RENT1_TAKRU
ID RENT1_TAKRU Reviewed; 1097 AA.
AC Q98TR3;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Putative 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 RENT1;
GN Name=rent1;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11353399; DOI=10.1007/s003350030004;
RA Clarke D., Elgar G., Clark M.S.;
RT "Comparative analysis of human 19p12-13 region in Fugu and mouse.";
RL Mamm. Genome 12:478-483(2001).
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. The formation of an rent1-rent2-
CC rent3 surveillance complex is believed to activate NMD (By similarity).
CC {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}. Cytoplasm, P-body
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; AJ301641; CAC33025.1; -; Genomic_DNA.
DR AlphaFoldDB; Q98TR3; -.
DR SMR; Q98TR3; -.
DR STRING; 31033.ENSTRUP00000012294; -.
DR eggNOG; KOG1802; Eukaryota.
DR InParanoid; Q98TR3; -.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
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; 1.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Metal-binding;
KW Nonsense-mediated mRNA decay; Nucleotide-binding; Reference proteome;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..1097
FT /note="Putative regulator of nonsense transcripts 1"
FT /id="PRO_0000080718"
FT DOMAIN 96..254
FT /note="Upf1 CH-rich"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 42..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..137
FT /note="C3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 119..147
FT /note="CC/SHH/C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 165..195
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 977..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 474..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT BINDING 683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 813
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
SQ SEQUENCE 1097 AA; 122339 MW; FDCC7C2B4E26AC54 CRC64;
MSVEAYGPSS QTLTFLDTEE TELLGADTQG SEYDFTDFTL PSQTQTQGHT QSQLDNQLNG
PDDGLHNGGM DDSVAKASQL LAELNFEEDE EDTYYTKDLP VHACRSYCGI HDPACVVYCN
TSKKWFCNGR GNTSGSHIVN HLVRAKCKEV TLHKDGPLGE TVLECYNCGC RNVFLLGFIP
AKADSVVVLL CRQPCASQSS LKDINWDSSQ WQPLIQDRCF LSWLVKIPSE QEQLRARQIT
AQQINKLEEL WKDNPCATLE DLEKPGVDEE PQHVLLRYED AYQYQNIFGP LVKLEADYDK
KLKESQTQDN ITVRWDLGLN KKRIAYFTLP KTDSDMRLMQ GDEICLRYKG DLAPLWKGIG
HVIKVPDSYG DEIAIELRTS VGAPVEIPHN YQVDFVWKST SFDRMQSALK TFAVDETSVS
GYIYHKLLGH EVEDVTIKCQ LPKRFTANGL PDLNHSQVYA VKTVLQRPLS LIQGPPGTGK
TVTSATIVYH LSRQGNGPVL VCAPSNIAVD QLTEKIDKTG LKVVRLCAKS REAIESPVSF
LALHNQISNM DSMPELQKLQ QLKDETGELS SADEKRYRAL KRTAERELLM NADVIWCTCV
RAGDPRLAKM QFRSILIDES TQATEPKCIG PVELGAKQLI LGEITASWSC VMCKKAAKAG
LSQSLFERLV VLGIRPIRLQ VQYRMHPALS AFPSNIFYEG SLQNGVTAGD RIKKGFDFQW
PQPEKPMFFY VTQGQEEIAS SGTSYLNRTE AANVEKITTR LLKAGAKPDQ IGIITPYEGQ
RSYLVQYMQF SGSLHTKLYQ VEIASVDAFQ GREKDFIILS CVRANEHQGI GFLNDPRRLN
VALTRAKYGV IIVGNPKALS KQPLWNNLLN NYKEQKVLVE GPLNNLRESL MQFSKPRKLV
NTINPRFMST AMYDAREALI PGSAYDRSNT GGRPSNMYFQ THDQIGMIGA AASHLAALNI
PIPFNLVMPP MPPPSYQGQT NGPAAGRGAM KGKSGRGGRQ RIQWFWEPGG WSHAKQSDQP
GWGFPVILSG ATDTGLHLHE PAFPDEPART LPARALPWDS YLGDEFKSQI DVALSQDSTY
QGERAYQHGG VTGLSQY
