MOV10_HUMAN
ID MOV10_HUMAN Reviewed; 1003 AA.
AC Q9HCE1; Q5JR03; Q8TEF0; Q9BSY3; Q9BUJ9;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Helicase MOV-10 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000269|PubMed:24726324};
DE AltName: Full=Armitage homolog {ECO:0000303|PubMed:17507929};
DE AltName: Full=Moloney leukemia virus 10 protein;
GN Name=MOV10 {ECO:0000312|HGNC:HGNC:7200}; Synonyms=KIAA1631;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, Placenta, and Skin;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH AGO1 AND
RP AGO2, AND SUBCELLULAR LOCATION.
RX PubMed=16289642; DOI=10.1016/j.cub.2005.10.048;
RA Meister G., Landthaler M., Peters L., Chen P.Y., Urlaub H., Luehrmann R.,
RA Tuschl T.;
RT "Identification of novel argonaute-associated proteins.";
RL Curr. Biol. 15:2149-2155(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH DICER1;
RP AGO2; EIF6; RPL7A AND TARBP2, AND ASSOCIATION WITH THE 60S RIBOSOME.
RX PubMed=17507929; DOI=10.1038/nature05841;
RA Chendrimada T.P., Finn K.J., Ji X., Baillat D., Gregory R.I.,
RA Liebhaber S.A., Pasquinelli A.E., Shiekhattar R.;
RT "MicroRNA silencing through RISC recruitment of eIF6.";
RL Nature 447:823-828(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION (MICROBIAL INFECTION),
RP RNA-BINDING, AND INTERACTION WITH HDAG (MICROBIAL INFECTION).
RX PubMed=18552826; DOI=10.1038/nsmb.1440;
RA Haussecker D., Cao D., Huang Y., Parameswaran P., Fire A.Z., Kay M.A.;
RT "Capped small RNAs and MOV10 in human hepatitis delta virus replication.";
RL Nat. Struct. Mol. Biol. 15:714-721(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254, 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY MASS
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254 AND SER-969, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP FUNCTION, AND INTERACTION WITH HIV-1 GAG (MICROBIAL INFECTION).
RX PubMed=20215113; DOI=10.1074/jbc.m110.109314;
RA Wang X., Han Y., Dang Y., Fu W., Zhou T., Ptak R.G., Zheng Y.H.;
RT "Moloney leukemia virus 10 (MOV10) protein inhibits retrovirus
RT replication.";
RL J. Biol. Chem. 285:14346-14355(2010).
RN [15]
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 [16]
RP FUNCTION, AND INTERACTION WITH APOBEC3G AND AGO2.
RX PubMed=22791714; DOI=10.1074/jbc.m112.354001;
RA Liu C., Zhang X., Huang F., Yang B., Li J., Liu B., Luo H., Zhang P.,
RA Zhang H.;
RT "APOBEC3G inhibits microRNA-mediated repression of translation by
RT interfering with the interaction between Argonaute-2 and MOV10.";
RL J. Biol. Chem. 287:29373-29383(2012).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH L1RE1.
RX PubMed=23093941; DOI=10.1371/journal.pgen.1002941;
RA Goodier J.L., Cheung L.E., Kazazian H.H. Jr.;
RT "MOV10 RNA helicase is a potent inhibitor of retrotransposition in cells.";
RL PLoS Genet. 8:E1002941-E1002941(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160 AND SER-432, AND
RP IDENTIFICATION BY 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 [19]
RP INTERACTION WITH TRIM71.
RX PubMed=23125361; DOI=10.1093/nar/gks1032;
RA Loedige I., Gaidatzis D., Sack R., Meister G., Filipowicz W.;
RT "The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
RT function.";
RL Nucleic Acids Res. 41:518-532(2013).
RN [20]
RP INTERACTION WITH DHX34.
RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020;
RA Hug N., Caceres J.F.;
RT "The RNA helicase DHX34 activates NMD by promoting a transition from the
RT surveillance to the decay-inducing complex.";
RL Cell Rep. 8:1845-1856(2014).
RN [21]
RP FUNCTION, INTERACTION WITH FMR1, AND RNA-BINDING.
RX PubMed=25464849; DOI=10.1016/j.celrep.2014.10.054;
RA Kenny P.J., Zhou H., Kim M., Skariah G., Khetani R.S., Drnevich J.,
RA Arcila M.L., Kosik K.S., Ceman S.;
RT "MOV10 and FMRP regulate AGO2 association with microRNA recognition
RT elements.";
RL Cell Rep. 9:1729-1741(2014).
