AGO1_SCHPO
ID AGO1_SCHPO Reviewed; 834 AA.
AC O74957;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein argonaute;
DE AltName: Full=Cell cycle control protein ago1;
DE AltName: Full=Eukaryotic translation initiation factor 2C 2-like protein ago1;
DE AltName: Full=PAZ Piwi domain protein ago1;
DE AltName: Full=Protein slicer;
DE AltName: Full=RNA interference pathway protein ago1;
GN Name=ago1; Synonyms=csp9; ORFNames=SPCC736.11;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=12193640; DOI=10.1126/science.1074973;
RA Volpe T.A., Kidner C., Hall I.M., Teng G., Grewal S.I.S., Martienssen R.A.;
RT "Regulation of heterochromatic silencing and histone H3 lysine-9
RT methylation by RNAi.";
RL Science 297:1833-1837(2002).
RN [3]
RP FUNCTION.
RX PubMed=12215653; DOI=10.1126/science.1076466;
RA Hall I.M., Shankaranarayana G.D., Noma K., Ayoub N., Cohen A.,
RA Grewal S.I.S.;
RT "Establishment and maintenance of a heterochromatin domain.";
RL Science 297:2232-2237(2002).
RN [4]
RP FUNCTION.
RX PubMed=12733640; DOI=10.1023/a:1022815931524;
RA Volpe T., Schramke V., Hamilton G.L., White S.A., Teng G.,
RA Martienssen R.A., Allshire R.C.;
RT "RNA interference is required for normal centromere function in fission
RT yeast.";
RL Chromosome Res. 11:137-146(2003).
RN [5]
RP FUNCTION.
RX PubMed=12509501; DOI=10.1073/pnas.232688099;
RA Hall I.M., Noma K., Grewal S.I.S.;
RT "RNA interference machinery regulates chromosome dynamics during mitosis
RT and meiosis in fission yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:193-198(2003).
RN [6]
RP FUNCTION, COMPOSITION OF THE RDRC AND RITS COMPLEXES, INTERACTION WITH
RP HRR1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15607976; DOI=10.1016/j.cell.2004.11.034;
RA Motamedi M.R., Verdel A., Colmenares S.U., Gerber S.A., Gygi S.P.,
RA Moazed D.;
RT "Two RNAi complexes, RITS and RDRC, physically interact and localize to
RT noncoding centromeric RNAs.";
RL Cell 119:789-802(2004).
RN [7]
RP FUNCTION.
RX PubMed=15371329; DOI=10.1101/gad.1218004;
RA Sigova A., Rhind N., Zamore P.D.;
RT "A single Argonaute protein mediates both transcriptional and
RT posttranscriptional silencing in Schizosaccharomyces pombe.";
RL Genes Dev. 18:2359-2367(2004).
RN [8]
RP FUNCTION.
RX PubMed=14699070; DOI=10.1091/mbc.e03-06-0433;
RA Carmichael J.B., Provost P., Ekwall K., Hobman T.C.;
RT "ago1 and dcr1, two core components of the RNA interference pathway,
RT functionally diverge from rdp1 in regulating cell cycle events in
RT Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 15:1425-1435(2004).
RN [9]
RP FUNCTION, AND COMPOSITION OF THE RITS COMPLEX.
RX PubMed=14704433; DOI=10.1126/science.1093686;
RA Verdel A., Jia S., Gerber S., Sugiyama T., Gygi S.P., Grewal S.I.S.,
RA Moazed D.;
RT "RNAi-mediated targeting of heterochromatin by the RITS complex.";
RL Science 303:672-676(2004).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [11]
RP FUNCTION, RNA CLEAVAGE ACTIVITY, AND MUTAGENESIS OF ASP-580; ASP-651 AND
RP HIS-788.
RX PubMed=16931764; DOI=10.1126/science.1128813;
RA Irvine D.V., Zaratiegui M., Tolia N.H., Goto D.B., Chitwood D.H.,
RA Vaughn M.W., Joshua-Tor L., Martienssen R.A.;
RT "Argonaute slicing is required for heterochromatic silencing and
RT spreading.";
RL Science 313:1134-1137(2006).
RN [12]
RP FUNCTION, INTERACTION WITH ARB1, COMPOSITION OF THE ARC COMPLEX, AND
RP MUTAGENESIS OF PHE-276 AND ASP-580.
