PQE1_CAEEL
ID PQE1_CAEEL Reviewed; 1647 AA.
AC Q10124; G8JYC4; Q8MQ26; Q8MQ27; Q8MQ28; Q8MQ29; Q8MQ30; Q8MQ31;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Putative RNA exonuclease pqe-1;
DE AltName: Full=PolyQ enhancer protein 1;
GN Name=pqe-1 {ECO:0000312|WormBase:F52C9.8b};
GN ORFNames=F52C9.8 {ECO:0000312|WormBase:F52C9.8b};
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 [GENOMIC DNA] (ISOFORMS A; B AND C), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12486229; DOI=10.1073/pnas.262544899;
RA Faber P.W., Voisine C., King D.C., Bates E.A., Hart A.C.;
RT "Glutamine/proline-rich PQE-1 proteins protect Caenorhabditis elegans
RT neurons from huntingtin polyglutamine neurotoxicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17131-17136(2002).
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, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22870397; DOI=10.1534/g3.112.002832;
RA Yamada K., Tsuchiya J., Iino Y.;
RT "Mutations in the pqe-1 gene enhance transgene expression in Caenorhabditis
RT elegans.";
RL G3 (Bethesda) 2:741-751(2012).
CC -!- FUNCTION: Putative RNA exonuclease which protects neurons from the
CC toxic effects of expanded poly-Q disease proteins (PubMed:12486229). It
CC is unknown whether this is via participation in the pathogenic
CC mechanism underlying poly-Q-induced neurodegeneration or if it is by
CC acting as a genetic modifier of the age of onset or progression of
CC neurodegeneration (PubMed:12486229). Regulates gene expression in
CC neurons (PubMed:22870397). {ECO:0000269|PubMed:12486229,
CC ECO:0000269|PubMed:22870397}.
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Nucleus
CC {ECO:0000269|PubMed:12486229, ECO:0000269|PubMed:22870397}. Note=Forms
CC aggregates in the nucleus. {ECO:0000269|PubMed:22870397}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=b {ECO:0000312|WormBase:F52C9.8b}; Synonyms=Pqe-1A
CC {ECO:0000303|PubMed:12486229};
CC IsoId=Q10124-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F52C9.8a}; Synonyms=Pqe-1C
CC {ECO:0000303|PubMed:12486229};
CC IsoId=Q10124-2; Sequence=VSP_060516, VSP_060517;
CC Name=c {ECO:0000312|WormBase:F52C9.8c}; Synonyms=Pqe-1B
CC {ECO:0000303|PubMed:12486229};
CC IsoId=Q10124-3; Sequence=VSP_060515;
CC Name=f {ECO:0000312|WormBase:F52C9.8f};
CC IsoId=Q10124-6; Sequence=VSP_060514, VSP_060519;
CC Name=g {ECO:0000312|WormBase:F52C9.8g};
CC IsoId=Q10124-7; Sequence=VSP_060515, VSP_060518;
CC -!- TISSUE SPECIFICITY: Expressed in the excretory canal, vulval cells, the
CC intestine and in head and tail neurons including ASH, RIC and AIZ
CC neurons. {ECO:0000269|PubMed:22870397}.
CC -!- DOMAIN: The Gln/Pro-rich N-terminus and the Arg/Asp/Glu/Lys-rich
CC charged domain are critical in protecting glutamatergic ASH sensory
CC neurons from degeneration. ASH neurons expressing isoforms lacking
CC these domains show progressive degeneration.
CC -!- SIMILARITY: Belongs to the REXO1/REXO3 family. {ECO:0000305}.
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DR EMBL; BX284603; CCD71610.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD71611.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD71612.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD71615.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD71616.1; -; Genomic_DNA.
DR PIR; T16421; T16421.
DR RefSeq; NP_001040854.1; NM_001047389.1. [Q10124-7]
DR RefSeq; NP_498135.2; NM_065734.5. [Q10124-1]
DR RefSeq; NP_498136.2; NM_065735.5. [Q10124-3]
DR RefSeq; NP_498137.2; NM_065736.5.
