TADBP_CAEEL
ID TADBP_CAEEL Reviewed; 414 AA.
AC D0VWM8; Q20414; Q6BEV0;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Tar DNA-binding protein homolog 1 {ECO:0000312|WormBase:F44G4.4c};
GN Name=tdp-1 {ECO:0000312|WormBase:F44G4.4c};
GN ORFNames=F44G4.4 {ECO:0000312|WormBase:F44G4.4c};
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] {ECO:0000312|Proteomes:UP000001940}
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] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22232551; DOI=10.1074/jbc.m111.311977;
RA Zhang T., Hwang H.Y., Hao H., Talbot C. Jr., Wang J.;
RT "Caenorhabditis elegans RNA-processing protein TDP-1 regulates protein
RT homeostasis and life span.";
RL J. Biol. Chem. 287:8371-8382(2012).
RN [3] {ECO:0000305}
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22792076; DOI=10.1371/journal.pgen.1002806;
RA Vaccaro A., Tauffenberger A., Ash P.E., Carlomagno Y., Petrucelli L.,
RA Parker J.A.;
RT "TDP-1/TDP-43 regulates stress signaling and age-dependent proteotoxicity
RT in Caenorhabditis elegans.";
RL PLoS Genet. 8:E1002806-E1002806(2012).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25391662; DOI=10.15252/embj.201488740;
RA Saldi T.K., Ash P.E., Wilson G., Gonzales P., Garrido-Lecca A.,
RA Roberts C.M., Dostal V., Gendron T.F., Stein L.D., Blumenthal T.,
RA Petrucelli L., Link C.D.;
RT "TDP-1, the Caenorhabditis elegans ortholog of TDP-43, limits the
RT accumulation of double-stranded RNA.";
RL EMBO J. 33:2947-2966(2014).
RN [5]
RP FUNCTION, AND INTERACTION WITH HPL-2.
RX PubMed=29760282; DOI=10.1128/mcb.00668-17;
RA Saldi T.K., Gonzales P., Garrido-Lecca A., Dostal V., Roberts C.M.,
RA Petrucelli L., Link C.D.;
RT "The Caenorhabditis elegans Ortholog of TDP-43 Regulates the Chromatin
RT Localization of the Heterochromatin Protein 1 Homolog HPL-2.";
RL Mol. Cell. Biol. 38:0-0(2018).
CC -!- FUNCTION: RNA-binding protein which regulates transcription, splicing
CC and RNA-editing (PubMed:25391662). Limits the accumulation of double-
CC stranded RNA by maintaining the abundance of the mature RNA transcripts
CC that are formed from double-stranded precursor RNAs (PubMed:25391662).
CC Stress response protein that acts downstream of daf-16 in the
CC insulin/IGF pathway to regulate longevity and the cellular stress
CC response to osmotic, oxidative, proteotoxic and endoplasmic reticulum
CC stress (PubMed:22232551, PubMed:22792076). Involved in the regulation
CC of physiological processes including aging, fertility, growth and
CC locomotion (PubMed:22232551, PubMed:29760282). Plays a role in
CC maintaining localization of chromobox protein homolog hpl-2 to gene
CC bodies, perhaps acting via binding to nascent RNA transcripts
CC (PubMed:29760282). {ECO:0000269|PubMed:22232551,
CC ECO:0000269|PubMed:22792076, ECO:0000269|PubMed:25391662,
CC ECO:0000269|PubMed:29760282}.
CC -!- SUBUNIT: Interacts with chromobox protein homolog hpl-2; interaction
CC may maintain localization of hpl-2 to gene bodies.
CC {ECO:0000269|PubMed:29760282}.
CC -!- INTERACTION:
CC D0VWM8; Q9XVS2: sup-46; NbExp=2; IntAct=EBI-311955, EBI-311961;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22792076}. Cytoplasm
CC {ECO:0000269|PubMed:22792076}. Note=Shuttles from the nucleus to the
CC cytoplasm under stress conditions. {ECO:0000269|PubMed:22792076}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c {ECO:0000312|WormBase:F44G4.4c};
CC IsoId=D0VWM8-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F44G4.4a};
CC IsoId=D0VWM8-2; Sequence=VSP_057752;
CC Name=b {ECO:0000312|WormBase:F44G4.4b};
CC IsoId=D0VWM8-3; Sequence=VSP_057750, VSP_057751;
CC -!- TISSUE SPECIFICITY: Widely expressed in a range of tissues including
CC body wall muscles, pharynx and neurons of the midbody in adults and
CC larvae (PubMed:22232551, PubMed:22792076).
