ID   MOV10_BOVIN             Reviewed;        1003 AA.
AC   Q0V8H6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Putative helicase MOV-10;
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9HCE1};
GN   Name=MOV10;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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. Plays an important role in innate antiviral
CC       immunity by promoting type I interferon production. Mechanistically,
CC       specifically uses IKKepsilon/IKBKE as the mediator kinase for IRF3
CC       activation. Contributes to UPF1 mRNA target degradation by
CC       translocation along 3' UTRs. Required for microRNA (miRNA)-mediated
CC       gene silencing by the RNA-induced silencing complex (RISC). Required
CC       for both miRNA-mediated translational repression and miRNA-mediated
CC       cleavage of complementary mRNAs by RISC. In cooperation with FMR1,
CC       regulates miRNA-mediated translational repression by AGO2. Restricts
CC       retrotransposition of long interspersed element-1 (LINE-1) in
CC       cooperation with TUT4 and TUT7 counteracting the RNA chaperonne
CC       activity of L1RE1. Facilitates LINE-1 uridylation by TUT4 and TUT7 (By
CC       similarity). Required for embryonic viability and for normal central
CC       nervous system development and function. Plays two critical roles in
CC       early brain development: suppresses retroelements in the nucleus by
CC       directly inhibiting cDNA synthesis, while regulates cytoskeletal mRNAs
CC       to influence neurite outgrowth in the cytosol (By similarity). May
CC       function as a messenger ribonucleoprotein (mRNP) clearance factor (By
CC       similarity). {ECO:0000250|UniProtKB:P23249,
CC       ECO:0000250|UniProtKB:Q9HCE1}.
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:Q9HCE1};
CC   -!- SUBUNIT: Interacts with DICER1, AGO2, TARBP2, EIF6 and RPL7A (60S
CC       ribosome subunit); they form a large RNA-induced silencing complex
CC       (RISC). Interacts with APOBEC3G in an RNA-dependent manner. Interacts
CC       with TRIM71 (via NHL repeats) in an RNA-dependent manner. Interacts
CC       with both protein products of LIRE1, ORF1p and ORF2p. Interacts with
CC       TUT4 and, to a lesser extent, TUT7; the interactions are RNA-dependent.
CC       Interacts with AGO2, TNRC6B and UPF1; the interactions are direct and
CC       RNA-dependent. Interacts with FMR1; this interaction is direct, occurs
CC       in an RNA-dependent manner on polysomes and induces association of
CC       MOV10 with RNAs. Interacts with SHFL; the interaction increases in
CC       presence of RNA (By similarity). Interacts with DHX34; the interaction
CC       is-RNA independent (By similarity). Interacts with RBM46 (By
CC       similarity). {ECO:0000250|UniProtKB:P23249,
CC       ECO:0000250|UniProtKB:Q9HCE1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9HCE1}.
CC       Cytoplasm, Cytoplasmic ribonucleoprotein granule
CC       {ECO:0000250|UniProtKB:Q9HCE1}. Cytoplasm, Stress granule
CC       {ECO:0000250|UniProtKB:Q9HCE1}. Nucleus {ECO:0000250|UniProtKB:P23249}.
CC       Cytoplasm {ECO:0000250|UniProtKB:P23249}. Note=Co-enriched in
CC       cytoplasmic foci with TUT4 (By similarity). In developing neurons,
CC       localizes both in nucleus and cytoplasm, but in the adulthood it is
CC       only cytoplasmic (By similarity). {ECO:0000250|UniProtKB:P23249,
CC       ECO:0000250|UniProtKB:Q9HCE1}.
CC   -!- PTM: Ubiquitinated by the DCX(DCAF12) complex that specifically
CC       recognizes the glutamate-leucine (Glu-Leu) degron at the C-terminus,
CC       leading to its degradation. {ECO:0000250|UniProtKB:Q9HCE1}.
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BT026242; ABG67081.1; -; mRNA.
DR   EMBL; BC148151; AAI48152.1; -; mRNA.
DR   RefSeq; NP_001069307.1; NM_001075839.1.
DR   AlphaFoldDB; Q0V8H6; -.
DR   SMR; Q0V8H6; -.
DR   STRING; 9913.ENSBTAP00000058600; -.
DR   PaxDb; 9913-ENSBTAP00000018997; -.
DR   PeptideAtlas; Q0V8H6; -.
DR   Ensembl; ENSBTAT00000018997.6; ENSBTAP00000018997.5; ENSBTAG00000014297.6.
DR   Ensembl; ENSBTAT00000072871.1; ENSBTAP00000058600.1; ENSBTAG00000014297.6.
DR   GeneID; 523206; -.
DR   KEGG; bta:523206; -.
DR   CTD; 4343; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014297; -.
DR   VGNC; VGNC:31566; MOV10.
DR   eggNOG; KOG1804; Eukaryota.
DR   GeneTree; ENSGT00940000156024; -.
DR   HOGENOM; CLU_001666_6_1_1; -.
DR   InParanoid; Q0V8H6; -.
DR   OMA; NDWDQDQ; -.
