ID SUV3_HUMAN Reviewed; 786 AA.
AC Q8IYB8; A8K301; O43630;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 178.
DE RecName: Full=ATP-dependent RNA helicase SUPV3L1, mitochondrial;
DE EC=3.6.4.13 {ECO:0000269|PubMed:12466530};
DE AltName: Full=Suppressor of var1 3-like protein 1;
DE Short=SUV3-like protein 1;
DE Flags: Precursor;
GN Name=SUPV3L1; Synonyms=SUV3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10453991;
RA Dmochowska A., Kalita K., Krawczyk M., Golik P., Mroczek K., Lazowska J.,
RA Stepien P.P., Bartnik E.;
RT "A human putative Suv3-like RNA helicase is conserved between Rhodobacter
RT and all eukaryotes.";
RL Acta Biochim. Pol. 46:155-162(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLY-207.
RX PubMed=12466530; DOI=10.1093/nar/gkf647;
RA Minczuk M., Piwowarski J., Papworth M.A., Awiszus K., Schalinski S.,
RA Dziembowski A., Dmochowska A., Bartnik E., Tokatlidis K., Stepien P.P.,
RA Borowski P.;
RT "Localisation of the human hSuv3p helicase in the mitochondrial matrix and
RT its preferential unwinding of dsDNA.";
RL Nucleic Acids Res. 30:5074-5086(2002).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=12694177; DOI=10.1046/j.1432-1033.2003.03540.x;
RA Borowski P., Deinert J., Schalinski S., Bretner M., Ginalski K.,
RA Kulikowski T., Shugar D.;
RT "Halogenated benzimidazoles and benzotriazoles as inhibitors of the
RT NTPase/helicase activities of hepatitis C and related viruses.";
RL Eur. J. Biochem. 270:1645-1653(2003).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=14561097; DOI=10.1021/jm030277k;
RA Zhang N., Chen H.-M., Koch V., Schmitz H., Minczuk M., Stepien P.,
RA Fattom A.I., Naso R.B., Kalicharran K., Borowski P., Hosmane R.S.;
RT "Potent inhibition of NTPase/helicase of the West Nile Virus by ring-
RT expanded ('fat') nucleoside analogues.";
RL J. Med. Chem. 46:4776-4789(2003).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND MUTAGENESIS OF
RP LYS-213.
RX PubMed=15096047; DOI=10.1021/bi0356449;
RA Shu Z., Vijayakumar S., Chen C.-F., Chen P.-L., Lee W.-H.;
RT "Purified human SUV3p exhibits multiple-substrate unwinding activity upon
RT conformational change.";
RL Biochemistry 43:4781-4790(2004).
RN [10]
RP INTERACTION WITH LAMTOR5/HBXIP.
RX PubMed=16176273; DOI=10.1111/j.1742-4658.2005.04910.x;
RA Minczuk M., Mroczek S., Pawlak S.D., Stepien P.P.;
RT "Human ATP-dependent RNA/DNA helicase hSuv3p interacts with the cofactor of
RT survivin HBXIP.";
RL FEBS J. 272:5008-5019(2005).
RN [11]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17352692; DOI=10.1042/bc20060108;
RA Szczesny R.J., Obriot H., Paczkowska A., Jedrzejczak R., Dmochowska A.,
RA Bartnik E., Formstecher P., Polakowska R., Stepien P.P.;
RT "Down-regulation of human RNA/DNA helicase SUV3 induces apoptosis by a
RT caspase- and AIF-dependent pathway.";
RL Biol. Cell 99:323-332(2007).
RN [12]
RP FUNCTION, AND INTERACTION WITH WRN AND BLM.
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 [13]
RP SUBCELLULAR LOCATION, ASSOCIATION WITH MITOCHONDRIAL DNA, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18063578; DOI=10.1074/jbc.m708444200;
RA Bogenhagen D.F., Rousseau D., Burke S.;
RT "The layered structure of human mitochondrial DNA nucleoids.";
RL J. Biol. Chem. 283:3665-3675(2008).
RN [14]
RP FUNCTION.
RX PubMed=18678873; DOI=10.1074/jbc.m802991200;
RA Khidr L., Wu G., Davila A., Procaccio V., Wallace D., Lee W.H.;
RT "Role of SUV3 helicase in maintaining mitochondrial homeostasis in human
RT cells.";
RL J. Biol. Chem. 283:27064-27073(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-725, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL DEGRADOSOME COMPLEX,
RP RNA-BINDING, HOMODIMERIZATION, AND MUTAGENESIS OF LYS-213 AND
RP 576-THR--LYS-581.
