AGO10_ARATH
ID AGO10_ARATH Reviewed; 988 AA.
AC Q9XGW1; O49256;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein argonaute 10 {ECO:0000303|PubMed:19054365};
DE AltName: Full=Protein PINHEAD {ECO:0000303|PubMed:12468725, ECO:0000303|PubMed:9876176};
DE AltName: Full=Protein ZWILLE {ECO:0000303|PubMed:9501101, ECO:0000303|PubMed:9876176};
GN Name=AGO10 {ECO:0000303|PubMed:19054365};
GN Synonyms=PNH {ECO:0000303|PubMed:12468725, ECO:0000303|PubMed:9876176},
GN ZLL {ECO:0000303|PubMed:9501101, ECO:0000303|PubMed:9876176};
GN OrderedLocusNames=At5g43810 {ECO:0000312|Araport:AT5G43810};
GN ORFNames=MQD19.17 {ECO:0000312|EMBL:BAB11310.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9876176; DOI=10.1242/dev.126.3.469;
RA Lynn K., Fernandez A., Aida M., Sedbrook J., Tasaka M., Masson P.,
RA Barton M.K.;
RT "The PINHEAD/ZWILLE gene acts pleiotropically in Arabidopsis development
RT and has overlapping functions with the ARGONAUTE1 gene.";
RL Development 126:469-481(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9501101; DOI=10.1093/emboj/17.6.1799;
RA Moussian B., Schoof H., Haecker A., Juergens G., Laux T.;
RT "Role of the ZWILLE gene in the regulation of central shoot meristem cell
RT fate during Arabidopsis embryogenesis.";
RL EMBO J. 17:1799-1809(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12468725; DOI=10.1105/tpc.005132;
RA Newman K.L., Fernandez A.G., Barton M.K.;
RT "Regulation of axis determinacy by the Arabidopsis PINHEAD gene.";
RL Plant Cell 14:3029-3042(2002).
RN [6]
RP FUNCTION.
RX PubMed=19054365; DOI=10.1111/j.1365-313x.2008.03757.x;
RA Liu Q., Yao X., Pi L., Wang H., Cui X., Huang H.;
RT "The ARGONAUTE10 gene modulates shoot apical meristem maintenance and leaf
RT polarity establishment by repressing miR165/166 in Arabidopsis.";
RL Plant J. 58:27-40(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19763164; DOI=10.1371/journal.pgen.1000646;
RA Mallory A.C., Hinze A., Tucker M.R., Bouche N., Gasciolli V., Elmayan T.,
RA Lauressergues D., Jauvion V., Vaucheret H., Laux T.;
RT "Redundant and specific roles of the ARGONAUTE proteins AGO1 and ZLL in
RT development and small RNA-directed gene silencing.";
RL PLoS Genet. 5:E1000646-E1000646(2009).
RN [8]
RP FUNCTION.
RX PubMed=20128885; DOI=10.1111/j.1365-313x.2010.04162.x;
RA Beauclair L., Yu A., Bouche N.;
RT "microRNA-directed cleavage and translational repression of the copper
RT chaperone for superoxide dismutase mRNA in Arabidopsis.";
RL Plant J. 62:454-462(2010).
RN [9]
RP INDUCTION BY REV.
RX PubMed=22781836; DOI=10.1016/j.mod.2012.06.007;
RA Brandt R., Xie Y., Musielak T., Graeff M., Stierhof Y.D., Huang H.,
RA Liu C.M., Wenkel S.;
RT "Control of stem cell homeostasis via interlocking microRNA and
RT microProtein feedback loops.";
RL Mech. Dev. 130:25-33(2013).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP GATA18/HAN AND KNAT1/BP.
RX PubMed=26390296; DOI=10.1371/journal.pgen.1005479;
RA Ding L., Yan S., Jiang L., Zhao W., Ning K., Zhao J., Liu X., Zhang J.,
RA Wang Q., Zhang X.;
RT "HANABA TARANU (HAN) bridges meristem and organ primordia boundaries
RT through PINHEAD, JAGGED, BLADE-ON-PETIOLE2 and CYTOKININ OXIDASE 3 during
RT flower development in Arabidopsis.";
RL PLoS Genet. 11:E1005479-E1005479(2015).
RN [11]
RP INTERACTION WITH RICE1 AND RICE2, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=28463111; DOI=10.7554/elife.24466;
RA Zhang Z., Hu F., Sung M.W., Shu C., Castillo-Gonzalez C., Koiwa H.,
RA Tang G., Dickman M., Li P., Zhang X.;
RT "RISC-interacting clearing 3'- 5' exoribonucleases (RICEs) degrade
RT uridylated cleavage fragments to maintain functional RISC in Arabidopsis
RT thaliana.";
RL Elife 6:E24466-E24466(2017).
