ARMI_DROME
ID ARMI_DROME Reviewed; 1188 AA.
AC Q6J5K9; Q59E56; Q9VZP4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable RNA helicase armi;
DE EC=3.6.4.13;
DE AltName: Full=Protein armitage;
GN Name=armi; ORFNames=CG11513;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=15035984; DOI=10.1016/s0092-8674(04)00250-8;
RA Cook H.A., Koppetsch B.S., Wu J., Theurkauf W.E.;
RT "The Drosophila SDE3 homolog armitage is required for oskar mRNA silencing
RT and embryonic axis specification.";
RL Cell 116:817-829(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP FUNCTION.
RX PubMed=15035985; DOI=10.1016/s0092-8674(04)00218-1;
RA Tomari Y., Du T., Haley B., Schwarz D.S., Bennett R., Cook H.A.,
RA Koppetsch B.S., Theurkauf W.E., Zamore P.D.;
RT "RISC assembly defects in the Drosophila RNAi mutant armitage.";
RL Cell 116:831-841(2004).
RN [5]
RP FUNCTION, INTERACTION WITH PIWI AND FS(Y)YB, AND SUBCELLULAR LOCATION.
RX PubMed=20966047; DOI=10.1101/gad.1989510;
RA Saito K., Ishizu H., Komai M., Kotani H., Kawamura Y., Nishida K.M.,
RA Siomi H., Siomi M.C.;
RT "Roles for the Yb body components Armitage and Yb in primary piRNA
RT biogenesis in Drosophila.";
RL Genes Dev. 24:2493-2498(2010).
CC -!- FUNCTION: Probable RNA helicase required for axial polarization of the
CC oocyte during early and mid oogenesis. Plays a central role in RNA
CC interference (RNAi) process, a process that mediates mRNA destruction
CC of translational repression. Required for the assembly of the RISC
CC complex, a complex required for target RNA destruction or repression.
CC May be required in the RISC assembly to unwind miRNAs, in the
CC production of single-stranded miRNA from the double-stranded miRNA, a
CC key step in RISC formation. Required both for the translational control
CC of oskar (osk) mRNA and cytoskeletal polarization in the oocyte.
CC Required for somatic primary piRNA biogenesis.
CC {ECO:0000269|PubMed:15035984, ECO:0000269|PubMed:15035985,
CC ECO:0000269|PubMed:20966047}.
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: Forms a complex with piwi and fs(1)Yb; this interaction is
CC required for proper piRNA loading and nuclear localization of piwi. The
CC interaction of piwi and fs(1)Yb is likely to occur via armi.
CC -!- INTERACTION:
CC Q6J5K9; Q9W4W2: fs(1)Yb; NbExp=4; IntAct=EBI-2890374, EBI-3424083;
CC Q6J5K9; Q9VKM1: piwi; NbExp=4; IntAct=EBI-2890374, EBI-3406276;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15035984,
CC ECO:0000269|PubMed:20966047}. Note=Component of Yb bodies, an electron
CC dense structure containing Yb protein found in somatic cells of ovary
CC and testis.
CC -!- TISSUE SPECIFICITY: Abundant in oocytes and syncytial blastoderm.
CC Expressed at low level throughout development, including somatic
CC tissues. First apparent early in oogenesis, in the cytoplasm of stem
CC cells and mitotically dividing cystoblasts. In regions 2a and 2b of the
CC germarium, it is most concentrated in the center of the germline cysts,
CC where the pro-oocyte is located. In stage 1 and early stage 2 egg
CC chambers, it accumulates at the anterior of the oocyte, near the ring
CC canals. It also extends through the ring canals forming a branched
CC structure that links the early oocyte with adjacent nurse cells. In
CC stage 3 cysts, it accumulates at the posterior cortex and localizes to
CC extensions that pass through the oocyte into the nurse cells. Through
CC stages 4 to 7, it continues to be somewhat enriched at the posterior
CC cortex of the oocyte, but at significantly lower level. In stage 9 to
CC 10 egg chambers, it is found throughout the cytoplasm of the oocyte and
CC nurse cells, with slight enrichment at the oocyte cortex.
CC {ECO:0000269|PubMed:15035984}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY598469; AAT12000.1; -; mRNA.
DR EMBL; AE014296; AAF47775.2; -; Genomic_DNA.
DR EMBL; AE014296; AAX52729.1; -; Genomic_DNA.
DR RefSeq; NP_001014556.1; NM_001014556.3.
DR RefSeq; NP_647816.2; NM_139559.4.
DR AlphaFoldDB; Q6J5K9; -.
DR SMR; Q6J5K9; -.
DR BioGRID; 63920; 16.
DR IntAct; Q6J5K9; 7.
DR MINT; Q6J5K9; -.
DR STRING; 7227.FBpp0100102; -.
DR PaxDb; Q6J5K9; -.
DR EnsemblMetazoa; FBtr0100641; FBpp0100102; FBgn0041164.
DR EnsemblMetazoa; FBtr0309841; FBpp0301575; FBgn0041164.
DR GeneID; 38427; -.
