RENT1_CAEEL
ID RENT1_CAEEL Reviewed; 1069 AA.
AC O76512; Q9BL16;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Regulator of nonsense transcripts 1;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q92900};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q92900};
DE AltName: Full=ATP-dependent helicase smg-2;
DE AltName: Full=Nonsense mRNA reducing factor 1;
DE AltName: Full=Up-frameshift suppressor 1 homolog;
GN Name=smg-2; ORFNames=Y48G8AL.6;
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], AND MUTAGENESIS OF GLY-470 AND GLY-472.
RX PubMed=10454541; DOI=10.1128/mcb.19.9.5943;
RA Page M.F., Carr B., Anders K.R., Grimson A., Anderson P.;
RT "SMG-2 is a phosphorylated protein required for mRNA surveillance in
RT Caenorhabditis elegans and related to Upf1p of yeast.";
RL Mol. Cell. Biol. 19:5943-5951(1999).
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).
CC -!- FUNCTION: RNA-dependent helicase required for nonsense-mediated decay
CC (NMD) of aberrant mRNAs containing premature stop codons and modulates
CC the expression level of normal mRNAs. Is recruited to mRNAs upon
CC translation termination and undergoes a cycle of phosphorylation and
CC dephosphorylation; its phosphorylation appears to be a key step in NMD.
CC The formation of an smg-2-3-4 surveillance complex is believed to
CC activate NMD (By similarity). {ECO:0000250|UniProtKB:Q92900}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q92900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q92900};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:Q92900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q92900};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated probably by smg-1. Smg-3 and smg-4 are required for
CC phosphorylation.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF074017; AAC26789.1; -; mRNA.
DR EMBL; FO081800; CCD73461.1; -; Genomic_DNA.
DR PIR; T43280; T43280.
DR RefSeq; NP_490829.1; NM_058428.4.
DR AlphaFoldDB; O76512; -.
DR SMR; O76512; -.
DR BioGRID; 37194; 22.
DR IntAct; O76512; 1.
DR MINT; O76512; -.
DR STRING; 6239.Y48G8AL.6; -.
DR iPTMnet; O76512; -.
DR EPD; O76512; -.
DR PaxDb; O76512; -.
DR PeptideAtlas; O76512; -.
DR EnsemblMetazoa; Y48G8AL.6.1; Y48G8AL.6.1; WBGene00004880.
DR GeneID; 171696; -.
DR KEGG; cel:CELE_Y48G8AL.6; -.
DR UCSC; Y48G8AL.6; c. elegans.
DR CTD; 171696; -.
DR WormBase; Y48G8AL.6; CE28367; WBGene00004880; smg-2.
DR eggNOG; KOG1802; Eukaryota.
DR GeneTree; ENSGT00940000157413; -.
DR HOGENOM; CLU_001666_4_1_1; -.
DR InParanoid; O76512; -.
DR OrthoDB; 62494at2759; -.
DR PhylomeDB; O76512; -.
DR Reactome; R-CEL-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-CEL-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:O76512; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004880; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IPI:WormBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISS:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0030538; P:embryonic genitalia morphogenesis; IMP:WormBase.
DR GO; GO:0034660; P:ncRNA metabolic process; IMP:WormBase.
DR GO; GO:0071030; P:nuclear mRNA surveillance of spliceosomal pre-mRNA splicing; IMP:CAFA.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:WormBase.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:WormBase.
DR CDD; cd21407; 1B_UPF1-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21400; ZBD_UPF1-like; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040812; UPF1_1B_dom.
DR InterPro; IPR018999; UPF1_CH/ZBD.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF18141; UPF1_1B_dom; 1.
DR Pfam; PF09416; UPF1_Zn_bind; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51997; UPF1_CH_RICH; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..1069
FT /note="Regulator of nonsense transcripts 1"
FT /id="PRO_0000080719"
FT DOMAIN 87..244
FT /note="Upf1 CH-rich"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..127
FT /note="C3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 109..137
FT /note="CC/SHH/C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 155..185
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 966..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 450
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 467..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT BINDING 639
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 807
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT MUTAGEN 470
FT /note="G->R: In R866; loss of activity and increased
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:10454541"
FT MUTAGEN 472
FT /note="G->E: In R895; loss of activity and increased
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:10454541"
FT CONFLICT 86..87
FT /note="HE -> QQ (in Ref. 2; CCD73461)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="S -> P (in Ref. 2; CCD73461)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1069 AA; 120020 MW; 5B4C91FB49B5C24B CRC64;
MDDSDDEYSR SHGETLTFVD PEDDGVSIGN TQDSQFAYEQ FSVPTQSSQA TDLLPGGTDG
TTNDLPFHDV EDDESDSEKS LTEEQHEQKL PEHACRYCGI SDPLCVAKCT VCRKWFCNSN
DGTSGGHIVH HMVRSQHKEA YTHKDSPCGD TQLECYRCGS KNVFNLGFIP GKKDQVVVII
CRTPCASIAF QNDDNWSPED WKSVIAEKQL LSWIVNVPSE EQVARARKIT ATQAVRMEEL
WRDHPEATVD DLNKPGLDRE PDHVQLRYVD AHHYSKVFRP LVAIEAEYDR RVKESASQAV
GTVRWEQGLR QSVLAFFHLP QFADGVMKLA KGDELRLKHS QTVDGSEWTK IGSVFKIPDN
HGDEVGIEIR GAVDKSVMES RIMFTVDVVW NATTFERQYK ALAALLNDSK AISPYLYQKL
LGHPAEEMML KFDLPRRLSV AGLPELNSSQ MQAVKQVLTR PLSLIQGPPG TGKTVVSATI
VYHLVQKTEG NVLVCSPSNI AVDHLAEKIH KTGLKVVRLC ARSREHSETT VPYLTLQHQL
KVMGGAELQK LIQLKDEAGE LEFKDDLRYM QLKRVKEHEL LAAADVICCT CSSAADARLS
KIRTRTVLID ESTQATEPEI LVSIMRGVRQ LVLVGDHCQL GPVVICKKAA IAGLSQSLFE
RLVLLGIRPF RLQVQYRMHP VLSEFPSNVF YDGSLQNGVT ENDRHMTGVD WHWPKPNKPA
FFWHCSGSEE LSASGTSFLN RTEAANVEKL VSKLIKAGVQ PHQIGVITSY EGQRSFIVNY
MHTQGTLNSK LYENVEIASV DAFQGREKDY IIVTCVRSND ILGIGFLSDP RRLNVAITRA
KYGLVLVGNA KVLARHDLWH ELINHYKSKE MLYEGPINAL KPLNLALPKA TIRTKNNIAG
NANRFGIKRM QYTFNEYKSN DPSQPRLPPT YSNSQNLLSM SKLAQTFNKN VPIPAHMMDP
NVYAAARNQK DRRRGDQRRP PPQAEAAMDL SQGMMSQQSQ QYPPQGASSQ SQYLLDGASS
LSGWSQSQTT TTTTRHHHHR QNRNSQQQMS QDMDDIQQKM DDLLFSQDC