DR   OrthoDB; 170190at2759; -.
DR   TreeFam; TF323999; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000014297; Expressed in diaphragm and 106 other cell types or tissues.
DR   ExpressionAtlas; Q0V8H6; baseline and differential.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS: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; ISS:UniProtKB.
DR   GO; GO:0032574; F:5'-3' 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:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR   GO; GO:0035279; P:miRNA-mediated gene silencing by mRNA destabilization; ISS:UniProtKB.
DR   GO; GO:0035195; P:miRNA-mediated post-transcriptional gene silencing; ISS:UniProtKB.
DR   GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0150011; P:regulation of neuron projection arborization; ISS:UniProtKB.
DR   GO; GO:0035194; P:regulatory ncRNA-mediated post-transcriptional gene silencing; IBA:GO_Central.
DR   GO; GO:0010526; P:retrotransposon silencing; ISS:UniProtKB.
DR   GO; GO:0141008; P:retrotransposon silencing by mRNA destabilization; ISS:UniProtKB.
DR   CDD; cd18038; DEXXQc_Helz-like; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR049080; MOV-10-like_beta-barrel.
DR   InterPro; IPR026122; MOV-10/SDE3_DEXXQ/H-box.
DR   InterPro; IPR049079; Mov-10_helical.
DR   InterPro; IPR049077; MOV-10_Ig-like.
DR   InterPro; IPR049075; MOV-10_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10887:SF537; HELICASE MOV-10; 1.
DR   Pfam; PF13086; AAA_11; 2.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF21634; MOV-10_beta-barrel; 1.
DR   Pfam; PF21635; Mov-10_helical; 1.
DR   Pfam; PF21633; MOV-10_Ig-like; 1.
DR   Pfam; PF21632; MOV-10_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; RNA-mediated gene silencing; Ubl conjugation.
FT   CHAIN           1..1003
FT                   /note="Putative helicase MOV-10"
FT                   /id="PRO_0000374666"
FT   REGION          921..965
FT                   /note="Interaction with AGO2 and APOBEC3G"
FT                   /evidence="ECO:0000250"
FT   REGION          968..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           645..648
FT                   /note="DEAG box"
FT   COMPBIAS        979..1003
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:Q9HCE1"
FT   MOD_RES         160
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCE1"
FT   MOD_RES         254
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCE1"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCE1"
FT   MOD_RES         969
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCE1"
FT   MOD_RES         977
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCE1"
SQ   SEQUENCE   1003 AA;  113885 MW;  EF25709C0B8F7959 CRC64;
     MPSKFSCRQL RETGQRFENF LVDRGQDRET DRERLRTIYN QDFKTSFGTP APGFSSMLYG
     MKIANLAYVT KTRVRFFGLD RWADVWFPEK RRMKPGLEMS KHHRSLLATI FHDRAEYMHG
     KHGVNVEVQG PHEARDGQLL IRLDLNRKEV LTLRLRNGGT QPVTLTHLFP FCRTPQFSFC
     NGDRELPCLL GPGECYELHV HCKTSFVGYF PATVLWELLG PGEPGSEGAG TFYIARFLAA
     VAHSPLAAQL KPTTPFKRTQ VSRNPVVTRR IEEGERPDRA KNYDLEFSLP LGTYYPPPRL
     RQLLPVLLRG TSIFTAPKEI AEIKAQLQTT LKWRNYEVKL RLLLHLEELQ MEHDIRHYDL
     ESVPMTWDPI DRNPRLLTLE VPGVAESRPS VLRGDHLFAL LSSETHHEDP VTYKGFVHKV
     ELDRVKLSFS TSLLSRFVDG LTFKVNFTFN RQPLRVQHRA LELTGRWPLE PMLFPVASRG
     VPLLPSDVKL KLYDRSLESN PEQLQAMKHI VMGTTRPAPY IIFGPPGTGK TVTLVEAIKQ
     VVKHLPKAHI LACAPSNSGA DLLCQRLRVH LPSSIYRLLA PSRDIHLVPE DIKPCCNWDA
     KKGDFVFPSK KKLQEYRVLI TTLITASRLV SAQFPIDHFT HIFIDEAGHA MEPESLVAIA
     GLMEVKEADN PGGQLVLAGD PRQLGPVLRC PLTQKHGLGY SLLERLLTFN ALYKKGPDGY
     NPQFITKLLR NYRSHPTILD VPNRLYYDGE LQACADVVDR ERFCRWEGLP RQDFPIIFHG
     VMGKDEREGN SPSFFNPEEA ATVTSYLKQL LAPSSKKGKA RLSPRSVGVI SPYRKQVEKI
     RYCITKLDKQ LRGLDDIKDL KVGSVEEFQG QERSVILIST VRSSQSFVQL DLDFNLGFLK
     NPKRFNVAVT RAKALLIVVG NPLLLGHDPD WKVFLEFCKE NGGYTGCPFP AKLDLQQGQN
     LLQGLSKLSP STSGLKSHDY LPQEREGEEG LSLQVEPEWR NEL
//