RN [22]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-530 AND ASP-645,
RP SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH AGO2; TNRC6B AND
RP UPF1.
RX PubMed=24726324; DOI=10.1016/j.molcel.2014.03.017;
RA Gregersen L.H., Schueler M., Munschauer M., Mastrobuoni G., Chen W.,
RA Kempa S., Dieterich C., Landthaler M.;
RT "MOV10 Is a 5' to 3' RNA helicase contributing to UPF1 mRNA target
RT degradation by translocation along 3' UTRs.";
RL Mol. Cell 54:573-585(2014).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-969 AND SER-977, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SHFL.
RX PubMed=27974568; DOI=10.1128/jvi.01606-16;
RA Balinsky C.A., Schmeisser H., Wells A.I., Ganesan S., Jin T., Singh K.,
RA Zoon K.C.;
RT "IRAV (FLJ11286), an Interferon-Stimulated Gene with Antiviral Activity
RT against Dengue Virus, Interacts with MOV10.";
RL J. Virol. 91:0-0(2017).
RN [25]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TUT4 AND TUT7, AND
RP MUTAGENESIS OF LYS-530.
RX PubMed=30122351; DOI=10.1016/j.cell.2018.07.022;
RA Warkocki Z., Krawczyk P.S., Adamska D., Bijata K., Garcia-Perez J.L.,
RA Dziembowski A.;
RT "Uridylation by TUT4/7 Restricts Retrotransposition of Human LINE-1s.";
RL Cell 0:0-0(2018).
RN [26]
RP FUNCTION, MUTAGENESIS OF GLN-129 AND GLN-869, INTERACTION WITH IKBKE, AND
RP CLEAVAGE BY PICORNAVIRUS PROTEASES (MICROBIAL INFECTION).
RX PubMed=27016603; DOI=10.4049/jimmunol.1501359;
RA Cuevas R.A., Ghosh A., Wallerath C., Hornung V., Coyne C.B., Sarkar S.N.;
RT "MOV10 Provides Antiviral Activity against RNA Viruses by Enhancing RIG-I-
RT MAVS-Independent IFN Induction.";
RL J. Immunol. 196:3877-3886(2016).
RN [27]
RP FUNCTION, AND MUTAGENESIS OF GLU-646.
RX PubMed=29258557; DOI=10.1186/s12977-017-0382-1;
RA Chen C., Ma X., Hu Q., Li X., Huang F., Zhang J., Pan T., Xia J., Liu C.,
RA Zhang H.;
RT "Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G
RT through interference with the Vif-mediated ubiquitin-proteasome pathway.";
RL Retrovirology 14:56-56(2017).
RN [28]
RP FUNCTION, AND MUTAGENESIS OF LYS-530 AND GLU-646.
RX PubMed=31722967; DOI=10.1074/jbc.ra119.009435;
RA Liu T., Sun Q., Liu Y., Cen S., Zhang Q.;
RT "The MOV10 helicase restricts hepatitis B virus replication by inhibiting
RT viral reverse transcription.";
RL J. Biol. Chem. 294:19804-19813(2019).
RN [29]
RP FUNCTION, INDUCTION BY HERPES SIMPLEX VIRUS 1 LYTIC INFECTION, AND
RP INTERACTION WITH IKBKE.
RX PubMed=35157734; DOI=10.1371/journal.ppat.1010301;
RA Yang X., Xiang Z., Sun Z., Ji F., Ren K., Pan D.;
RT "Host MOV10 is induced to restrict herpes simplex virus 1 lytic infection
RT by promoting type I interferon response.";
RL PLoS Pathog. 18:e1010301-e1010301(2022).
CC -!- FUNCTION: 5' to 3' RNA helicase that is involved in a number of
CC cellular roles ranging from mRNA metabolism and translation, modulation
CC of viral infectivity, inhibition of retrotransposition, or regulation
CC of synaptic transmission (PubMed:23093941). Plays an important role in
CC innate antiviral immunity by promoting type I interferon production
CC (PubMed:27016603, PubMed:35157734, PubMed:27974568). Mechanistically,
CC specifically uses IKKepsilon/IKBKE as the mediator kinase for IRF3
CC activation (PubMed:27016603, PubMed:35157734). Blocks HIV-1 virus
CC replication at a post-entry step (PubMed:20215113). Counteracts HIV-1
CC Vif-mediated degradation of APOBEC3G through its helicase activity by
CC interfering with the ubiquitin-proteasome pathway (PubMed:29258557).
