SUV3_MOUSE
ID SUV3_MOUSE Reviewed; 779 AA.
AC Q80YD1; Q50HX5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
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; Synonyms=Suv3l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Zhang C., Yang T., Liu G., Chen Q.;
RT "A null mutation existed in SUV3L1 of SAMP8/Ta.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=17961633; DOI=10.1016/j.mad.2007.09.001;
RA Pereira M., Mason P., Szczesny R.J., Maddukuri L., Dziwura S.,
RA Jedrzejczak R., Paul E., Wojcik A., Dybczynska L., Tudek B., Bartnik E.,
RA Klysik J., Bohr V.A., Stepien P.P.;
RT "Interaction of human SUV3 RNA/DNA helicase with BLM helicase; loss of the
RT SUV3 gene results in mouse embryonic lethality.";
RL Mech. Ageing Dev. 128:609-617(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By
CC similarity). ATPase and ATP-dependent multisubstrate helicase, able to
CC unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in
CC the 5'-to-3' direction. Plays a role in the RNA surveillance system in
CC mitochondria; regulates the stability of mature mRNAs, the removal of
CC aberrantly formed mRNAs and the rapid degradation of non coding
CC processing intermediates. Also implicated in recombination and
CC chromatin maintenance pathways. May protect cells from apoptosis.
CC Associates with 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 -!- DISRUPTION PHENOTYPE: Die in utero before midgestation. Show elevated
CC sister chromatid exchange (SCE). {ECO:0000269|PubMed:17961633}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; AJ968954; CAI92124.1; -; mRNA.
DR EMBL; BC049796; AAH49796.1; -; mRNA.
DR CCDS; CCDS35920.1; -.
DR RefSeq; NP_852088.1; NM_181423.2.
DR AlphaFoldDB; Q80YD1; -.
DR SMR; Q80YD1; -.
DR BioGRID; 237212; 3.
DR STRING; 10090.ENSMUSP00000020273; -.
DR iPTMnet; Q80YD1; -.
DR PhosphoSitePlus; Q80YD1; -.
DR EPD; Q80YD1; -.
DR MaxQB; Q80YD1; -.
DR PaxDb; Q80YD1; -.
DR PeptideAtlas; Q80YD1; -.
DR PRIDE; Q80YD1; -.
DR ProteomicsDB; 254784; -.
DR Antibodypedia; 28732; 140 antibodies from 26 providers.
DR DNASU; 338359; -.
DR Ensembl; ENSMUST00000020273; ENSMUSP00000020273; ENSMUSG00000020079.
DR GeneID; 338359; -.
DR KEGG; mmu:338359; -.
DR UCSC; uc007fhd.1; mouse.
DR CTD; 6832; -.
DR MGI; MGI:2441711; Supv3l1.
DR VEuPathDB; HostDB:ENSMUSG00000020079; -.
DR eggNOG; KOG0953; Eukaryota.
DR GeneTree; ENSGT00390000003100; -.
DR HOGENOM; CLU_010647_3_2_1; -.
DR InParanoid; Q80YD1; -.
DR OMA; AKTVFPH; -.
DR OrthoDB; 1106167at2759; -.
DR PhylomeDB; Q80YD1; -.
DR TreeFam; TF106432; -.
DR BRENDA; 3.6.4.13; 3474.
DR BioGRID-ORCS; 338359; 27 hits in 77 CRISPR screens.
DR PRO; PR:Q80YD1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q80YD1; protein.
DR Bgee; ENSMUSG00000020079; Expressed in otic placode and 257 other tissues.
DR ExpressionAtlas; Q80YD1; baseline and differential.
DR Genevisible; Q80YD1; MM.
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:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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:0042803; F:protein homodimerization activity; ISO:MGI.
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:0070584; P:mitochondrion morphogenesis; 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 Gene3D; 3.40.50.300; -; 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 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; SSF52540; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein 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..779
FT /note="ATP-dependent RNA helicase SUPV3L1, mitochondrial"
FT /id="PRO_0000310546"
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..779
FT /note="Interaction with LAMTOR5, important for protein
FT stability"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB8"
FT REGION 693..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..779
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 725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB8"
FT CONFLICT 109
FT /note="L -> R (in Ref. 1; CAI92124)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="D -> G (in Ref. 1; CAI92124)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 779 AA; 87005 MW; 877F2B611FEEE1A9 CRC64;
MSLPRCTLLW ARLPAGRGAG PRAAPCSALR ALVGSFPGAS GRVPCLAASS SASGGSKAPN
TSLFVPLTVK PQGPSADGDV GAELTRPLDK NEVKKILDKF YKRQEIQKLS ADYGLDARLF
HQAFISFRNY IMQSHSLDVD IHIVLNDICF SAAHVDDLFP FFLRHAKQIF PVLECKDDLR
KISDLRIPPN WYPEARARQR KIIFHSGPTN SGKTYHAIQR YLSATSGVYC GPLKLLAHEI
FEKSNAAGVP CDLVTGEERL TVEPEGKQAT HVSCTVEMCN VATPYEVAVI DEIQMIRDPA
RGWAWTRALL GLCAEEVHLC GESAAINLVS ELLYTTGEEV EVQKYERLTP ISVLDHALES
LDNLQPGDCI VCFSKNDIYS VSRQIEIRGL ESAVIYGSLP PGTKLAQARK FNDPNDPCKI
LVATDAIGMG LNLSIRRIIF YSLIKPSINE KGEKELEPIT TSQALQIAGR AGRFSSHFKE
GQVTTMHRDD LALLKDILNR PVDPIQAAGL HPTAEQIEMF AYHLPETTLS NLIDIFVDFA
QVDGQYFVCN MDDFKFSAEL IQHIPLSLRV RYVFCTAPIN KKQPFVCSSL LQFARQYSRN
EPLTFAWLRR YIKWPLLPPK NIKDLMDLEA VHDVFDLYLW LSYRFIDMFP DSSLVRSLQK
ELDAIIQEGV HNITKLIKIS ESRKLLNLES LPSGDQSRLS GASKSPARRT RGTKSAGNKA
TEPLSPSDKE LPLASRLVQQ GLLTADMLRQ LQKEWLTQQP EHSREKVGTR RKKKDPDSD