DR RefSeq; NP_741135.1; NM_171120.3. [Q10124-6]
DR AlphaFoldDB; Q10124; -.
DR SMR; Q10124; -.
DR BioGRID; 40962; 1.
DR DIP; DIP-26275N; -.
DR STRING; 6239.F52C9.8b; -.
DR iPTMnet; Q10124; -.
DR EPD; Q10124; -.
DR PaxDb; Q10124; -.
DR PeptideAtlas; Q10124; -.
DR PRIDE; Q10124; -.
DR EnsemblMetazoa; F52C9.8a.1; F52C9.8a.1; WBGene00004095. [Q10124-2]
DR EnsemblMetazoa; F52C9.8a.2; F52C9.8a.2; WBGene00004095. [Q10124-2]
DR EnsemblMetazoa; F52C9.8a.3; F52C9.8a.3; WBGene00004095. [Q10124-2]
DR EnsemblMetazoa; F52C9.8a.4; F52C9.8a.4; WBGene00004095. [Q10124-2]
DR EnsemblMetazoa; F52C9.8b.1; F52C9.8b.1; WBGene00004095. [Q10124-1]
DR EnsemblMetazoa; F52C9.8c.1; F52C9.8c.1; WBGene00004095. [Q10124-3]
DR EnsemblMetazoa; F52C9.8f.1; F52C9.8f.1; WBGene00004095. [Q10124-6]
DR EnsemblMetazoa; F52C9.8g.1; F52C9.8g.1; WBGene00004095. [Q10124-7]
DR GeneID; 175731; -.
DR KEGG; cel:CELE_F52C9.8; -.
DR UCSC; F52C9.8d.2; c. elegans. [Q10124-1]
DR CTD; 175731; -.
DR WormBase; F52C9.8a; CE30802; WBGene00004095; pqe-1. [Q10124-2]
DR WormBase; F52C9.8b; CE30998; WBGene00004095; pqe-1. [Q10124-1]
DR WormBase; F52C9.8c; CE30672; WBGene00004095; pqe-1. [Q10124-3]
DR WormBase; F52C9.8f; CE30675; WBGene00004095; pqe-1. [Q10124-6]
DR WormBase; F52C9.8g; CE39256; WBGene00004095; pqe-1. [Q10124-7]
DR eggNOG; KOG2248; Eukaryota.
DR GeneTree; ENSGT00940000169529; -.
DR HOGENOM; CLU_002891_0_0_1; -.
DR InParanoid; Q10124; -.
DR OMA; DDEMENT; -.
DR OrthoDB; 774159at2759; -.
DR PRO; PR:Q10124; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004095; Expressed in embryo and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0004527; F:exonuclease activity; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR CDD; cd06145; REX1_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR034922; REX1-like_exo.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Exonuclease; Hydrolase; Nuclease;
KW Nucleus; Reference proteome.
FT CHAIN 1..1647
FT /note="Putative RNA exonuclease pqe-1"
FT /id="PRO_0000120940"
FT DOMAIN 1477..1637
FT /note="Exonuclease"
FT /evidence="ECO:0000255"
FT REGION 1..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 686..726
FT /evidence="ECO:0000255"
FT COILED 1142..1187
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..904
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..1207
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_060514"
FT VAR_SEQ 96..1072
FT /note="Missing (in isoform c and isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_060515"