RX PubMed=19509288; DOI=10.1074/jbc.m109.009605;
RA Wang D.D., Shu Z., Lieser S.A., Chen P.L., Lee W.H.;
RT "Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa
RT heteropentamer to cooperatively degrade double-stranded RNA with a 3'-to-5'
RT directionality.";
RL J. Biol. Chem. 284:20812-20821(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-99 AND LYS-220, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19864255; DOI=10.1093/nar/gkp903;
RA Szczesny R.J., Borowski L.S., Brzezniak L.K., Dmochowska A.,
RA Gewartowski K., Bartnik E., Stepien P.P.;
RT "Human mitochondrial RNA turnover caught in flagranti: involvement of
RT hSuv3p helicase in RNA surveillance.";
RL Nucleic Acids Res. 38:279-298(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-725, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL DEGRADOSOME COMPLEX, AND
RP INTERACTION WITH GRSF1.
RX PubMed=29967381; DOI=10.1038/s41467-018-05007-9;
RA Pietras Z., Wojcik M.A., Borowski L.S., Szewczyk M., Kulinski T.M.,
RA Cysewski D., Stepien P.P., Dziembowski A., Szczesny R.J.;
RT "Dedicated surveillance mechanism controls G-quadruplex forming non-coding
RT RNAs in human mitochondria.";
RL Nat. Commun. 9:2558-2558(2018).
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
CC (PubMed:29967381). ATPase and ATP-dependent multisubstrate helicase,
CC able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA
CC heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA
CC surveillance system in mitochondria; regulates the stability of mature
CC mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation
CC of non coding processing intermediates. Also implicated in
CC recombination and chromatin maintenance pathways. May protect cells
CC from apoptosis. Associates with mitochondrial DNA.
CC {ECO:0000269|PubMed:12466530, ECO:0000269|PubMed:15096047,
CC ECO:0000269|PubMed:17352692, ECO:0000269|PubMed:17961633,
CC ECO:0000269|PubMed:18678873, ECO:0000269|PubMed:19509288,
CC ECO:0000269|PubMed:19864255, ECO:0000269|PubMed:29967381}.
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:0000269|PubMed:12466530};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15096047};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15096047};
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:0000269|PubMed:12694177, ECO:0000269|PubMed:14561097}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41.9 uM for ATP {ECO:0000269|PubMed:12466530,
CC ECO:0000269|PubMed:15096047};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:12466530,
CC ECO:0000269|PubMed:15096047};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:12466530, ECO:0000269|PubMed:15096047};
CC -!- SUBUNIT: Homodimer; in free form (PubMed:19509288). Component of the
CC mitochondrial degradosome (mtEXO) complex which is a heteropentamer
CC containing 2 copies of SUPV3L1 and 3 copies of PNPT1 (PubMed:19509288,
CC PubMed:29967381). As part of mitochondrial degradosome complex,
CC interacts with GRSF1 in a RNA-dependent manner; the interaction
CC enhances the activity of the complex (PubMed:29967381). Interacts with
CC LAMTOR5/HBXIP, WRN and BLM (PubMed:16176273, PubMed:17961633).
CC {ECO:0000269|PubMed:16176273, ECO:0000269|PubMed:17961633,
CC ECO:0000269|PubMed:19509288, ECO:0000269|PubMed:29967381}.
CC -!- INTERACTION:
CC Q8IYB8; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2876787, EBI-741037;
CC Q8IYB8; Q8N7X4: MAGEB6; NbExp=3; IntAct=EBI-2876787, EBI-6447163;
CC Q8IYB8; Q8TCS8: PNPT1; NbExp=6; IntAct=EBI-2876787, EBI-1052020;
CC Q8IYB8; Q8IYB8: SUPV3L1; NbExp=2; IntAct=EBI-2876787, EBI-2876787;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17352692}.
CC Mitochondrion matrix {ECO:0000269|PubMed:12466530,
CC ECO:0000269|PubMed:17352692, ECO:0000269|PubMed:19864255}.
CC Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000269|PubMed:18063578}.
CC -!- TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:10453991}.
CC -!- SIMILARITY: Belongs to the 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; AF042169; AAB97370.1; -; mRNA.
DR EMBL; AK290416; BAF83105.1; -; mRNA.
DR EMBL; AL596223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54314.1; -; Genomic_DNA.
DR EMBL; BC036112; AAH36112.1; -; mRNA.