CC -!- FUNCTION: Involved in RNA-mediated post-transcriptional gene silencing
CC (PTGS). Main component of the RNA-induced silencing complex (RISC) that
CC binds to a short guide RNA such as a microRNA (miRNA) or small
CC interfering RNA (siRNA). RISC uses the mature miRNA or siRNA as a guide
CC for slicer-directed cleavage of homologous mRNAs to repress gene
CC expression. Required for reliable formation of primary and axillary
CC shoot apical meristems. Specifies leaf adaxial identity by repressing
CC the miR165 and miR166 microRNAs in the embryonic shoot apex, in the
CC shoot apical meristem (SAM) and leaf. Represses the microRNA miR398
CC which targets CCS1 chaperone mRNAs for translational inhibition. Acts
CC as a negative regulator of AGO1 protein level. Like AGO1, is required
CC for stem cell function and organ polarity. Unlike AGO1, is not
CC subjected to small RNA-mediated repression itself. Essential for
CC multiple processes in development. Coregulates, with GATA18/HAN, the
CC shoot apical meristem (SAM) organization (PubMed:26390296).
CC {ECO:0000269|PubMed:12468725, ECO:0000269|PubMed:19054365,
CC ECO:0000269|PubMed:19763164, ECO:0000269|PubMed:20128885,
CC ECO:0000269|PubMed:26390296, ECO:0000269|PubMed:9501101,
CC ECO:0000269|PubMed:9876176}.
CC -!- SUBUNIT: Interacts with GATA18/HAN and KNAT1/BP (PubMed:26390296).
CC Interacts with RICE1 and RICE2 that act as cofactors (PubMed:28463111).
CC {ECO:0000269|PubMed:26390296, ECO:0000269|PubMed:28463111}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28463111}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, developing
CC embryo, siliques, inflorescences, provascular tissue, shoot apical
CC meristem (SAM) and adaxial (upper) sides of lateral organ primordia.
CC Observed in the floral meristem, the adaxial side of sepal primordia,
CC and the provascular tissue (PubMed:26390296).
CC {ECO:0000269|PubMed:12468725, ECO:0000269|PubMed:26390296,
CC ECO:0000269|PubMed:9876176}.
CC -!- INDUCTION: Up-regulated by REV (PubMed:22781836).
CC {ECO:0000269|PubMed:22781836}.
CC -!- DISRUPTION PHENOTYPE: Defects in meristem formation. Shoot apical
CC meristem (SAM) terminates to a flat meristem, a small radially
CC symmetric pin-like structure that lacks a vascular strand, a radially
CC symmetric leaf, a single leaf or two leaves fused on their adaxial
CC sides. Abnormal ovules and embryos. The double mutant pnh-2 han-2 has
CC smaller inflorescence meristems (IM) and taller floral meristems (FM)
CC leading to fewer petals (PubMed:26390296).
CC {ECO:0000269|PubMed:19763164, ECO:0000269|PubMed:26390296,
CC ECO:0000269|PubMed:9501101, ECO:0000269|PubMed:9876176}.
CC -!- MISCELLANEOUS: Plants overexpressing AGO10 show upward curling of leaf
CC blades and double cotyledon-like structures.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000305}.
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DR EMBL; AF154272; AAD40098.1; -; Genomic_DNA.
DR EMBL; AJ223508; CAA11429.1; -; mRNA.
DR EMBL; AB026651; BAB11310.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95011.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95012.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69955.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69956.1; -; Genomic_DNA.
DR PIR; T52134; T52134.
DR RefSeq; NP_001190464.1; NM_001203535.1.
DR RefSeq; NP_001331599.1; NM_001344506.1.
DR RefSeq; NP_001331600.1; NM_001344505.1.
DR RefSeq; NP_199194.1; NM_123748.3.
DR AlphaFoldDB; Q9XGW1; -.
DR SMR; Q9XGW1; -.
DR BioGRID; 19653; 3.
DR STRING; 3702.AT5G43810.2; -.
DR PaxDb; Q9XGW1; -.
DR PRIDE; Q9XGW1; -.
DR ProteomicsDB; 244887; -.
DR EnsemblPlants; AT5G43810.1; AT5G43810.1; AT5G43810.
DR EnsemblPlants; AT5G43810.2; AT5G43810.2; AT5G43810.
DR EnsemblPlants; AT5G43810.3; AT5G43810.3; AT5G43810.
DR EnsemblPlants; AT5G43810.4; AT5G43810.4; AT5G43810.
DR GeneID; 834403; -.
