MOV10_MOUSE
ID MOV10_MOUSE Reviewed; 1004 AA.
AC P23249; Q9DC64;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Putative helicase MOV-10;
DE EC=3.6.4.13;
DE AltName: Full=Moloney leukemia virus 10 protein;
GN Name=Mov10; Synonyms=Gb110;
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].
RX PubMed=1899287; DOI=10.1128/mcb.11.2.886-893.1991;
RA Mooslehner K., Mueller U., Karls U., Hamann L., Harbers K.;
RT "Structure and expression of a gene encoding a putative GTP-binding protein
RT identified by provirus integration in a transgenic mouse strain.";
RL Mol. Cell. Biol. 11:886-893(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RC STRAIN=BALB/cJ;
RX PubMed=8065313; DOI=10.1128/mcb.14.9.5786-5793.1994;
RA Hamann L., Bayer K.-U., Jensen K., Harbers K.;
RT "Interaction of several related GC-box- and GT-box-binding proteins with
RT the intronic enhancer is required for differential expression of the gb110
RT gene in embryonal carcinoma cells.";
RL Mol. Cell. Biol. 14:5786-5793(1994).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Spleen, and 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).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP RNA-BINDING, MUTAGENESIS OF LYS-531, AND INTERACTION WITH LIRE1.
RX PubMed=28662698; DOI=10.1186/s12915-017-0387-1;
RA Skariah G., Seimetz J., Norsworthy M., Lannom M.C., Kenny P.J.,
RA Elrakhawy M., Forsthoefel C., Drnevich J., Kalsotra A., Ceman S.;
RT "Mov10 suppresses retroelements and regulates neuronal development and
RT function in the developing brain.";
RL BMC Biol. 15:54-54(2017).
CC -!- FUNCTION: Probable RNA helicase. Required for miRNA-mediated gene
CC silencing by the RNA-induced silencing complex (RISC). Required for
CC both miRNA-mediated translational repression and miRNA-mediated
CC cleavage of complementary mRNAs by RISC (By similarity). In cooperation
CC with FMR1, regulates miRNA-mediated translational repression by AGO2
CC (By similarity). Restricts retrotransposition of long interspersed
CC element-1 (LINE-1) in cooperation with TUT4 and TUT7 counteracting the
CC RNA chaperonne activity of L1RE1. Facilitates LINE-1 uridylation by
CC TUT4 and TUT7 (By similarity). Required for embryonic viability and for
CC normal central nervous system development and function. Plays two
CC critical roles in early brain development: suppresses retroelements in
CC the nucleus by directly inhibiting cDNA synthesis, while regulates
CC cytoskeletal mRNAs to influence neurite outgrowth in the cytosol
CC (PubMed:28662698). May function as a messenger ribonucleoprotein (mRNP)
CC clearance factor (By similarity). {ECO:0000250|UniProtKB:Q9HCE1,
CC ECO:0000269|PubMed:28662698}.
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
CC (PubMed:28662698) (By similarity). Interacts with both protein products
CC of LIRE1, ORF1p and ORF2p (PubMed:28662698). Interacts with TUT4 and,
CC to a lesser extent, TUT7; the interactions are RNA-dependent. Interacts
CC with AGO2, TNRC6B and UPF1; the interactions are direct and RNA-
CC dependent. Interacts with FMR1; this interaction is direct, occurs in
CC an RNA-dependent manner on polysomes and induces association of MOV10
CC with RNAs (By similarity). Interacts with SHFL; the interaction
CC increases in presence of RNA (By similarity). Interacts with DHX34; the
CC interaction is RNA-independent (By similarity).
CC {ECO:0000250|UniProtKB:Q9HCE1, ECO:0000269|PubMed:28662698}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9HCE1}.
CC Nucleus {ECO:0000269|PubMed:28662698}. Cytoplasm
CC {ECO:0000269|PubMed:28662698}. Cytoplasm, Cytoplasmic ribonucleoprotein
CC granule {ECO:0000250|UniProtKB:Q9HCE1}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q9HCE1}. Note=In young mouse (P2) neurons,
CC localizes both in nucleus and cytoplasm, but in the adulthood it is
CC only cytoplasmic (PubMed:28662698). Co-enriched in cytoplasmic foci
CC with TUT4 (By similarity). {ECO:0000250|UniProtKB:Q9HCE1,
CC ECO:0000269|PubMed:28662698}.
CC -!- DEVELOPMENTAL STAGE: As early as embryonic day 18, there is a higher
CC level of expression in the whole brain compared to adults. Expression
CC continues to rise at birth (P0) and remains elevated over adult levels
CC until P10-P14, when it begins to decline (PubMed:28662698). Highly
CC expressed throughout the P1 brain, including the cortex, hippocampus,
CC cerebellum, midbrain, and hindbrain, there is very little expression in
CC the adult brain except in the hippocampus (PubMed:28662698).
CC {ECO:0000269|PubMed:28662698}.
CC -!- DISRUPTION PHENOTYPE: Knockout leads to early embryonic lethality.
CC {ECO:0000269|PubMed:28662698}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
CC {ECO:0000305}.
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DR EMBL; X52574; CAA36803.1; -; mRNA.
DR EMBL; AK004542; BAB23358.1; -; mRNA.
DR EMBL; BC053743; AAH53743.1; -; mRNA.
DR EMBL; X75819; CAA53453.1; -; Genomic_DNA.
