ID SUV3_RAT Reviewed; 776 AA.
AC Q5EBA1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=ATP-dependent RNA helicase SUPV3L1, mitochondrial;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q8IYB8};
DE AltName: Full=Suppressor of var1 3-like protein 1;
DE Short=SUV3-like protein 1;
DE Flags: Precursor;
GN Name=Supv3l1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Major helicase player in mitochondrial RNA metabolism.
CC Component of the mitochondrial degradosome (mtEXO) complex, that
CC degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality
CC in an ATP-dependent manner. Involved in the degradation of non-coding
CC mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules. ATPase
CC and ATP-dependent multisubstrate helicase, able to unwind double-
CC stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3'
CC direction. Plays a role in the RNA surveillance system in mitochondria;
CC regulates the stability of mature mRNAs, the removal of aberrantly
CC formed mRNAs and the rapid degradation of non coding processing
CC intermediates. Also implicated in recombination and chromatin
CC maintenance pathways. May protect cells from apoptosis. Associates with
CC mitochondrial DNA. {ECO:0000250|UniProtKB:Q8IYB8}.
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:Q8IYB8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8IYB8};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8IYB8};
CC -!- ACTIVITY REGULATION: Helicase activity toward DNA substrate is
CC inhibited by micromolar concentrations of 5,6-dichloro-1-(beta-D-
CC ribofuranosyl)benzotriazole (DRBT) and 4,5,6,7-tetrabromobenzotriazole
CC (TBBT). Helicase activity toward RNA substrate is inhibited by elevated
CC concentrations of TBBT. Inhibited by some ring-expanded nucleoside
CC analogs. {ECO:0000250|UniProtKB:Q8IYB8}.
CC -!- SUBUNIT: Homodimer; in free form. Component of the mitochondrial
CC degradosome (mtEXO) complex which is a heteropentamer containing 2
CC copies of SUPV3L1 and 3 copies of PNPT1. As part of mitochondrial
CC degradosome complex, interacts with GRSF1 in a RNA-dependent manner;
CC the interaction enhances the activity of the complex. Interacts with
CC LAMTOR5/HBXIP, WRN and BLM. {ECO:0000250|UniProtKB:Q8IYB8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IYB8}.
CC Mitochondrion matrix {ECO:0000250|UniProtKB:Q8IYB8}. Mitochondrion
CC matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q8IYB8}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; BC089883; AAH89883.1; -; mRNA.
DR RefSeq; NP_001012480.1; NM_001012462.1.
DR AlphaFoldDB; Q5EBA1; -.
DR SMR; Q5EBA1; -.
DR STRING; 10116.ENSRNOP00000075096; -.
DR iPTMnet; Q5EBA1; -.
DR PhosphoSitePlus; Q5EBA1; -.
DR PaxDb; 10116-ENSRNOP00000000441; -.
DR Ensembl; ENSRNOT00055025059; ENSRNOP00055020489; ENSRNOG00055014607.
DR Ensembl; ENSRNOT00060012415; ENSRNOP00060009386; ENSRNOG00060007530.
DR Ensembl; ENSRNOT00065004628; ENSRNOP00065003327; ENSRNOG00065003251.
DR GeneID; 294385; -.
DR KEGG; rno:294385; -.
DR UCSC; RGD:1305565; rat.
DR AGR; RGD:1305565; -.
DR CTD; 6832; -.
DR RGD; 1305565; Supv3l1.
DR eggNOG; KOG0953; Eukaryota.
DR InParanoid; Q5EBA1; -.
DR OrthoDB; 161833at2759; -.
DR PhylomeDB; Q5EBA1; -.
DR PRO; PR:Q5EBA1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045025; C:mitochondrial degradosome; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; ISS:UniProtKB.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0035946; P:mitochondrial mRNA surveillance; ISS:UniProtKB.
DR GO; GO:0035945; P:mitochondrial ncRNA surveillance; ISS:UniProtKB.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:2000827; P:mitochondrial RNA surveillance; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
DR CDD; cd17913; DEXQc_Suv3; 1.
DR CDD; cd18805; SF2_C_suv3; 1.
DR Gene3D; 1.10.1740.140; -; 1.
DR Gene3D; 1.20.272.40; -; 1.
DR Gene3D; 1.20.58.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022192; SUV3_C.
DR InterPro; IPR041082; Suv3_C_1.
DR InterPro; IPR044774; Suv3_DEXQc.
DR InterPro; IPR041453; Suv3_N.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12513; SUV3_C; 1.
DR Pfam; PF18147; Suv3_C_1; 1.
DR Pfam; PF18114; Suv3_N; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Helicase; Hydrolase; Mitochondrion;
KW Mitochondrion nucleoid; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..776
FT /note="ATP-dependent RNA helicase SUPV3L1, mitochondrial"
FT /id="PRO_0000310547"
FT DOMAIN 194..334
FT /note="Helicase ATP-binding"
FT DOMAIN 353..521
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 650..776
FT /note="Interaction with LAMTOR5, important for protein
FT stability"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB8"
FT REGION 689..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT MOD_RES 99
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB8"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB8"
SQ SEQUENCE 776 AA; 86706 MW; E2C263973DCC0396 CRC64;
MSLPRCALLW ARLPAGRGAG PRAAPCSALR ALVGSFPGAS GRVPCLAASS SASGGSKAPN
TSLFVPLTVK PQGPSADGDV GAELTRPLDK NEVKKILDKF YKRQEIQKLS ADYGLDARLF
HQAFISFRNY IMQSHSLDVD IHIVLNDICF SAAHVDDLFP FFLRHAKQIF PVLECKDDLR
QISDLRRPPN WYPEARAIQR KIIFHSGPTN SGKTYHAIQR YLSATSGVYC GPLKLLAHEI
FEKSNAAGVP CDLVTGEERL TVEPEGKQAT HVSCTVEMCN VATPYEVAVI DEIQMIRDPA
RGWAWTRALL GLCAEEVHLC GESAAIDLVT ELLYTTGEEV EVQKYERLTP ISVLDRALES
LDNLRPGDCI VCFSKNDIYS VSRQIEIRGL ESAVIYGSLP PGTKLAQARK FNDPNDPCKI
LVATDAIGMG LNLSIRRIIF YSLIKPSINE KGEKELEPIT TSQALQIAGR AGRFSSHFKE
GEVTTMHRDD LALLKEILNR PVDPIQAAGL HPTAEQIEMF AYHLPETTLS NLIDIFVDFA
QVDGQYFVCN MDDFKFSAEL IQHIPLSLRV RYVFCTAPIN KKQPFVCSSL LQFARQYSRN
EPLTFAWLRR YIKWPLLPPK NIKDLMDLEA VHDVFDLYLW LSYRFIDMFP DSSFVRSLQK
ELDVIIQEGV HNITKLIKIS ESHKLLNLEP SGSQSRLPGA SKSPARRTRG TKTGNKAAEP
PSPSDKELPL ASRLVQQGLL TADMLKQLQK EWLTQRPEQG KEKVGTRRKK KDPNSD
//
