RENT1_DICDI
ID RENT1_DICDI Reviewed; 1331 AA.
AC Q54I89;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Up-frameshift suppressor 1 homolog;
GN Name=upf1; ORFNames=DDB_G0288923;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 a surveillance
CC complex is believed to activate NMD. {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 -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC from the PI3/PI4-kinase family. {ECO:0000250}.
CC -!- PTM: Phosphorylated probably by smg1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; AAFI02000126; EAL62985.1; -; Genomic_DNA.
DR RefSeq; XP_636490.1; XM_631398.1.
DR AlphaFoldDB; Q54I89; -.
DR SMR; Q54I89; -.
DR STRING; 44689.DDB0233746; -.
DR PaxDb; Q54I89; -.
DR EnsemblProtists; EAL62985; EAL62985; DDB_G0288923.
DR GeneID; 8626873; -.
DR KEGG; ddi:DDB_G0288923; -.
DR dictyBase; DDB_G0288923; upf1.
DR eggNOG; KOG1802; Eukaryota.
DR HOGENOM; CLU_001666_4_1_1; -.
DR InParanoid; Q54I89; -.
DR PhylomeDB; Q54I89; -.
DR Reactome; R-DDI-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DDI-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q54I89; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
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:0043024; F:ribosomal small subunit binding; ISS:dictyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:dictyBase.
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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; Helicase; Hydrolase; Metal-binding;
KW Nonsense-mediated mRNA decay; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1331
FT /note="Regulator of nonsense transcripts 1"
FT /id="PRO_0000375999"
FT DOMAIN 176..336
FT /note="Upf1 CH-rich"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..218
FT /note="C3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 198..228
FT /note="CC/SHH/C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 246..276
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 1032..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..131
FT /evidence="ECO:0000255"
FT COILED 1149..1178
FT /evidence="ECO:0000255"
FT MOTIF 1174..1175
FT /note="[ST]-Q motif 1"
FT MOTIF 1189..1190
FT /note="[ST]-Q motif 2"
FT COMPBIAS 18..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..127
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 558..565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT BINDING 735
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 772
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 902
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
SQ SEQUENCE 1331 AA; 151558 MW; C2D37523D76EE85D CRC64;
MYGFNIGKAE NAGLHLDNKK SENNNSSNNE LHKVINTINN GFQFKDDDDE DNENNLNNES
SSDEENQQQQ NNNNNNNKNQ FEDDDEDQEE EEYISGDDLN NNGQESDDYE EEEEDDDEDE
EEEDEESKKL NYDSFFGANM SHNMDFLNSQ NINSQIGLMD PHLHSSQLNF EEPQEEIELP
AHACAYCATH ELSTVVKCMH PSCGKWFCNG KGKTKSSHII THLVKSKHKE VALHPESSFG
DTTLECFNCG CKNIFLLGFI TARTESVVVL LCRDPCASGP SKEVNWDMSS WQPLINGGEK
AFCSWLVKTP SQVDSERSRQ ITIQQILRLE EFWKMDPEAT LLDIEAPRSD DEKPASTQLA
YKDAYEYREI ISPLIELEAK HEKELRESLS QSGISIEWSQ GINKRYTATF PFSRSDLEFK
VVPGDELKLQ FISSTGGVIE WEDTGRVIHI DDENLLSLET KSRCSFDSGP KGSYRMEMVW
RSTSSERILS AMKSFAIKEQ ALSSYLYHAL LGHPDIPPAP LDIQLPTNFH LKNLPRLNES
QISAVNKVLT APLSLIQGPP GTGKTVISSF IIHHLVKYVK GNDKVLVCTP SNVAIDQLTG
KLHEIGLKVV RLSSKLREEV ASPVEHLTLH KQVYKLDQMG DGELGKLRKL KEAFGSLSNE
DEKRYIYLRR MMEMAILRKA DVICATCVGA GDPRLSQFRF PHILIDESTQ ASEPECLIPL
MMGAKQVILV GDHRQLGPVL LCKKVVDAGL SQSLFERLIS LGHHPERLTI QYRMHPSLTE
FPSNTSYEGQ LVSELSHTDR DSQSKFPWPQ PKDPMFFFNC TGSEEISSSG TSFINTTEAS
ICEKIVTKFL ELGSLPGQIG IITPYEGQRA YITSHMQKSG KLNLELYKSI EVASVDSFQG
REKDYIILSC VRSNDYQGIG FLQDPRRLNV ALTRARFGLI ILGNAKVLSK DPLWNSLISH
FKNKNVLVEG SLANLKQSPV ILQKPKKLYG QGKLPIPGQN SNSFNYDREH IDPNIGMNMV
YGISNNNINN NSNNINNNNN NNINNNINNN NNQRFNTQDG RYSNSQTSSS SQTYYGSTNS
SGNTINSNQN QFFNTPSSYS ANTGSSYQYR FQQYQQLQQP QPQQQQQPQQ QQQPQQQQQP
QQPQQQQPQQ QKQYQQQQQQ QQQQQQQQQQ QQQQQKQQPH QQYQSQKQQQ QQQYQQPQQY
QQQNQQYHQS QLPPKQYHNQ RFNNNNNNNI NNNNNNNNNN NNNNNNNNNN NNINNNNSKN
QNQNQSPRRS PVVGTLQLHC KFDSQPNNNK HISDPNQPQI SNPNMSIPLS QSLSFNDLSQ
EQFNKSNSRK D