DR KEGG; dme:Dmel_CG11513; -.
DR UCSC; CG11513-RA; d. melanogaster.
DR CTD; 38427; -.
DR FlyBase; FBgn0041164; armi.
DR VEuPathDB; VectorBase:FBgn0041164; -.
DR eggNOG; KOG1804; Eukaryota.
DR GeneTree; ENSGT00940000165903; -.
DR InParanoid; Q6J5K9; -.
DR OrthoDB; 286011at2759; -.
DR PhylomeDB; Q6J5K9; -.
DR BioGRID-ORCS; 38427; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38427; -.
DR PRO; PR:Q6J5K9; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0041164; Expressed in egg chamber and 20 other tissues.
DR ExpressionAtlas; Q6J5K9; differential.
DR Genevisible; Q6J5K9; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IDA:FlyBase.
DR GO; GO:0070725; C:Yb body; IDA:FlyBase.
DR GO; GO:0032574; F:5'-3' RNA helicase activity; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0034584; F:piRNA binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IMP:FlyBase.
DR GO; GO:0003724; F:RNA helicase activity; NAS:UniProtKB.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0000578; P:embryonic axis specification; IMP:UniProtKB.
DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0031023; P:microtubule organizing center organization; IMP:FlyBase.
DR GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IGI:FlyBase.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:1990511; P:piRNA biosynthetic process; IMP:FlyBase.
DR GO; GO:0007318; P:pole plasm protein localization; IMP:FlyBase.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0070922; P:RISC complex assembly; IMP:UniProtKB.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 3.
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:SF419; PTHR10887:SF419; 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 ATP-binding; Cytoplasm; Developmental protein; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..1188
FT /note="Probable RNA helicase armi"
FT /id="PRO_0000080708"
FT MOTIF 862..865
FT /note="DEAG box"
FT BINDING 723..730
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 522
FT /note="T -> K (in Ref. 1; AAT12000)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="I -> V (in Ref. 1; AAT12000)"
FT /evidence="ECO:0000305"
FT CONFLICT 905
FT /note="S -> L (in Ref. 1; AAT12000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1188 AA; 135658 MW; BA1D8F4305825B0A CRC64;
MFTYVSKFFT NPDRNREDIL ESLDRENSFL DQKLMEEKMD QQLKANPNEI NGVLSNKIAE
LTHGLSEMDV SKESSCTARK GVITSLDGDR GVIDKDVLFE TKVAEDIILD LHVGCVVEYL
TFTTGEAMRV VKVKSILEHS WEDTSQKEIE KAVDNLKNEK PTFFNTETRS VLGLISQRLA
SSIDVETEYG QLTVELDNIE MNFIPTNGDR VRLECNIQLD DGFVDKQGEI LEVTKLFPTR
IQEGEKCIVE RVYVHMVVLG PETYILKTDL PTGTDLHLGD IVLADLIECQ YSKFTRRAIK
ITPLEKNFGA TKLTQQSSMG SSGSGKAVTV TGVNRFITAE LWQKESVSLK LTNNLNRTLR
LESITVCNDS ESQLSVVSPL ESKEISSGSE ITVTFEIHTQ FLGEAIEKYV LNFDLLKVRR
VFTVIVCKTK EEVAEAEKRM IAAEALMAPG RNSQERSRFY ANQVWCNKVD VIPGQQIVTK
RRFVALRLGC FEVPKELRQI CLTSERRQEM IKAIEQHYSF LTEPLSIKTY MHRFRLLLHL
EEIECFVNFR NYDRDRAHFL RDGEFLTLQI ENLAERRPSL VIGDTLRVIN PWSDPDSQTT
KSYEGIIHKV LFDRILLKFH SSFQEKYNGE DYRLEFYFSR YSFRKQHHAI SKIVGVMGED
FLFPSKVTKR ENPQLDVYMK DDDMYLYDSK LEWYNQSLNS IQKRAVFNIL RGEAENIPYV
LFGPPGSGKT MTLIETLLQL VRNLPGARIL VGTPSNSSAD LVTKRLIDSK ALLQGDFIRL
VSYNQVEKDL IPPEIMSYCA TSDVGAVGSC EDKMMVTESG LKLRCQAKFI GTHRITISTC
TTLGNFLQLG FPAGHFTHVL FDEAGQCTEP ETMVPIVMLT KKRSQVVLSG DPRQLQSIVT
SRIASKMGFS ISFLERLLER SPYRKDLQRF PESSGYNPLV LTKLLYNYRA LPSIMSIYSR
LFYDDELIPV LSEKDSRESR LLSKLRCVFE SEKDIPQAHG TFFYGIIGEN RQNNDSPSWF
NPQEVREVFL MTIALYRANV TADQIGIITP YQKQVKMLRS MFIGTDVVMP KIGSVEEFQG
QERDIILIST VRSSEEILRM DARFSLGFVR CSKRLNVAVS RARAMMIIFG NPHLLAVDEC
WRQLILFCVK NNAYFGCDLP QMVINQKDEV PVCLETFVPS LNTTDDLN