DR CCDS; CCDS38579.1; -.
DR PIR; A39611; A39611.
DR RefSeq; NP_001156912.1; NM_001163440.1.
DR RefSeq; NP_001156913.1; NM_001163441.1.
DR RefSeq; NP_032645.2; NM_008619.2.
DR RefSeq; XP_006501163.1; XM_006501100.1.
DR RefSeq; XP_006501164.1; XM_006501101.3.
DR AlphaFoldDB; P23249; -.
DR SMR; P23249; -.
DR BioGRID; 201471; 30.
DR DIP; DIP-48575N; -.
DR IntAct; P23249; 4.
DR MINT; P23249; -.
DR STRING; 10090.ENSMUSP00000126897; -.
DR iPTMnet; P23249; -.
DR PhosphoSitePlus; P23249; -.
DR EPD; P23249; -.
DR jPOST; P23249; -.
DR MaxQB; P23249; -.
DR PaxDb; P23249; -.
DR PRIDE; P23249; -.
DR ProteomicsDB; 295652; -.
DR Antibodypedia; 20136; 176 antibodies from 25 providers.
DR DNASU; 17454; -.
DR Ensembl; ENSMUST00000168015; ENSMUSP00000128246; ENSMUSG00000002227.
DR GeneID; 17454; -.
DR KEGG; mmu:17454; -.
DR UCSC; uc008qum.3; mouse.
DR CTD; 4343; -.
DR MGI; MGI:97054; Mov10.
DR VEuPathDB; HostDB:ENSMUSG00000002227; -.
DR eggNOG; KOG1804; Eukaryota.
DR GeneTree; ENSGT00940000156024; -.
DR InParanoid; P23249; -.
DR OrthoDB; 286011at2759; -.
DR BioGRID-ORCS; 17454; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Mov10; mouse.
DR PRO; PR:P23249; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P23249; protein.
DR Bgee; ENSMUSG00000002227; Expressed in granulocyte and 166 other tissues.
DR ExpressionAtlas; P23249; baseline and differential.
DR Genevisible; P23249; MM.
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; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA: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; ISO:MGI.
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; IMP: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; IMP: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; IPR041677; DNA2/NAM7_AAA_11.
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; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein 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..1004
FT /note="Putative helicase MOV-10"
FT /id="PRO_0000080705"
FT REGION 922..966
FT /note="Interaction with AGO2 and APOBEC3G"
FT /evidence="ECO:0000250"
FT REGION 966..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 646..649
FT /note="DEAG box"
FT BINDING 525..532
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 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE1"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE1"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE1"
FT MUTAGEN 531
FT /note="K->A: Abolishes inhibition of retrotransposition."
FT /evidence="ECO:0000269|PubMed:28662698"
FT CONFLICT 142
FT /note="H -> R (in Ref. 1; CAA36803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1004 AA; 113583 MW; 8B2522AAB35B6F2B CRC64;
MPSKFSCRKL RETGQRFESF LAERGLDLET DRERLRTIYN HDFKPSYGTP APGFSSMLYG
MKIANLAFVT KTRVRFFKLD RWADVQLPEK RRIKPGSNIS KQHRSLLARI FHDRAEYLHG
KHGVDVEVQG PHEARDGQLL IHLDLNRKEV LTLRLRNGGS KPVTLTHLFP LCWTPQFVFY
HGEQDLPCPL GPGESYELHI YCKTSIVGYF PATVLWELLG PGESGAEGAE TFYIARFLAA
VAHSPLAAQL KPTTPFKRPP RLTRNSVLTN RIEEGERPDR AKGYELELSL ALGTYYPPIL
LRQLLPTLLQ GPSIFTAPKE VAEIKAQLET TLKSRNYEVK LRLLLHLEEL QMEHDIRHYD
LDSVPMTWDP VDQNPRLLTL EVPGVAESRP SVLRGDHLFA LLSSETQQDD PVTYKGFVHK
VELDRVKLSF STSLLSRFVD GLTFKVNFTF NRQPLRVQHR ALELTGRWVL WPMLFPVASR
GVSLLPSDVK FKLYDRSLES NPEQLQAMKH IVRGTTRPAP YIIFGPPGTG KTVTLVEAIK
QVVKHLPKAH ILACAPSNSG ADLLCQRLRV HLPSSIYRLL APSRDIRMVP EDIKTCCNWD
AKKGEYVYPA KKHLQQYRVL ITTLITASRL VSAQFPIDHF THIFIDEAGH CMEPESLVAI
AGLMDVKETG NPGGQLVLAG DPRQLGPVLR SPLALKHGLG YSLLERLLAY NSLYKKGPNG
YDPQFITKLL RNYRSHPTIL DIPNQLYYDG ELQACADVVD RERFCRWEGL PQQGFPIIFH
GVMGKDEREG NSPSFFNPEE AATVTSYLKQ LLAPSSKKGK ARLSPRNVGV ISPYRKQVEK
IRYCITKLDR ELRGLDDIKD LKVGSVEEFQ GQERSVILIS TVRSSQSFVQ LDLDFNLGFL
KNPKRFNVAV TRAKALLIVV GNPLLLGHDP DWKTFLEFCK ENGGYTGCPF PAKLDLQQGQ
DLLQGLSKLS PSTSGPRRHQ NLPQEREGEG GLPLQVEPEW RNEL
