14331_CAEEL
ID 14331_CAEEL Reviewed; 248 AA.
AC P41932; Q21537;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=14-3-3-like protein 1;
DE AltName: Full=Partitioning defective protein 5;
GN Name=par-5; Synonyms=ftt-1; ORFNames=M117.2;
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].
RC STRAIN=Bristol N2;
RX PubMed=7926802; DOI=10.1016/0378-1119(94)90068-x;
RA Wang W., Shakes D.C.;
RT "Isolation and sequence analysis of a Caenorhabditis elegans cDNA which
RT encodes a 14-3-3 homologue.";
RL Gene 147:215-218(1994).
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 IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DAF-16 AND SIR-2.1,
RP 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 [4]
RP FUNCTION, AND INTERACTION WITH 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 [5]
RP INTERACTION WITH ATGL-1.
RX PubMed=26098762; DOI=10.1371/journal.pone.0130480;
RA Xie M., Roy R.;
RT "AMP-activated kinase regulates lipid droplet localization and stability of
RT adipose triglyceride lipase in C. elegans dauer larvae.";
RL PLoS ONE 10:E0130480-E0130480(2015).
CC -!- FUNCTION: Required to modulate lifespan, in concert with hcf-1, acting
CC redundantly with 14-3-3-like protein ftt-2.
CC {ECO:0000269|PubMed:21909281}.
CC -!- SUBUNIT: Interacts with daf-16 and sir-2.1 (PubMed:16777605). Interacts
CC with atgl-1 (PubMed:26098762). Interacts with hcf-1 (PubMed:21909281).
CC {ECO:0000269|PubMed:16777605, ECO:0000269|PubMed:21909281,
CC ECO:0000269|PubMed:26098762}.
CC -!- INTERACTION:
CC P41932; G5EC23: hcf-1; NbExp=2; IntAct=EBI-318108, EBI-4480523;
CC P41932; Q11184: let-756; NbExp=3; IntAct=EBI-318108, EBI-3843983;
CC P41932; Q10666: pop-1; NbExp=2; IntAct=EBI-318108, EBI-317870;
CC P41932; Q21921: sir-2.1; NbExp=3; IntAct=EBI-318108, EBI-966082;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16777605}. Nucleus
CC {ECO:0000269|PubMed:16777605}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; U05038; AAA61872.1; -; mRNA.
DR EMBL; Z73910; CAA98138.1; -; Genomic_DNA.
DR PIR; JC2581; JC2581.
DR PIR; T23759; T23759.
DR RefSeq; NP_502235.1; NM_069834.5.
DR AlphaFoldDB; P41932; -.
DR SMR; P41932; -.
DR BioGRID; 43208; 38.
DR ComplexPortal; CPX-3884; daf-16-par-5 complex.
DR ComplexPortal; CPX-3886; sir-2.1-par-5 complex.
DR DIP; DIP-27044N; -.
DR IntAct; P41932; 12.
DR STRING; 6239.M117.2a.2; -.
DR iPTMnet; P41932; -.
DR EPD; P41932; -.
DR PaxDb; P41932; -.
DR PeptideAtlas; P41932; -.
DR EnsemblMetazoa; M117.2a.1; M117.2a.1; WBGene00003920.
DR EnsemblMetazoa; M117.2a.2; M117.2a.2; WBGene00003920.
DR EnsemblMetazoa; M117.2a.3; M117.2a.3; WBGene00003920.
DR EnsemblMetazoa; M117.2a.4; M117.2a.4; WBGene00003920.
DR UCSC; M117.2.2; c. elegans.
DR WormBase; M117.2a; CE06200; WBGene00003920; par-5.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P41932; -.
DR OMA; SMKAYQT; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P41932; -.
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 SignaLink; P41932; -.
DR PRO; PR:P41932; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003920; Expressed in reproductive system and 7 other tissues.
DR ExpressionAtlas; P41932; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:WormBase.
DR GO; GO:0001708; P:cell fate specification; IMP:WormBase.
DR GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IC:ComplexPortal.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:WormBase.
DR GO; GO:0030590; P:first cell cycle pseudocleavage; IMP:WormBase.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IC:ComplexPortal.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:WormBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IC:ComplexPortal.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:WormBase.
DR GO; GO:0035046; P:pronuclear migration; IMP:WormBase.
DR GO; GO:0006611; P:protein export from 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:0007346; P:regulation of mitotic cell cycle; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0010070; P:zygote asymmetric cell division; IMP:WormBase.
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 1"
FT /id="PRO_0000058647"
FT CONFLICT 118
FT /note="V -> A (in Ref. 1; AAA61872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 28191 MW; ABBE0DA27D9341AF CRC64;
MSDTVEELVQ RAKLAEQAER YDDMAAAMKK VTEQGQELSN EERNLLSVAY KNVVGARRSS
WRVISSIEQK TEGSEKKQQL AKEYRVKVEQ ELNDICQDVL KLLDEFLIVK AGAAESKVFY
LKMKGDYYRY LAEVASEDRA AVVEKSQKAY QEALDIAKDK MQPTHPIRLG LALNFSVFYY
EILNTPEHAC QLAKQAFDDA IAELDTLNED SYKDSTLIMQ LLRDNLTLWT SDVGAEDQEQ
EGNQEAGN
