PATR1_CAEEL
ID PATR1_CAEEL Reviewed; 833 AA.
AC Q20374;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein PAT1 homolog 1;
GN Name=patr-1 {ECO:0000312|WormBase:F43G6.9};
GN ORFNames=F43G6.9 {ECO:0000312|WormBase:F43G6.9};
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, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18692039; DOI=10.1016/j.ydbio.2008.07.008;
RA Gallo C.M., Munro E., Rasoloson D., Merritt C., Seydoux G.;
RT "Processing bodies and germ granules are distinct RNA granules that
RT interact in C. elegans embryos.";
RL Dev. Biol. 323:76-87(2008).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=18695045; DOI=10.1083/jcb.200801183;
RA Boag P.R., Atalay A., Robida S., Reinke V., Blackwell T.K.;
RT "Protection of specific maternal messenger RNAs by the P body protein CGH-1
RT (Dhh1/RCK) during Caenorhabditis elegans oogenesis.";
RL J. Cell Biol. 182:543-557(2008).
RN [4]
RP FUNCTION.
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).
CC -!- FUNCTION: RNA-binding protein involved in deadenylation-dependent
CC decapping of mRNAs, leading to the degradation of mRNAs. Acts as a
CC scaffold protein that connects deadenylation and decapping machinery
CC (By similarity). Required for the recruitment of P-body components such
CC as cgh-1 in somatic blastomeres (PubMed:18692039). May play a role in
CC recruiting the decapping enzyme dcap-1 to cytoplasmic puncta in the
CC cell body of the posterior touch receptor neuron, PLM
CC (PubMed:31983639). {ECO:0000250, ECO:0000269|PubMed:18692039,
CC ECO:0000269|PubMed:31983639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:18692039,
CC ECO:0000269|PubMed:18695045}.
CC -!- DEVELOPMENTAL STAGE: Localizes to germline and somatic blastomeres (at
CC protein level). {ECO:0000269|PubMed:18692039}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces the number of
CC cgh-1-positive foci in somatic blastomeres.
CC {ECO:0000269|PubMed:18692039}.
CC -!- SIMILARITY: Belongs to the PAT1 family. {ECO:0000305}.
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DR EMBL; BX284602; CAA90402.1; -; Genomic_DNA.
DR EMBL; Z83108; CAA90402.1; JOINED; Genomic_DNA.
DR PIR; T22139; T22139.
DR RefSeq; NP_496514.1; NM_064113.5.
DR AlphaFoldDB; Q20374; -.
DR BioGRID; 40112; 8.
DR STRING; 6239.F43G6.9; -.
DR EPD; Q20374; -.
DR PaxDb; Q20374; -.
DR PeptideAtlas; Q20374; -.
DR PRIDE; Q20374; -.
DR EnsemblMetazoa; F43G6.9.1; F43G6.9.1; WBGene00009661.
DR GeneID; 174808; -.
DR KEGG; cel:CELE_F43G6.9; -.
DR UCSC; F43G6.9.1; c. elegans.
DR CTD; 42058; -.
DR WormBase; F43G6.9; CE18675; WBGene00009661; patr-1.
DR eggNOG; KOG4592; Eukaryota.
DR GeneTree; ENSGT00520000055649; -.
DR HOGENOM; CLU_363404_0_0_1; -.
DR InParanoid; Q20374; -.
DR OMA; STHNPRH; -.
DR OrthoDB; 415246at2759; -.
DR Reactome; R-CEL-430039; mRNA decay by 5' to 3' exoribonuclease.
DR PRO; PR:Q20374; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00009661; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000932; C:P-body; IDA:WormBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
DR InterPro; IPR039900; Pat1-like.
DR PANTHER; PTHR21551; PTHR21551; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; RNA-binding.
FT CHAIN 1..833
FT /note="Protein PAT1 homolog 1"
FT /id="PRO_0000404582"
FT REGION 279..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 93672 MW; 5047A926A94E2EE5 CRC64;
MEEVKKYGKT LEEIEGGLMF DDFPESLVDS DEDHNIFDDE FDAANDETFG GGLDNIGENA
ELENYATQTA KLRFDDPVWQ KPSSSDHVAP SASEIPIPFP NFGNGDASDS FKSSFEAESP
FLKKSIWGNG TDGAYNIWGT NFGISSVPAA PTLDLDFGAL LPTPTIQATK EVKSSQIPSM
PSSALTLEDC ERMQMGNKPD SLVDAFKDLQ LGSTPVQPQS AQFSKHPLEA RIAAPGTPAT
ASSQALPTLP TAALSLEELE LQIMKEAQIL KGRQQVPSDM REDNKFSHPP PGFNQNVQPR
MDPSLSPGGM HGMPPSMGTS MPHMGPMMPP QNMQLPRLPP LNPQFLPLIP VWFNAIINNI
QLPMGVPPPP PFLFQLLNHY RNPQLVHAMI MQSSIPPNIR QNGPQFSHPS GPHSPGNRVQ
RKHSGMPSTR TIYDLALDSF AGYMSYKERE WLIRIQFIQC KGSGDPQVDD YYYVTWRDKQ
IANGWTAETK LEEATKEKKE KSSESQKDYL ERISRMNYRE MQKERARERD KERQRERQER
IDRGEDKKLR QTLSDKFATS LGLPSKSSTH NPRHVLDMKA QVESVDNQTK KLSDEERKIA
VAKKLRTMLL RLEGALNILM EVDELRRSSL PEKSQFKDLS SDEKDQEVEK RTTVIINELM
GDDLSKLMQM SKGRAVITRT LKVVEPRDQA RIILALMTAG GLVSKKMYGE IVLDILPVVY
QKVSNLHPDQ FKYLVGALNL DTLKRQLLDS NMFIRDMMMT LFFVSVKNNQ QLVEWAKATK
FSSLKMPSSA PLSIWRKALS VISDSEIKEF ADDIKYSGIV DCHDVAQLIE QSL
