DCP1_CAEEL
ID DCP1_CAEEL Reviewed; 332 AA.
AC Q9N363;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=mRNA-decapping enzyme 1 {ECO:0000312|WormBase:Y55F3AM.12};
GN Name=dcap-1 {ECO:0000312|WormBase:Y55F3AM.12};
GN ORFNames=Y55F3AM.12 {ECO:0000312|WormBase:Y55F3AM.12};
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]
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]
RP FUNCTION.
RX PubMed=16199859; DOI=10.1128/mcb.25.20.8779-8791.2005;
RA Cohen L.S., Mikhli C., Jiao X., Kiledjian M., Kunkel G., Davis R.E.;
RT "Dcp2 Decaps m2,2,7GpppN-capped RNAs, and its activity is sequence and
RT context dependent.";
RL Mol. Cell. Biol. 25:8779-8791(2005).
RN [3]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16267265; DOI=10.1091/mbc.e05-09-0874;
RA Squirrell J.M., Eggers Z.T., Luedke N., Saari B., Grimson A., Lyons G.E.,
RA Anderson P., White J.G.;
RT "CAR-1, a protein that localizes with the mRNA decapping component DCAP-1,
RT is required for cytokinesis and ER organization in Caenorhabditis elegans
RT embryos.";
RL Mol. Biol. Cell 17:336-344(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25061667; DOI=10.1371/journal.pone.0103365;
RA Rousakis A., Vlanti A., Borbolis F., Roumelioti F., Kapetanou M.,
RA Syntichaki P.;
RT "Diverse functions of mRNA metabolism factors in stress defense and aging
RT of Caenorhabditis elegans.";
RL PLoS ONE 9:e103365-e103365(2014).
RN [5]
RP FUNCTION.
RX PubMed=28887031; DOI=10.1016/j.bbrc.2017.09.014;
RA Adachi T., Nagahama K., Izumi S.;
RT "The C. elegans mRNA decapping enzyme shapes morphology of cilia.";
RL Biochem. Biophys. Res. Commun. 493:382-387(2017).
RN [6]
RP FUNCTION.
RX PubMed=28250105; DOI=10.1098/rsob.160313;
RA Borbolis F., Flessa C.M., Roumelioti F., Diallinas G., Stravopodis D.J.,
RA Syntichaki P.;
RT "Neuronal function of the mRNA decapping complex determines survival of
RT Caenorhabditis elegans at high temperature through temporal regulation of
RT heterochronic gene expression.";
RL Open Biol. 7:0-0(2017).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31983639; DOI=10.1016/j.cub.2019.12.061;
RA Tang N.H., Kim K.W., Xu S., Blazie S.M., Yee B.A., Yeo G.W., Jin Y.,
RA Chisholm A.D.;
RT "The mRNA Decay Factor CAR-1/LSM14 Regulates Axon Regeneration via
RT Mitochondrial Calcium Dynamics.";
RL Curr. Biol. 30:865-876(2020).
RN [8]
RP FUNCTION.
RX PubMed=32366357; DOI=10.7554/elife.53757;
RA Borbolis F., Rallis J., Kanatouris G., Kokla N., Karamalegkos A.,
RA Vasileiou C., Vakaloglou K.M., Diallinas G., Stravopodis D.J., Zervas C.G.,
RA Syntichaki P.;
RT "mRNA decapping is an evolutionarily conserved modulator of neuroendocrine
RT signaling that controls development and ageing.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Component of the decapping complex necessary for the
CC degradation of mRNAs, both in normal mRNA turnover and in nonsense-
CC mediated mRNA decay (By similarity). In contrast to orthologs, does not
CC possess decapping activity and does not remove the 7-methyl guanine cap
CC structure from mRNA molecules (PubMed:16199859). In the nervous system,
CC negatively regulates the expression of insulin-like peptide ins-7,
CC which in turn promotes longevity (PubMed:32366357). This may in part be
CC through promoting the activity of daf-16 in distal tissues
CC (PubMed:32366357). Required for the developmental axon guidance and
CC regrowth of PLM touch receptor neurons (PubMed:31983639). In ADL
CC sensory neurons, plays a role in ciliary shape formation
CC (PubMed:28887031). Acts in neurons to promote larval survival at high
CC temperatures by negatively regulating lin-14 expression
CC (PubMed:28250105) (Probable). {ECO:0000250|UniProtKB:Q12517,
CC ECO:0000269|PubMed:16199859, ECO:0000269|PubMed:28250105,
CC ECO:0000269|PubMed:28887031, ECO:0000269|PubMed:31983639,
CC ECO:0000269|PubMed:32366357, ECO:0000305|PubMed:25061667}.