CC {ECO:0000269|PubMed:22232551, ECO:0000269|PubMed:22792076}.
CC -!- INDUCTION: By hyperosmotic, oxidative and endoplasmic reticulum stress
CC (at protein level). {ECO:0000269|PubMed:22792076}.
CC -!- DISRUPTION PHENOTYPE: Increased lifespan, slower growth rate, reduced
CC egg-laying and reduced fertility (PubMed:22232551, PubMed:22792076).
CC Defective locomotion and chemotaxis (PubMed:22232551, PubMed:25391662).
CC Increased sensitivity to osmotic and oxidative stress
CC (PubMed:22792076). Increased intronic A-to-I RNA editing and splicing
CC abnormalities, which may contribute to the increased accumulation of
CC double-stranded RNA observed in the nucleus of multiple tissues
CC including gut, muscle and the anterior head region (PubMed:25391662).
CC {ECO:0000269|PubMed:22232551, ECO:0000269|PubMed:22792076,
CC ECO:0000269|PubMed:25391662}.
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DR EMBL; BX284602; CAA90120.1; -; Genomic_DNA.
DR EMBL; BX284602; CAH04715.1; -; Genomic_DNA.
DR EMBL; BX284602; CBH29662.1; -; Genomic_DNA.
DR PIR; T22207; T22207.
DR RefSeq; NP_001022166.1; NM_001026995.5. [D0VWM8-2]
DR RefSeq; NP_001022167.1; NM_001026996.3.
DR RefSeq; NP_001254189.1; NM_001267260.1. [D0VWM8-1]
DR AlphaFoldDB; D0VWM8; -.
DR SMR; D0VWM8; -.
DR DIP; DIP-26310N; -.
DR IntAct; D0VWM8; 1.
DR STRING; 6239.F44G4.4c; -.
DR EPD; D0VWM8; -.
DR PaxDb; D0VWM8; -.
DR PeptideAtlas; D0VWM8; -.
DR EnsemblMetazoa; F44G4.4a.1; F44G4.4a.1; WBGene00006514. [D0VWM8-2]
DR EnsemblMetazoa; F44G4.4c.1; F44G4.4c.1; WBGene00006514. [D0VWM8-1]
DR GeneID; 174436; -.
DR KEGG; cel:CELE_F44G4.4; -.
DR UCSC; F44G4.4a; c. elegans.
DR CTD; 174436; -.
DR WormBase; F44G4.4a; CE02231; WBGene00006514; tdp-1. [D0VWM8-2]
DR WormBase; F44G4.4b; CE36440; WBGene00006514; tdp-1. [D0VWM8-3]
DR WormBase; F44G4.4c; CE44236; WBGene00006514; tdp-1. [D0VWM8-1]
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000154343; -.
DR HOGENOM; CLU_664372_0_0_1; -.
DR InParanoid; D0VWM8; -.
DR OMA; FCEIKRK; -.
DR OrthoDB; 1425837at2759; -.
DR PhylomeDB; D0VWM8; -.
DR PRO; PR:D0VWM8; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006514; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0006972; P:hyperosmotic response; IMP:WormBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IMP:WormBase.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR041105; TDP43_N.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF18694; TDP43_N; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..414
FT /note="Tar DNA-binding protein homolog 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433365"
FT DOMAIN 173..259
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 262..341
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 124
FT /note="Q -> L (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057750"
FT VAR_SEQ 125..414
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057751"
FT VAR_SEQ 251..253
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057752"
SQ SEQUENCE 414 AA; 45803 MW; B42F416DF6FA013D CRC64;
MADETPKVKT EPAAEVKSPL DEVKEIRKEA ELTQTGSDEK KTTDPEFITV QDPNGDEPIE
LPTVDGVVLM TTLQASFPGA TGLKYKNPKT GANRAVQVDP SGLKLIAPAD GWENKTFFVI
VAPQSERVRA LSSADATSAK RRKVGSSDDS DSDDGRDGRS GRKRAVERDS QPVDLIVLGV
DFKTTDECFQ KYFEDIGTVV FCEIKRKSDG NSKGFGFVRM SSVGEQNKVL AIPQHMIDGR
RCDVKVPDGR SLQDKQGRPS ISRIFVGRLT DKVDEHQLRK VFGDEAKSYI ETAVVTDVFI
PKPFRGFAFV TLSSAEAAER IVSKGSLTVN GLSVGLSIAQ PREENNQSVG PDYGLPAGYR
NRRERDRPDR RPIQNEAPLP MPFVRPPQDY SYRQQNSPLE RRYWAPGDSR GPGW
