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Database: UniProt
Entry: Q9XGW1
LinkDB: Q9XGW1
Original site: Q9XGW1 
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   18-SEP-2019, entry version 127.
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,
GN   ECO:0000303|PubMed:9876176}, ZLL {ECO:0000303|PubMed:9501101,
GN   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;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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;
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
RT   development 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
RT   cell 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
RT   reference 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
RT   leaf 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.,
RA   Elmayan T., Lauressergues D., Jauvion V., Vaucheret H., Laux T.;
RT   "Redundant and specific roles of the ARGONAUTE proteins AGO1 and ZLL
RT   in 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
RP   WITH 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.,
RA   Zhang J., 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
RT   during 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
RT   Arabidopsis thaliana.";
RL   Elife 6:E24466-E24466(2017).
CC   -!- FUNCTION: Involved in RNA-mediated post-transcriptional gene
CC       silencing (PTGS). Main component of the RNA-induced silencing
CC       complex (RISC) that binds to a short guide RNA such as a microRNA
CC       (miRNA) or small interfering RNA (siRNA). RISC uses the mature
CC       miRNA or siRNA as a guide for slicer-directed cleavage of
CC       homologous mRNAs to repress gene expression. Required for reliable
CC       formation of primary and axillary shoot apical meristems.
CC       Specifies leaf adaxial identity by repressing the miR165 and
CC       miR166 microRNAs in the embryonic shoot apex, in the shoot apical
CC       meristem (SAM) and leaf. Represses the microRNA miR398 which
CC       targets CCS1 chaperone mRNAs for translational inhibition. Acts as
CC       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,
CC       the 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
CC       (PubMed:28463111). {ECO:0000269|PubMed:26390296,
CC       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
CC       primordia. Observed in the floral meristem, the adaxial side of
CC       sepal primordia, 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
CC       radially symmetric leaf, a single leaf or two leaves fused on
CC       their adaxial sides. Abnormal ovules and embryos. The double
CC       mutant pnh-2 han-2 has smaller inflorescence meristems (IM) and
CC       taller floral meristems (FM) leading to fewer petals
CC       (PubMed:26390296). {ECO:0000269|PubMed:19763164,
CC       ECO:0000269|PubMed:26390296, ECO:0000269|PubMed:9501101,
CC       ECO:0000269|PubMed:9876176}.
CC   -!- MISCELLANEOUS: Plants overexpressing AGO10 show upward curling of
CC       leaf blades and double cotyledon-like structures.
CC   -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC       {ECO:0000305}.
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   SMR; Q9XGW1; -.
DR   BioGrid; 19653; 3.
DR   STRING; 3702.AT5G43810.2; -.
DR   PaxDb; Q9XGW1; -.
DR   PRIDE; Q9XGW1; -.
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   eggNOG; ENOG410XP07; LUCA.
DR   HOGENOM; HOG000116043; -.
DR   InParanoid; Q9XGW1; -.
DR   KO; K11593; -.
DR   OMA; SPDGYYH; -.
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:0035198; F:miRNA binding; IDA:TAIR.
DR   GO; GO:0051607; P:defense response to virus; IDA:TAIR.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0010586; P:miRNA metabolic process; IMP:TAIR.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
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   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; 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   Complete proteome; Cytoplasm; Developmental protein;
KW   Reference proteome; Repressor; Ribonucleoprotein; RNA-binding;
KW   RNA-mediated gene silencing; Transcription; Transcription regulation;
KW   Translation regulation.
FT   CHAIN         1    988       Protein argonaute 10.
FT                                /FTId=PRO_0000194069.
FT   DOMAIN      337    451       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN      625    946       Piwi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00150}.
FT   CONFLICT    475    479       PRDRE -> AEGQR (in Ref. 2; CAA11429).
FT                                {ECO:0000305}.
FT   CONFLICT    671    671       N -> D (in Ref. 2; CAA11429).
FT                                {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
//
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