CC Inhibits also hepatitis B virus/HBV replication by interacting with HBV
CC RNA and thereby inhibiting the early step of viral reverse
CC transcription (PubMed:31722967). Contributes to UPF1 mRNA target
CC degradation by translocation along 3' UTRs (PubMed:24726324). Required
CC for microRNA (miRNA)-mediated gene silencing by the RNA-induced
CC silencing complex (RISC). Required for both miRNA-mediated
CC translational repression and miRNA-mediated cleavage of complementary
CC mRNAs by RISC (PubMed:16289642, PubMed:17507929, PubMed:22791714). In
CC cooperation with FMR1, regulates miRNA-mediated translational
CC repression by AGO2 (PubMed:25464849). Restricts retrotransposition of
CC long interspersed element-1 (LINE-1) in cooperation with TUT4 and TUT7
CC counteracting the RNA chaperonne activity of L1RE1 (PubMed:30122351,
CC PubMed:23093941). Facilitates LINE-1 uridylation by TUT4 and TUT7
CC (PubMed:30122351). Required for embryonic viability and for normal
CC central nervous system development and function. Plays two critical
CC roles in early brain development: suppresses retroelements in the
CC nucleus by directly inhibiting cDNA synthesis, while regulates
CC cytoskeletal mRNAs to influence neurite outgrowth in the cytosol (By
CC similarity). May function as a messenger ribonucleoprotein (mRNP)
CC clearance factor (PubMed:24726324). {ECO:0000250|UniProtKB:P23249,
CC ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:17507929,
CC ECO:0000269|PubMed:20215113, ECO:0000269|PubMed:22791714,
CC ECO:0000269|PubMed:23093941, ECO:0000269|PubMed:24726324,
CC ECO:0000269|PubMed:25464849, ECO:0000269|PubMed:27016603,
CC ECO:0000269|PubMed:27974568, ECO:0000269|PubMed:29258557,
CC ECO:0000269|PubMed:30122351, ECO:0000269|PubMed:31722967,
CC ECO:0000269|PubMed:35157734}.
CC -!- FUNCTION: (Microbial infection) Required for RNA-directed transcription
CC and replication of the human hepatitis delta virus (HDV). Interacts
CC with small capped HDV RNAs derived from genomic hairpin structures that
CC mark the initiation sites of RNA-dependent HDV RNA transcription.
CC {ECO:0000269|PubMed:18552826}.
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:24726324};
CC -!- SUBUNIT: Interacts with DICER1, AGO2, TARBP2, EIF6 and RPL7A (60S
CC ribosome subunit); they form a large RNA-induced silencing complex
CC (RISC) (PubMed:17507929). Interacts with APOBEC3G in an RNA-dependent
CC manner. Interacts with TRIM71 (via NHL repeats) in an RNA-dependent
CC manner (PubMed:23125361). Interacts with both protein products of
CC LIRE1, ORF1p and ORF2p (PubMed:23093941). Interacts with TUT4 and, to a
CC lesser extent, TUT7; the interactions are RNA-dependent
CC (PubMed:30122351). Interacts with AGO2, TNRC6B and UPF1; the
CC interactions are direct and RNA-dependent (PubMed:24726324). Interacts
CC with FMR1; this interaction is direct, occurs in an RNA-dependent
CC manner on polysomes and induces association of MOV10 with RNAs
CC (PubMed:25464849). Interacts with SHFL; the interaction increases in
CC presence of RNA (PubMed:27974568). Interacts with DHX34; the
CC interaction is RNA-independent (PubMed:25220460). Interacts with IKBKE
CC (PubMed:27016603, PubMed:35157734). {ECO:0000269|PubMed:16289642,
CC ECO:0000269|PubMed:17507929, ECO:0000269|PubMed:22791714,
CC ECO:0000269|PubMed:23093941, ECO:0000269|PubMed:23125361,
CC ECO:0000269|PubMed:24726324, ECO:0000269|PubMed:25220460,
CC ECO:0000269|PubMed:25464849, ECO:0000269|PubMed:27016603,
CC ECO:0000269|PubMed:27974568, ECO:0000269|PubMed:30122351,
CC ECO:0000269|PubMed:35157734}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the human hepatitis delta
CC virus (HDV) antigen HDAg. {ECO:0000269|PubMed:18552826}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 protein GAG.