DR CCDS; CCDS7287.1; -.
DR RefSeq; NP_001288612.1; NM_001301683.1.
DR RefSeq; NP_003162.2; NM_003171.4.
DR PDB; 3RC3; X-ray; 2.08 A; A=47-722.
DR PDB; 3RC8; X-ray; 2.90 A; A=47-722.
DR PDB; 7W1R; X-ray; 3.20 A; A=49-722.
DR PDBsum; 3RC3; -.
DR PDBsum; 3RC8; -.
DR PDBsum; 7W1R; -.
DR AlphaFoldDB; Q8IYB8; -.
DR SMR; Q8IYB8; -.
DR BioGRID; 112699; 137.
DR ComplexPortal; CPX-2842; Mitochondrial degradosome complex.
DR IntAct; Q8IYB8; 31.
DR MINT; Q8IYB8; -.
DR STRING; 9606.ENSP00000352678; -.
DR BindingDB; Q8IYB8; -.
DR ChEMBL; CHEMBL3642; -.
DR GlyGen; Q8IYB8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IYB8; -.
DR PhosphoSitePlus; Q8IYB8; -.
DR SwissPalm; Q8IYB8; -.
DR BioMuta; SUPV3L1; -.
DR DMDM; 74759699; -.
DR EPD; Q8IYB8; -.
DR jPOST; Q8IYB8; -.
DR MassIVE; Q8IYB8; -.
DR MaxQB; Q8IYB8; -.
DR PaxDb; 9606-ENSP00000352678; -.
DR PeptideAtlas; Q8IYB8; -.
DR ProteomicsDB; 71153; -.
DR Pumba; Q8IYB8; -.
DR Antibodypedia; 28732; 174 antibodies from 26 providers.
DR DNASU; 6832; -.
DR Ensembl; ENST00000359655.9; ENSP00000352678.4; ENSG00000156502.14.
DR GeneID; 6832; -.
DR KEGG; hsa:6832; -.
DR MANE-Select; ENST00000359655.9; ENSP00000352678.4; NM_003171.5; NP_003162.2.
DR UCSC; uc001jpe.2; human.
DR AGR; HGNC:11471; -.
DR CTD; 6832; -.
DR DisGeNET; 6832; -.
DR GeneCards; SUPV3L1; -.
DR HGNC; HGNC:11471; SUPV3L1.
DR HPA; ENSG00000156502; Low tissue specificity.
DR MIM; 605122; gene.
DR neXtProt; NX_Q8IYB8; -.
DR OpenTargets; ENSG00000156502; -.
DR PharmGKB; PA36257; -.
DR VEuPathDB; HostDB:ENSG00000156502; -.
DR eggNOG; KOG0953; Eukaryota.
DR GeneTree; ENSGT00390000003100; -.
DR HOGENOM; CLU_010647_3_2_1; -.
DR InParanoid; Q8IYB8; -.
DR OMA; QPANWYT; -.
DR OrthoDB; 161833at2759; -.
DR PhylomeDB; Q8IYB8; -.
DR TreeFam; TF106432; -.
DR PathwayCommons; Q8IYB8; -.
DR Reactome; R-HSA-9836573; Mitochondrial RNA degradation.
DR SignaLink; Q8IYB8; -.
DR BioGRID-ORCS; 6832; 697 hits in 1184 CRISPR screens.
DR ChiTaRS; SUPV3L1; human.
DR GeneWiki; SUPV3L1; -.
DR GenomeRNAi; 6832; -.
DR Pharos; Q8IYB8; Tbio.
DR PRO; PR:Q8IYB8; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8IYB8; Protein.
DR Bgee; ENSG00000156502; Expressed in oocyte and 200 other cell types or tissues.
DR ExpressionAtlas; Q8IYB8; baseline and differential.
DR Genevisible; Q8IYB8; HS.
DR GO; GO:0045025; C:mitochondrial degradosome; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; IDA: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; IMP:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IMP:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0004386; F:helicase activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IMP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IMP:UniProtKB.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0035946; P:mitochondrial mRNA surveillance; IMP:UniProtKB.
DR GO; GO:0035945; P:mitochondrial ncRNA surveillance; IMP:UniProtKB.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IMP:UniProtKB.
DR GO; GO:0000957; P:mitochondrial RNA catabolic process; TAS:Reactome.
