MOV10_BOVIN
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 03-AUG-2022, entry version 98.
DE RecName: Full=Putative helicase MOV-10;
DE EC=3.6.4.13;
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 contributing to UPF1 mRNA target
CC degradation by translocation along 3' UTRs. Required for microRNA
CC (miRNA)-mediated gene silencing by the RNA-induced silencing complex
CC (RISC). Required for both miRNA-mediated translational repression and
CC miRNA-mediated cleavage of complementary mRNAs by RISC. In cooperation
CC with FMR1, regulates miRNA-mediated translational repression by AGO2.
CC Restricts 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 -!- 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). {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 -!- 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.ENSBTAP00000018997; -.
DR PaxDb; Q0V8H6; -.
DR PeptideAtlas; Q0V8H6; -.
DR PRIDE; Q0V8H6; -.
DR Ensembl; ENSBTAT00000018997; ENSBTAP00000018997; ENSBTAG00000014297.
DR Ensembl; ENSBTAT00000072871; ENSBTAP00000058600; ENSBTAG00000014297.
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; RPYQGFI; -.
DR OrthoDB; 286011at2759; -.
DR TreeFam; TF323999; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000014297; Expressed in diaphragm and 106 other 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:0035195; P:miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0035279; P:miRNA-mediated gene silencing by mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS: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 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.
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