RX PubMed=17310250; DOI=10.1038/nsmb1211;
RA Buker S.M., Iida T., Buehler M., Villen J., Gygi S.P., Nakayama J.,
RA Moazed D.;
RT "Two different Argonaute complexes are required for siRNA generation and
RT heterochromatin assembly in fission yeast.";
RL Nat. Struct. Mol. Biol. 14:200-207(2007).
CC -!- FUNCTION: Required for G1 arrest and mating in response to nitrogen
CC starvation. Ago1 regulation of cytokinesis and cell cycle checkpoints
CC occurs downstream of dcr1. Required, indirectly, for regulated
CC hyperphosphorylation of cdc2. Has a role in the RNA interference (RNAi)
CC pathway which is important for heterochromatin formation, accurate
CC chromosome segregation, centromere cohesion and telomere function
CC during mitosis and meiosis. Required for silencing at the centromeres
CC and for initiation of transcriptionally silent heterochromatin at the
CC mating type locus. Promotes histone H3K9 methylation necessary for
CC centromere function. Required for recruitment of swi6 and cohesin to an
CC ectopic dg repeat. A member of the RNA-induced transcriptional
CC silencing (RITS) complex which is involved in the biosynthesis of dsRNA
CC from primer siRNAs provided by the RNA-directed RNA polymerase (RDRC)
CC complex. Has ribonuclease H-like cleavage (slicing) activity towards
CC target messages complementary to siRNA and can direct site-specific
CC cleavage of RNA substrates via siRNA. Slicing activity is required for
CC both post-transcriptional and transcriptional gene silencing as well as
CC for histone H3 'Lys-10' methylation spreading, conversion of double-
CC stranded siRNA to single-stranded siRNA and siRNA-dependent association
CC of ago1 with chromatin. A member of the argonaute siRNA chaperone (ARC)
CC complex which is required for histone H3K9 methylation, heterochromatin
CC assembly and siRNA generation. The ARC complex contains mostly double-
CC stranded siRNA. {ECO:0000269|PubMed:12193640,
CC ECO:0000269|PubMed:12215653, ECO:0000269|PubMed:12509501,
CC ECO:0000269|PubMed:12733640, ECO:0000269|PubMed:14699070,
CC ECO:0000269|PubMed:14704433, ECO:0000269|PubMed:15371329,
CC ECO:0000269|PubMed:15607976, ECO:0000269|PubMed:16931764,
CC ECO:0000269|PubMed:17310250}.
CC -!- SUBUNIT: Ago1, chp1 and tas3 interact to form the core of the RNA-
CC induced transcriptional silencing (RITS) complex. The RITS complex
CC interacts with the RDRC complex via interaction between ago1 and hrr1.
CC Clr4 has a role in mediating this interaction. Component of the
CC argonaute siRNA chaperone (ARC) complex composed of ago1, arb1 and
CC arb2. Interacts with arb1. {ECO:0000269|PubMed:15607976,
CC ECO:0000269|PubMed:17310250}.
CC -!- INTERACTION:
CC O74957; Q9P7B8: arb1; NbExp=5; IntAct=EBI-422882, EBI-15624131;
CC O74957; Q10271: arb2; NbExp=4; IntAct=EBI-422882, EBI-15624152;
CC O74957; O94276: SPBP8B7.28c; NbExp=2; IntAct=EBI-422882, EBI-2651917;
CC O74957; O94687: tas3; NbExp=5; IntAct=EBI-422882, EBI-423002;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere.
CC Chromosome, telomere. Note=Associates with telomeric and mating-type
CC region heterochromatin.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA19275.1; -; Genomic_DNA.
DR PIR; T41568; T41568.
DR RefSeq; NP_587782.1; NM_001022775.2.
DR AlphaFoldDB; O74957; -.
DR SMR; O74957; -.
DR BioGRID; 275968; 225.
DR DIP; DIP-29298N; -.
DR IntAct; O74957; 7.
DR STRING; 4896.SPCC736.11.1; -.
DR MaxQB; O74957; -.
DR PaxDb; O74957; -.
DR EnsemblFungi; SPCC736.11.1; SPCC736.11.1:pep; SPCC736.11.
DR GeneID; 2539403; -.
DR KEGG; spo:SPCC736.11; -.
DR PomBase; SPCC736.11; ago1.
DR VEuPathDB; FungiDB:SPCC736.11; -.
DR eggNOG; KOG1041; Eukaryota.
DR HOGENOM; CLU_004544_0_1_1; -.
DR InParanoid; O74957; -.
DR OMA; KPRQAQP; -.
DR PhylomeDB; O74957; -.
DR Reactome; R-SPO-426486; Small interfering RNA (siRNA) biogenesis.