DR GO; GO:2000827; P:mitochondrial RNA surveillance; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; IDA:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; IMP: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 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Helicase; Hydrolase; Mitochondrion;
KW Mitochondrion nucleoid; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..786
FT /note="ATP-dependent RNA helicase SUPV3L1, mitochondrial"
FT /id="PRO_0000310545"
FT DOMAIN 194..334
FT /note="Helicase ATP-binding"
FT DOMAIN 353..518
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 650..786
FT /note="Interaction with LAMTOR5, important for protein
FT stability"
FT /evidence="ECO:0000269|PubMed:16176273"
FT REGION 690..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..786
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:0007744|PubMed:19608861"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 2
FT /note="S -> F (in dbSNP:rs33998366)"
FT /id="VAR_061214"
FT VARIANT 30
FT /note="P -> T (in dbSNP:rs34596380)"
FT /id="VAR_037076"
FT MUTAGEN 207
FT /note="G->V: Abolishes ATPase and dsDNA and dsRNA helicase
FT activities."
FT /evidence="ECO:0000269|PubMed:12466530"
FT MUTAGEN 213
FT /note="K->A,R: Abolishes ATPase activity. Abolishes
FT helicase activity and reduces double-stranded RNA
FT degradation. Does not abolish formation of the
FT mitochondrial RNA-degrading complex."
FT /evidence="ECO:0000269|PubMed:15096047,
FT ECO:0000269|PubMed:19509288"
FT MUTAGEN 576..581
FT /note="Missing: Does not abolish ATPase activity. Shows a
FT loss of double-stranded RNA-binding, helicase and degrading
FT activities."
FT /evidence="ECO:0000269|PubMed:19509288"
FT CONFLICT 234..235
FT /note="KL -> TS (in Ref. 1; AAB97370)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="V -> E (in Ref. 1; AAB97370)"
FT /evidence="ECO:0000305"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:3RC8"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:3RC8"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:3RC3"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 302..311
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 375..387
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 401..412
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 435..441
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 461..468
FT /evidence="ECO:0007829|PDB:3RC3"
FT TURN 475..477
FT /evidence="ECO:0007829|PDB:3RC8"
FT STRAND 479..487
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 490..499
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 514..523
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 529..539
FT /evidence="ECO:0007829|PDB:3RC3"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 552..560
FT /evidence="ECO:0007829|PDB:3RC3"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 568..576
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 584..598
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 605..611
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 622..642
FT /evidence="ECO:0007829|PDB:3RC3"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 652..671
FT /evidence="ECO:0007829|PDB:3RC3"
FT HELIX 673..682
FT /evidence="ECO:0007829|PDB:3RC3"
SQ SEQUENCE 786 AA; 87991 MW; FD3BC8EC64C23E42 CRC64;
MSFSRALLWA RLPAGRQAGH RAAICSALRP HFGPFPGVLG QVSVLATASS SASGGSKIPN
TSLFVPLTVK PQGPSADGDV GAELTRPLDK NEVKKVLDKF YKRKEIQKLG ADYGLDARLF
HQAFISFRNY IMQSHSLDVD IHIVLNDICF GAAHADDLFP FFLRHAKQIF PVLDCKDDLR
KISDLRIPPN WYPDARAMQR KIIFHSGPTN SGKTYHAIQK YFSAKSGVYC GPLKLLAHEI
FEKSNAAGVP CDLVTGEERV TVQPNGKQAS HVSCTVEMCS VTTPYEVAVI DEIQMIRDPA
RGWAWTRALL GLCAEEVHLC GEPAAIDLVM ELMYTTGEEV EVRDYKRLTP ISVLDHALES
LDNLRPGDCI VCFSKNDIYS VSRQIEIRGL ESAVIYGSLP PGTKLAQAKK FNDPNDPCKI
LVATDAIGMG LNLSIRRIIF YSLIKPSINE KGERELEPIT TSQALQIAGR AGRFSSRFKE
GEVTTMNHED LSLLKEILKR PVDPIRAAGL HPTAEQIEMF AYHLPDATLS NLIDIFVDFS
QVDGQYFVCN MDDFKFSAEL IQHIPLSLRV RYVFCTAPIN KKQPFVCSSL LQFARQYSRN
EPLTFAWLRR YIKWPLLPPK NIKDLMDLEA VHDVLDLYLW LSYRFMDMFP DASLIRDLQK
ELDGIIQDGV HNITKLIKMS ETHKLLNLEG FPSGSQSRLS GTLKSQARRT RGTKALGSKA
TEPPSPDAGE LSLASRLVQQ GLLTPDMLKQ LEKEWMTQQT EHNKEKTESG THPKGTRRKK
KEPDSD
//