FT VAR_SEQ 1073..1081
FT /note="KKDAKSSEN -> VRRCGGDNV (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060516"
FT VAR_SEQ 1082..1647
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060517"
FT VAR_SEQ 1091
FT /note="N -> NFQ (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_060518"
FT VAR_SEQ 1208..1299
FT /note="AKKQKPAPAVPKILDFSVGRTFTAIRQTAIKLVFDTFLERDSPNAAREAQEF
FT ELSIAKQYTDGQKYRINIGHKVAALRKENTSGILEVNKNA -> MSTYYQSAPVLVHAH
FT AYQPPLSPPQSPPHGYLPFYTSNPMMCSTSPLYFSPQMVQPLPPQQHYHMYPSTSAGPG
FT MYYTDFNPHYVQIQISQS (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_060519"
SQ SEQUENCE 1647 AA; 182262 MW; A3A66BA183B3D650 CRC64;
MFNGGYGSGN SFNLQNYAPI DPMTGIPGFG PSQNAQQQQQ QASAPGTSSG GPSQAVSGAS
SGASMKTEPV ARQVSTAQMK RDLEQAAVYV PTPIPEGSTQ PQQRQQQQSQ PQARQMSTQQ
AANLRKNAAA AGTPPKQAMQ GASREQGNAH QPTAGQIPQS SNQPAQQTHN VPRMPQPLQQ
VPHPSPVRGS HPAAQQVQNA PQRIPQHVPM PQGVAPHQVI QQVRAPNIGA SQMVQQAPSR
GHTGAAPASR MAQQPVPLHQ GVAPHQAAPQ TIQQTPARGR PANAQLAQNA QQRNPQQVPM
PQGVAPHHIP PQALGPHGAA PQMTQQAPAR GPSGAAQHAQ NAHRMTHQQV PLQAPVQGPH
RGAPQMAQQP GPHGAAQHPS SGTVAPMHIT SLPGNHPLNR THLLFNRQVV PALDIRNLIA
QHRLMVDDFV RAQICYRLPE NHQDYWPPGG HPIPMQQQQM RQGAGLPNMA MPPPPLMRHP
GPHQNPIHAM QSMQVQPPLS PDQMNMQMFQ QRALMMQQQA MQMQMQNPPP VHQQPPPQQP
PQQQRQKQQR SQPAPARVPP QVPSQVPVTG GVAADEPPPP CSYSPVAQSS ESKIEPVDVK
PRVAPVPPQV PVTPTKPVIT NNKKKRIDVV TLDEDAPRRV QVKQEIPEVS STSDATKSDA
APTARGAVRI KQEVESDVAP NTILISAKKF ERMKAEAEDK EDMKKKIAAL QEALFNIQEE
RRVEKEIAAF ATTNQAVPQN QPASSVQIAQ VSTSESDAPG TSEAAATETM TSPKTKNNVI
VETEGEQEED EDEIPIKKSK KRRAKIVSND EEEEPVRHPK RRSDEKREKR HVSYAESDDD
MPVVKKKRRN QSPEDPEYSA ASPSEDEDDD IGSFVVSDNE DDDADSFVVG DDEPIEYEEE
DEDDMIERRS SRKRRSDSRS KKSATPTDRR RSRDTPTGSR SMRSTSPNDR RKSRETPPGN
RSMRRTSPSD GRKSRDTPTA SSSMSSSTLS YCKKSKETPM SYEEIEQQKK AKRQRNCKTR
EENRERKRLA QLEELESSET TGVRRTLRST QDNSDPLDAS LATTIEEFRK TKKKDAKSSE
NRAKEKQKPM NKRPTSSASV DSNDDGVHIP AKRMAHASSV PGPSRSKPPM IGAVKNRPNH
TEMLDKRNKE SEEKRRKDRD ELERLRNKKH TTEEEKIKMA RLQNALKVVG KAAGLKATVK
KELTGSPAKK QKPAPAVPKI LDFSVGRTFT AIRQTAIKLV FDTFLERDSP NAAREAQEFE
LSIAKQYTDG QKYRINIGHK VAALRKENTS GILEVNKNAV SHDKILAGGP KDNCTVARGR
KTHVDHRQLS IEKLHPLLLQ FKLTTSELET NAYPMRRDGS TKAVSIADTV YTQNKKMFLD
DYDMSRNCSR CNKEFKLSPN GTMIRSTGIC RYHNRGVAIN GKRDTFRKRY SCCNEEFNVA
LGCKFSDVHV TDQLFKKELS TFVSTPVPVP NDQRSTRVYA LDCEMVYTIA GPALARLTMV
DMQRNRVLDV FVKPPTDVLD PNTEFSGLTM EQINSAPDTL KTCHQKLFKY VNADTILIGH
SLESDLKAMR VVHKNVIDTA ILFRSTRDTK VALKVLSAKL LHKNIQGDNE DAIGHDSMED
ALTCVDLIFY GLRNPESIAI REANTNC