CC {ECO:0000269|PubMed:20215113}.
CC -!- INTERACTION:
CC Q9HCE1; P35226: BMI1; NbExp=4; IntAct=EBI-1055820, EBI-2341576;
CC Q9HCE1; O95503: CBX6; NbExp=2; IntAct=EBI-1055820, EBI-3951758;
CC Q9HCE1; O95931: CBX7; NbExp=5; IntAct=EBI-1055820, EBI-3923843;
CC Q9HCE1; Q9HC52: CBX8; NbExp=5; IntAct=EBI-1055820, EBI-712912;
CC Q9HCE1; P19525: EIF2AK2; NbExp=3; IntAct=EBI-1055820, EBI-640775;
CC Q9HCE1; P35227: PCGF2; NbExp=2; IntAct=EBI-1055820, EBI-2129767;
CC Q9HCE1; Q01085: TIAL1; NbExp=2; IntAct=EBI-1055820, EBI-2820828;
CC Q9HCE1; Q8VDS3: Cbx7; Xeno; NbExp=4; IntAct=EBI-1055820, EBI-1216533;
CC Q9HCE1; P0DTC9: N; Xeno; NbExp=5; IntAct=EBI-1055820, EBI-25475856;
CC Q9HCE1; P0C6L3; Xeno; NbExp=2; IntAct=EBI-1055820, EBI-15709810;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16289642,
CC ECO:0000269|PubMed:24726324, ECO:0000269|PubMed:27974568,
CC ECO:0000269|PubMed:30122351}. Cytoplasm, Cytoplasmic ribonucleoprotein
CC granule {ECO:0000269|PubMed:30122351}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:23093941}. Nucleus {ECO:0000250|UniProtKB:P23249}.
CC Cytoplasm {ECO:0000250|UniProtKB:P23249}. Note=Co-enriched in
CC cytoplasmic foci with TUT4 (PubMed:30122351). In developing neurons,
CC localizes both in nucleus and cytoplasm, but in the adulthood it is
CC only cytoplasmic (By similarity). After infection, relocalizes to the
CC DENV replication complex in perinuclear regions (PubMed:27974568).
CC {ECO:0000250|UniProtKB:P23249, ECO:0000269|PubMed:27974568,
CC ECO:0000269|PubMed:30122351}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HCE1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCE1-2; Sequence=VSP_010943, VSP_010944;
CC Name=3;
CC IsoId=Q9HCE1-3; Sequence=VSP_037305, VSP_037306;
CC -!- INDUCTION: By herpes simplex 1/HHV-1 virus infection.
CC {ECO:0000269|PubMed:35157734}.
CC -!- PTM: (Microbial infection) Cleaved and targeted for degradation by
CC picornavirus proteases. {ECO:0000269|PubMed:27016603}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13457.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAB85000.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB046851; BAB13457.1; ALT_SEQ; mRNA.
DR EMBL; AK074174; BAB85000.1; ALT_INIT; mRNA.
DR EMBL; AL833353; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL603832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002548; AAH02548.1; -; mRNA.
DR EMBL; BC004499; AAH04499.2; -; mRNA.
DR EMBL; BC009312; AAH09312.1; -; mRNA.
DR CCDS; CCDS853.1; -. [Q9HCE1-1]
DR RefSeq; NP_001123551.1; NM_001130079.2. [Q9HCE1-1]
DR RefSeq; NP_001273001.1; NM_001286072.1.
DR RefSeq; NP_001308253.1; NM_001321324.1. [Q9HCE1-1]
DR RefSeq; NP_066014.1; NM_020963.4. [Q9HCE1-1]
DR RefSeq; XP_005270926.1; XM_005270869.4.
DR RefSeq; XP_005270927.1; XM_005270870.4.
DR RefSeq; XP_016856807.1; XM_017001318.1.
DR AlphaFoldDB; Q9HCE1; -.
DR SMR; Q9HCE1; -.
DR BioGRID; 110484; 1254.
DR CORUM; Q9HCE1; -.
DR DIP; DIP-44158N; -.
DR IntAct; Q9HCE1; 131.
DR MINT; Q9HCE1; -.
DR STRING; 9606.ENSP00000399797; -.
DR CarbonylDB; Q9HCE1; -.
DR GlyGen; Q9HCE1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HCE1; -.
DR MetOSite; Q9HCE1; -.
DR PhosphoSitePlus; Q9HCE1; -.
