti G., Ito S., Hengartner M.O., Derry W.B., Martin S.J.;
RT "Establishing a blueprint for CED-3-dependent killing through
RT identification of multiple substrates for this protease.";
RL J. Biol. Chem. 282:15011-15021(2007).
RN [4]
RP FUNCTION, INTERACTION WITH DAF-16, AND SUBCELLULAR LOCATION.
RX PubMed=21531333; DOI=10.1016/j.cmet.2011.03.017;
RA Takahashi Y., Daitoku H., Hirota K., Tamiya H., Yokoyama A., Kako K.,
RA Nagashima Y., Nakamura A., Shimada T., Watanabe S., Yamagata K., Yasuda K.,
RA Ishii N., Fukamizu A.;
RT "Asymmetric arginine dimethylation determines life span in C. elegans by
RT regulating forkhead transcription factor DAF-16.";
RL Cell Metab. 13:505-516(2011).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION HCF-1.
RX PubMed=21909281; DOI=10.1371/journal.pgen.1002235;
RA Rizki G., Iwata T.N., Li J., Riedel C.G., Picard C.L., Jan M., Murphy C.T.,
RA Lee S.S.;
RT "The evolutionarily conserved longevity determinants HCF-1 and SIR-
RT 2.1/SIRT1 collaborate to regulate DAF-16/FOXO.";
RL PLoS Genet. 7:E1002235-E1002235(2011).
RN [6]
RP FUNCTION.
RX PubMed=23396260; DOI=10.1016/j.yexcr.2013.01.020;
RA Iwasa H., Maimaiti S., Kuroyanagi H., Kawano S., Inami K., Timalsina S.,
RA Ikeda M., Nakagawa K., Hata Y.;
RT "Yes-associated protein homolog, YAP-1, is involved in the thermotolerance
RT and aging in the nematode Caenorhabditis elegans.";
RL Exp. Cell Res. 319:931-945(2013).
CC -!- FUNCTION: Required for extension of lifespan by sir-2.1
CC (PubMed:16777605). Required to modulate lifespan, in concert with hcf-
CC 1, acting redundantly with 14-3-3-like protein par-5 (PubMed:21909281).
CC Promotes nuclear export of yap-1 (PubMed:23396260). Negatively
CC regulates the transcriptional activity of daf-16 by sequestering it to
CC the cytoplasm (PubMed:21531333). {ECO:0000269|PubMed:16777605,
CC ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:21909281,
CC ECO:0000269|PubMed:23396260}.
CC -!- SUBUNIT: Interacts with daf-16 (PubMed:16777605, PubMed:21531333).
CC Interacts with sir-2.1 (PubMed:16777605). Interacts with hcf-1
CC (PubMed:21909281). {ECO:0000269|PubMed:16777605,
CC ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:21909281}.
CC -!- INTERACTION:
CC Q20655; G5EC23: hcf-1; NbExp=2; IntAct=EBI-966073, EBI-4480523;
CC Q20655; Q11184: let-756; NbExp=3; IntAct=EBI-966073, EBI-3843983;
CC Q20655; Q21921: sir-2.1; NbExp=3; IntAct=EBI-966073, EBI-966082;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16777605,
CC ECO:0000305|PubMed:21531333}. Nucleus {ECO:0000269|PubMed:16777605}.
CC -!- SIMILARITY: Belongs to the 14-3-3 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; Z66564; CAA91474.1; -; Genomic_DNA.
DR PIR; T22500; T22500.
DR RefSeq; NP_509939.1; NM_077538.4.
DR AlphaFoldDB; Q20655; -.
DR SMR; Q20655; -.
DR BioGRID; 46256; 26.
DR ComplexPortal; CPX-3882; daf-16-ftt-2 complex.
DR ComplexPortal; CPX-3885; sir-2.1-ftt-2 complex.
DR DIP; DIP-25505N; -.
DR IntAct; Q20655; 8.
DR STRING; 6239.F52D10.3a.1; -.
DR iPTMnet; Q20655; -.
DR World-2DPAGE; 0020:Q20655; -.
DR EPD; Q20655; -.
DR PaxDb; Q20655; -.
DR PeptideAtlas; Q20655; -.
DR EnsemblMetazoa; F52D10.3a.1; F52D10.3a.1; WBGene00001502.
DR GeneID; 181348; -.
DR UCSC; F52D10.3b.1; c. elegans.
DR CTD; 181348; -.
DR WormBase; F52D10.3a; CE03389; WBGene00001502; ftt-2.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; Q20655; -.
DR OMA; ERVCQDV; -.
DR PhylomeDB; Q20655; -.
DR Reactome; R-CEL-165159; MTOR signalling.
DR Reactome; R-CEL-166208; mTORC1-mediated signalling.
DR Reactome; R-CEL-170968; Frs2-mediated activation.
DR Reactome; R-CEL-2028269; Signaling by Hippo.
DR Reactome; R-CEL-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-CEL-392517; Rap1 signalling.
DR Reactome; R-CEL-430116; GP1b-IX-V activation signalling.
DR Reactome; R-CEL-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-CEL-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR Reactome; R-CEL-5673000; RAF activation.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR Reactome; R-CEL-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-CEL-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-CEL-9013700; NOTCH4 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-CEL-9614399; Regulation of localization of FOXO transcription factors.
DR PRO; PR:Q20655; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001502; Expressed in pharyngeal muscle cell (C elegans) and 21 other tissues.
DR ExpressionAtlas; Q20655; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IMP:WormBase.
DR GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IC:ComplexPortal.
DR GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IC:ComplexPortal.
DR GO; GO:0010629; P:negative regulation of gene expression; IC:ComplexPortal.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IC:ComplexPortal.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..248
FT /note="14-3-3-like protein 2"
FT /id="PRO_0000058648"
FT SITE 240..241
FT /note="Cleavage; by ced-3"
FT /evidence="ECO:0000269|PubMed:17371877"
FT MUTAGEN 240
FT /note="D->E: Loss of ced-3-mediated cleavage."
FT /evidence="ECO:0000269|PubMed:17371877"
SQ SEQUENCE 248 AA; 28067 MW; 566D9CF5DB7A4B96 CRC64;
MSDGKEELVN RAKLAEQAER YDDMAASMKK VTELGAELSN EERNLLSVAY KNVVGARRSS
WRVISSIEQK TEGSEKKQQM AKEYREKVEK ELRDICQDVL NLLDKFLIPK AGAAESKVFY
LKMKGDYYRY LAEVASGDDR NSVVEKSQQS YQEAFDIAKD KMQPTHPIRL GLALNFSVFF
YEILNAPDKA CQLAKQAFDD AIAELDTLNE DSYKDSTLIM QLLRDNLTLW TSDAATDDTD
ANETEGGN