DR Reactome; R-SPO-426496; Post-transcriptional silencing by small RNAs.
DR Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR PRO; PR:O74957; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0033167; C:ARC complex; IDA:PomBase.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0030958; C:RITS complex; IDA:PomBase.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IDA:PomBase.
DR GO; GO:0035198; F:miRNA binding; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; EXP:PomBase.
DR GO; GO:0003723; F:RNA binding; IDA:PomBase.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:PomBase.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0033562; P:co-transcriptional gene silencing by RNA interference machinery; IMP:PomBase.
DR GO; GO:0070314; P:G1 to G0 transition; IMP:PomBase.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0070317; P:negative regulation of G0 to G1 transition; IMP:PomBase.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:PomBase.
DR GO; GO:1990431; P:priRNA 3'-end processing; IMP:PomBase.
DR GO; GO:1990432; P:siRNA 3'-end processing; IMP:PomBase.
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 Cell cycle; Centromere; Chromosome; Chromosome partition; Cytoplasm;
KW Nucleus; Reference proteome; RNA-mediated gene silencing; Telomere.
FT CHAIN 1..834
FT /note="Protein argonaute"
FT /id="PRO_0000194065"
FT DOMAIN 212..326
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 500..799
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT MUTAGEN 276
FT /note="F->A: Decreased association with siRNAs. Normal
FT histone H3 'K-10' methylation."
FT /evidence="ECO:0000269|PubMed:17310250"
FT MUTAGEN 580
FT /note="D->A: Lower target RNA cleavage activity. Up-
FT regulated centromeric transcripts from the dg and dh
FT heterochromatic repeats. Defective for centromeric
FT heterochromatin assembly and silencing. Decreased
FT association with siRNAs."
FT /evidence="ECO:0000269|PubMed:16931764,
FT ECO:0000269|PubMed:17310250"
FT MUTAGEN 651
FT /note="D->A: Lower target RNA cleavage activity. Up-
FT regulated centromeric transcripts from the dg and dh
FT heterochromatic repeats."
FT /evidence="ECO:0000269|PubMed:16931764"
FT MUTAGEN 788
FT /note="H->A: Up-regulated centromeric transcripts from the
FT dg and dh heterochromatic repeats. Reduced siRNA
FT corresponding to heterochromatic repeats."
FT /evidence="ECO:0000269|PubMed:16931764"
SQ SEQUENCE 834 AA; 94439 MW; F5CE397BF590D9E4 CRC64;
MSYKPSSEIA LRPGYGGLGK QITLKANFFQ IISLPNETIN QYHVIVGDGS RVPRKQSQLI
WNSKEVKQYF GSSWMNSVYD GRSMCWSKGD IADGTIKVNI GSESHPREIE FSIQKSSKIN
LHTLSQFVNS KYSSDPQVLS SIMFLDLLLK KKPSETLFGF MHSFFTGENG VSLGGGVEAW
KGFYQSIRPN QGFMSVNVDI SSSAFWRNDS LLQILMEYTD CSNVRDLTRF DLKRLSRKFR
FLKVTCQHRN NVGTDLANRV YSIEGFSSKS ASDSFFVRRL NGEEQKISVA EYFLENHNVR
LQYPNLPCIL VKNGAMLPIE FCFVVKGQRY TAKLNSDQTA NMIRFAVQRP FERVQQIDDF
VHQMDWDTDP YLTQYGMKIQ KKMLEVPARV LETPSIRYGG DCIERPVSGR WNLRGKRFLD
PPRAPIRSWA VMCFTSTRRL PMRGIENFLQ TYVQTLTSLG INFVMKKPPV LYADIRGSVE
ELCITLYKKA EQVGNAPPDY LFFILDKNSP EPYGSIKRVC NTMLGVPSQC AISKHILQSK
PQYCANLGMK INVKVGGINC SLIPKSNPLG NVPTLILGGD VYHPGVGATG VSIASIVASV
DLNGCKYTAV SRSQPRHQEV IEGMKDIVVY LLQGFRAMTK QQPQRIIYFR DGTSEGQFLS
VINDELSQIK EACHSLSPKY NPKILVCTTQ KRHHARFFIK NKSDGDRNGN PLPGTIIEKH
VTHPYQYDFY LISHPSLQGV SVPVHYTVLH DEIQMPPDQF QTLCYNLCYV YARATSAVSL
VPPVYYAHLV SNLARYQDVT ADDTFVETSE ASMDQEVKPL LALSSKLKTK MWYM