DR SwissPalm; Q9HCE1; -.
DR BioMuta; MOV10; -.
DR DMDM; 24638063; -.
DR EPD; Q9HCE1; -.
DR jPOST; Q9HCE1; -.
DR MassIVE; Q9HCE1; -.
DR MaxQB; Q9HCE1; -.
DR PaxDb; Q9HCE1; -.
DR PeptideAtlas; Q9HCE1; -.
DR PRIDE; Q9HCE1; -.
DR ProteomicsDB; 81683; -. [Q9HCE1-1]
DR ProteomicsDB; 81684; -. [Q9HCE1-2]
DR ProteomicsDB; 81685; -. [Q9HCE1-3]
DR Antibodypedia; 20136; 176 antibodies from 25 providers.
DR DNASU; 4343; -.
DR Ensembl; ENST00000357443.2; ENSP00000350028.2; ENSG00000155363.19. [Q9HCE1-1]
DR Ensembl; ENST00000369645.6; ENSP00000358659.1; ENSG00000155363.19. [Q9HCE1-1]
DR Ensembl; ENST00000413052.6; ENSP00000399797.2; ENSG00000155363.19. [Q9HCE1-1]
DR GeneID; 4343; -.
DR KEGG; hsa:4343; -.
DR MANE-Select; ENST00000369645.6; ENSP00000358659.1; NM_001321324.2; NP_001308253.1.
DR UCSC; uc001ecn.5; human. [Q9HCE1-1]
DR CTD; 4343; -.
DR DisGeNET; 4343; -.
DR GeneCards; MOV10; -.
DR HGNC; HGNC:7200; MOV10.
DR HPA; ENSG00000155363; Low tissue specificity.
DR MIM; 610742; gene.
DR neXtProt; NX_Q9HCE1; -.
DR OpenTargets; ENSG00000155363; -.
DR PharmGKB; PA30908; -.
DR VEuPathDB; HostDB:ENSG00000155363; -.
DR eggNOG; KOG1804; Eukaryota.
DR GeneTree; ENSGT00940000156024; -.
DR InParanoid; Q9HCE1; -.
DR OMA; RPYQGFI; -.
DR OrthoDB; 286011at2759; -.
DR PhylomeDB; Q9HCE1; -.
DR TreeFam; TF323999; -.
DR PathwayCommons; Q9HCE1; -.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8943723; Regulation of PTEN mRNA translation.
DR Reactome; R-HSA-8948700; Competing endogenous RNAs (ceRNAs) regulate PTEN translation.
DR Reactome; R-HSA-8986944; Transcriptional Regulation by MECP2.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; Q9HCE1; -.
DR SIGNOR; Q9HCE1; -.
DR BioGRID-ORCS; 4343; 15 hits in 1090 CRISPR screens.
DR ChiTaRS; MOV10; human.
DR GeneWiki; MOV10; -.
DR GenomeRNAi; 4343; -.
DR Pharos; Q9HCE1; Tbio.
DR PRO; PR:Q9HCE1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9HCE1; protein.
DR Bgee; ENSG00000155363; Expressed in right testis and 160 other tissues.
DR ExpressionAtlas; Q9HCE1; baseline and differential.
DR Genevisible; Q9HCE1; HS.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0032574; F:5'-3' 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:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IMP:UniProtKB.
DR GO; GO:0035279; P:miRNA-mediated gene silencing by mRNA destabilization; IDA:UniProtKB.
DR GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; IDA:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0150011; P:regulation of neuron projection arborization; ISS:UniProtKB.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR026122; MOV-10.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR PANTHER; PTHR10887:SF322; PTHR10887:SF322; 1.
DR Pfam; PF13087; AAA_12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Helicase;
KW Host-virus interaction; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Transcription; Transcription regulation.
FT CHAIN 1..1003
FT /note="Helicase MOV-10"
FT /id="PRO_0000080704"
FT REGION 921..965
FT /note="Interaction with AGO2 and APOBEC3G"
FT /evidence="ECO:0000269|PubMed:22791714"
FT REGION 966..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 645..648
FT /note="DEAG box"
FT BINDING 524..531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 47..56
FT /note="FGTPAPGFSS -> LASSKSILQS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_037305"
FT VAR_SEQ 57..1003
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_037306"
FT VAR_SEQ 838..900
FT /note="EKIRYCITKLDRELRGLDDIKDLKVGSVEEFQGQERSVILISTVRSSQSFVQ
FT LDLDFNLGFLK -> RSSVTSKGGAPPPDGTSLISRPLGRGSRSLGLCWLRISEEHQGQ
FT LPPPFVPQLPGLLPGSLLH (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010943"
FT VAR_SEQ 901..1003
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010944"
FT MUTAGEN 129
FT /note="Q->A: About 70% more antiviral activity against
FT encephalomyocarditis virus replication; when associated
FT with A-869."