CC -!- SUBUNIT: May be a component of the decapping complex composed of dcap-1
CC and dcap-2. {ECO:0000250|UniProtKB:Q12517}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16267265}.
CC Cytoplasmic granule {ECO:0000269|PubMed:16267265,
CC ECO:0000269|PubMed:31983639}. Note=Diffusely localized in the
CC cytoplasm, but accumulates in puncta during pronuclear migration in
CC embryos (PubMed:16267265). After pronuclear migration, accumulates in
CC P-granules which segregated to the posterior cell, and smaller puncta
CC scattered in the cytoplasm (PubMed:16267265). Localizes to cytoplasmic
CC puncta in neuronal cell bodies of neurons such as touch receptor
CC neurons (PubMed:31983639). In some cytoplasmic puncta in touch receptor
CC neurons, co-localizes with car-1 (PubMed:31983639).
CC {ECO:0000269|PubMed:16267265, ECO:0000269|PubMed:31983639}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons including touch receptor
CC neurons and motor neurons. {ECO:0000269|PubMed:31983639}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (at protein level).
CC {ECO:0000269|PubMed:16267265}.
CC -!- DISRUPTION PHENOTYPE: Double RNAi-mediated knockdown with dcap-2
CC reduces survival at 20 degrees Celsius. {ECO:0000269|PubMed:25061667}.
CC -!- SIMILARITY: Belongs to the DCP1 family. {ECO:0000305}.
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DR EMBL; BX284604; CCD74070.1; -; Genomic_DNA.
DR RefSeq; NP_500030.1; NM_067629.3.
DR AlphaFoldDB; Q9N363; -.
DR SMR; Q9N363; -.
DR IntAct; Q9N363; 1.
DR STRING; 6239.Y55F3AM.12; -.
DR EPD; Q9N363; -.
DR PaxDb; Q9N363; -.
DR PeptideAtlas; Q9N363; -.
DR EnsemblMetazoa; Y55F3AM.12.1; Y55F3AM.12.1; WBGene00021929.
DR GeneID; 176924; -.
DR KEGG; cel:CELE_Y55F3AM.12; -.
DR UCSC; Y55F3AM.12.1; c. elegans.
DR CTD; 176924; -.
DR WormBase; Y55F3AM.12; CE22543; WBGene00021929; dcap-1.
DR eggNOG; KOG2868; Eukaryota.
DR GeneTree; ENSGT00940000172151; -.
DR HOGENOM; CLU_829590_0_0_1; -.
DR InParanoid; Q9N363; -.
DR OMA; QIHQAYV; -.
DR OrthoDB; 1509316at2759; -.
DR PhylomeDB; Q9N363; -.
DR Reactome; R-CEL-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-CEL-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR PRO; PR:Q9N363; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00021929; Expressed in embryo and 4 other tissues.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0000932; C:P-body; IDA:WormBase.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IEA:InterPro.
DR GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0009408; P:response to heat; IMP:WormBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:WormBase.
DR GO; GO:0009411; P:response to UV; IMP:WormBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010334; Dcp1.
DR InterPro; IPR031953; mRNA_decap_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16290; PTHR16290; 1.
DR Pfam; PF06058; DCP1; 1.
DR Pfam; PF16741; mRNA_decap_C; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; Nonsense-mediated mRNA decay;
KW Reference proteome; RNA-binding.
FT CHAIN 1..332
FT /note="mRNA-decapping enzyme 1"
FT /id="PRO_0000451759"
FT REGION 141..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 36549 MW; 4AE594C627B1A6EE CRC64;
MSDAKKKAAA ELAAKNLAQL QKIDIAASKI LDKMPFAAIY HIDAARKEWN QSNCEGTFFV
YQRADRPYFS FLIANRNDPS DFIEPLTLNH ILRHDGNFIY FYKDLASIQA LWFHQIDDAQ
KIYNLLQKLV NRLKGSTTEQ ARAAKAASEA PQASVPAPTQ APAAPAQAPQ MAPQAPPKVD
LLQLIKSAQN PPQKSAATIE QMPPMLQKLM LKEPGAAMSA DELEKDLIKS AKPHRNHLLQ
EFTNSTSAIS LAAVSTKPLH GSEGDVESDI AEGEILEPLD ASFVVGSGEQ TPVLNKEQFI
SAIAHLMQTD DEFVSQIHQA YVSALNRRLN ID