DR Gramene; AT5G43810.1; AT5G43810.1; AT5G43810.
DR Gramene; AT5G43810.2; AT5G43810.2; AT5G43810.
DR Gramene; AT5G43810.3; AT5G43810.3; AT5G43810.
DR Gramene; AT5G43810.4; AT5G43810.4; AT5G43810.
DR KEGG; ath:AT5G43810; -.
DR Araport; AT5G43810; -.
DR TAIR; locus:2170897; AT5G43810.
DR eggNOG; KOG1041; Eukaryota.
DR HOGENOM; CLU_004544_0_0_1; -.
DR InParanoid; Q9XGW1; -.
DR OMA; CFAQQQH; -.
DR OrthoDB; 159407at2759; -.
DR PhylomeDB; Q9XGW1; -.
DR PRO; PR:Q9XGW1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XGW1; baseline and differential.
DR Genevisible; Q9XGW1; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0035198; F:miRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IDA:TAIR.
DR GO; GO:0010586; P:miRNA metabolic process; IMP:TAIR.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0010072; P:primary shoot apical meristem specification; IMP:TAIR.
DR GO; GO:0009934; P:regulation of meristem structural organization; IMP:UniProtKB.
DR GO; GO:1902183; P:regulation of shoot apical meristem development; IMP:TAIR.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:UniProtKB.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR032472; ArgoL2.
DR InterPro; IPR032473; Argonaute_Mid_dom.
DR InterPro; IPR032474; Argonaute_N.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR045246; Piwi_ago-like.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF08699; ArgoL1; 1.
DR Pfam; PF16488; ArgoL2; 1.
DR Pfam; PF16487; ArgoMid; 1.
DR Pfam; PF16486; ArgoN; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM01163; DUF1785; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00950; Piwi; 1.
DR SUPFAM; SSF101690; SSF101690; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Reference proteome; Repressor;
KW Ribonucleoprotein; RNA-binding; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..988
FT /note="Protein argonaute 10"
FT /id="PRO_0000194069"
FT DOMAIN 337..451
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 625..946
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 475..479
FT /note="PRDRE -> AEGQR (in Ref. 2; CAA11429)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="N -> D (in Ref. 2; CAA11429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 988 AA; 110868 MW; 32EBB349C613DA20 CRC64;
MPIRQMKDSS ETHLVIKTQP LKHHNPKTVQ NGKIPPPSPS PVTVTTPATV TQSQASSPSP
PSKNRSRRRN RGGRKSDQGD VCMRPSSRPR KPPPPSQTTS SAVSVATAGE IVAVNHQMQM
GVRKNSNFAP RPGFGTLGTK CIVKANHFLA DLPTKDLNQY DVTITPEVSS KSVNRAIIAE
LVRLYKESDL GRRLPAYDGR KSLYTAGELP FTWKEFSVKI VDEDDGIING PKRERSYKVA
IKFVARANMH HLGEFLAGKR ADCPQEAVQI LDIVLRELSV KRFCPVGRSF FSPDIKTPQR
LGEGLESWCG FYQSIRPTQM GLSLNIDMAS AAFIEPLPVI EFVAQLLGKD VLSKPLSDSD
RVKIKKGLRG VKVEVTHRAN VRRKYRVAGL TTQPTRELMF PVDENCTMKS VIEYFQEMYG
FTIQHTHLPC LQVGNQKKAS YLPMEACKIV EGQRYTKRLN EKQITALLKV TCQRPRDREN
DILRTVQHNA YDQDPYAKEF GMNISEKLAS VEARILPAPW LKYHENGKEK DCLPQVGQWN
MMNKKMINGM TVSRWACVNF SRSVQENVAR GFCNELGQMC EVSGMEFNPE PVIPIYSARP
DQVEKALKHV YHTSMNKTKG KELELLLAIL PDNNGSLYGD LKRICETELG LISQCCLTKH
VFKISKQYLA NVSLKINVKM GGRNTVLVDA ISCRIPLVSD IPTIIFGADV THPENGEESS
PSIAAVVASQ DWPEVTKYAG LVCAQAHRQE LIQDLYKTWQ DPVRGTVSGG MIRDLLISFR
KATGQKPLRI IFYRDGVSEG QFYQVLLYEL DAIRKACASL EPNYQPPVTF IVVQKRHHTR
LFANNHRDKN STDRSGNILP GTVVDTKICH PTEFDFYLCS HAGIQGTSRP AHYHVLWDEN
NFTADGIQSL TNNLCYTYAR CTRSVSIVPP AYYAHLAAFR ARFYLEPEIM QDNGSPGKKN
TKTTTVGDVG VKPLPALKEN VKRVMFYC