FT /evidence="ECO:0000269|PubMed:27016603"
FT MUTAGEN 530
FT /note="K->A: Abolishes 5' to 3' directional unwinding
FT activity. Abolishes inhibition of RNA chaperonne activity
FT of LIRE1. No effect on interaction with UPF1."
FT /evidence="ECO:0000269|PubMed:24726324,
FT ECO:0000269|PubMed:30122351"
FT MUTAGEN 530
FT /note="K->R: Attenuated anti-HBV activity."
FT /evidence="ECO:0000269|PubMed:31722967"
FT MUTAGEN 645
FT /note="D->N: Abolishes 5' to 3' directional unwinding
FT activity."
FT /evidence="ECO:0000269|PubMed:24726324"
FT MUTAGEN 646
FT /note="E->Q: Almost complete lost of the ability to prevent
FT the degradation of APOBEC3G mediated by HIV-1 Vif.
FT Attenuated anti-HBV activity."
FT /evidence="ECO:0000269|PubMed:29258557,
FT ECO:0000269|PubMed:31722967"
FT MUTAGEN 869
FT /note="Q->A: About 70% more antiviral activity against
FT encephalomyocarditis virus replication; when associated
FT with A-129."
FT /evidence="ECO:0000269|PubMed:27016603"
FT CONFLICT 98
FT /note="D -> N (in Ref. 4; AL833353)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="A -> T (in Ref. 4; AL833353)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="S -> T (in Ref. 4; AL833353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1003 AA; 113671 MW; 28A8B3BF9B5B54FC CRC64;
MPSKFSCRQL REAGQCFESF LVVRGLDMET DRERLRTIYN RDFKISFGTP APGFSSMLYG
MKIANLAYVT KTRVRFFRLD RWADVRFPEK RRMKLGSDIS KHHKSLLAKI FYDRAEYLHG
KHGVDVEVQG PHEARDGQLL IRLDLNRKEV LTLRLRNGGT QSVTLTHLFP LCRTPQFAFY
NEDQELPCPL GPGECYELHV HCKTSFVGYF PATVLWELLG PGESGSEGAG TFYIARFLAA
VAHSPLAAQL KPMTPFKRTR ITGNPVVTNR IEEGERPDRA KGYDLELSMA LGTYYPPPRL
RQLLPMLLQG TSIFTAPKEI AEIKAQLETA LKWRNYEVKL RLLLHLEELQ MEHDIRHYDL
ESVPMTWDPV DQNPRLLTLE VPGVTESRPS VLRGDHLFAL LSSETHQEDP ITYKGFVHKV
ELDRVKLSFS MSLLSRFVDG LTFKVNFTFN RQPLRVQHRA LELTGRWLLW PMLFPVAPRD
VPLLPSDVKL KLYDRSLESN PEQLQAMRHI VTGTTRPAPY IIFGPPGTGK TVTLVEAIKQ
VVKHLPKAHI LACAPSNSGA DLLCQRLRVH LPSSIYRLLA PSRDIRMVPE DIKPCCNWDA
KKGEYVFPAK KKLQEYRVLI TTLITAGRLV SAQFPIDHFT HIFIDEAGHC MEPESLVAIA
GLMEVKETGD PGGQLVLAGD PRQLGPVLRS PLTQKHGLGY SLLERLLTYN SLYKKGPDGY
DPQFITKLLR NYRSHPTILD IPNQLYYEGE LQACADVVDR ERFCRWAGLP RQGFPIIFHG
VMGKDEREGN SPSFFNPEEA ATVTSYLKLL LAPSSKKGKA RLSPRSVGVI SPYRKQVEKI
RYCITKLDRE LRGLDDIKDL KVGSVEEFQG QERSVILIST VRSSQSFVQL DLDFNLGFLK
NPKRFNVAVT RAKALLIIVG NPLLLGHDPD WKVFLEFCKE NGGYTGCPFP AKLDLQQGQN
LLQGLSKLSP STSGPHSHDY LPQEREGEGG LSLQVEPEWR NEL
