O74957 (AGO1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein argonaute

Alternative name(s):
Cell cycle control protein ago1
Eukaryotic translation initiation factor 2C 2-like protein ago1
PAZ Piwi domain protein ago1
Protein slicer
RNA interference pathway protein ago1

Gene names

Name:	ago1
Synonyms:	csp9
ORF Names:	SPCC736.11

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	834 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for G1 arrest and mating in response to nitrogen starvation. Ago1 regulation of cytokinesis and cell cycle checkpoints occurs downstream of dcr1. Required, indirectly, for regulated hyperphosphorylation of cdc2. Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation, accurate chromosome segregation, centromere cohesion and telomere function during mitosis and meiosis. Required for silencing at the centromeres and for initiation of transcriptionally silent heterochromatin at the mating type locus. Promotes histone H3K9 methylation necessary for centromere function. Required for recruitment of swi6 and cohesin to an ectopic dg repeat. A member of the RNA-induced transcriptional silencing (RITS) complex which is involved in the biosynthesis of dsRNA from primer siRNAs provided by the RNA-directed RNA polymerase (RDRC) complex. Has ribonuclease H-like cleavage (slicing) activity towards target messages complementary to siRNA and can direct site-specific cleavage of RNA substrates via siRNA. Slicing activity is required for both post-transcriptional and transcriptional gene silencing as well as for histone H3 'Lys-10' methylation spreading, conversion of double-stranded siRNA to single-stranded siRNA and siRNA-dependent association of ago1 with chromatin. A member of the argonaute siRNA chaperone (ARC) complex which is required for histone H3K9 methylation, heterochromatin assembly and siRNA generation. The ARC complex contains mostly double-stranded siRNA. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12
Subunit structure	Ago1, chp1 and tas3 interact to form the core of the RNA-induced transcriptional silencing (RITS) complex. The RITS complex interacts with the RDRC complex via interaction between ago1 and hrr1. Clr4 has a role in mediating this interaction. Component of the argonaute siRNA chaperone (ARC) complex composed of ago1, arb1 and arb2. Interacts with arb1. Ref.6 Ref.12
Subcellular location	Cytoplasm. Nucleus. Chromosome › centromere. Chromosome › telomere. Note: Associates with telomeric and mating-type region heterochromatin. Ref.6 Ref.10
Sequence similarities	Belongs to the argonaute family. Ago subfamily. Contains 1 PAZ domain. Contains 1 Piwi domain.

Ontologies

Keywords
Biological process	Cell cycle Chromosome partition RNA-mediated gene silencing
Cellular component	Centromere Chromosome Cytoplasm Nucleus Telomere
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin silencing at centromere Inferred from mutant phenotype. Source: GeneDB_Spombe chromatin silencing by small RNA Inferred from mutant phenotype. Source: GeneDB_Spombe conversion of ds siRNA to ss siRNA involved in RNA interference Inferred from mutant phenotype. Source: GeneDB_Spombe mitotic sister chromatid segregation Inferred from genetic interaction. Source: GeneDB_Spombe negative regulation of transcription from RNA polymerase II promoter Inferred from expression pattern. Source: GeneDB_Spombe regulation of chromatin silencing at centromere Inferred from mutant phenotype. Source: GeneDB_Spombe regulation of histone H3-K9 methylation Inferred from mutant phenotype. Source: GeneDB_Spombe regulation of nitrogen utilization Inferred from mutant phenotype. Source: GeneDB_Spombe
Cellular component	ARC complex Inferred from direct assay. Source: GeneDB_Spombe RITS complex Inferred from direct assay. Source: GeneDB_Spombe centromeric heterochromatin Inferred from direct assay. Source: GeneDB_Spombe cytosol Inferred from direct assay. Source: GeneDB_Spombe mating-type region heterochromatin Inferred from direct assay. Source: GeneDB_Spombe nuclear telomeric heterochromatin Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SPBP8B7.28c	O94276	2	EBI-422882,EBI-2651917

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 834	834	Protein argonaute		PRO_0000194065
Regions
	Domain	212 – 326	115	PAZ
	Domain	500 – 799	300	Piwi
Experimental info
	Mutagenesis	276	1	F → A: Decreased association with siRNAs. Normal histone H3 'K-10' methylation. Ref.12
	Mutagenesis	580	1	D → A: Lower target RNA cleavage activity. Up-regulated centromeric transcripts from the dg and dh heterochromatic repeats. Defective for centromeric heterochromatin assembly and silencing. Decreased association with siRNAs. Ref.11 Ref.12
	Mutagenesis	651	1	D → A: Lower target RNA cleavage activity. Up-regulated centromeric transcripts from the dg and dh heterochromatic repeats. Ref.11
	Mutagenesis	788	1	H → A: Up-regulated centromeric transcripts from the dg and dh heterochromatic repeats. Reduced siRNA corresponding to heterochromatic repeats. Ref.11

Sequences

	Sequence		Length	Mass (Da)
	O74957 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: F5CE397BF590D9E4	FASTA	834	94,439
	10 20 30 40 50 60 MSYKPSSEIA LRPGYGGLGK QITLKANFFQ IISLPNETIN QYHVIVGDGS RVPRKQSQLI 70 80 90 100 110 120 WNSKEVKQYF GSSWMNSVYD GRSMCWSKGD IADGTIKVNI GSESHPREIE FSIQKSSKIN 130 140 150 160 170 180 LHTLSQFVNS KYSSDPQVLS SIMFLDLLLK KKPSETLFGF MHSFFTGENG VSLGGGVEAW 190 200 210 220 230 240 KGFYQSIRPN QGFMSVNVDI SSSAFWRNDS LLQILMEYTD CSNVRDLTRF DLKRLSRKFR 250 260 270 280 290 300 FLKVTCQHRN NVGTDLANRV YSIEGFSSKS ASDSFFVRRL NGEEQKISVA EYFLENHNVR 310 320 330 340 350 360 LQYPNLPCIL VKNGAMLPIE FCFVVKGQRY TAKLNSDQTA NMIRFAVQRP FERVQQIDDF 370 380 390 400 410 420 VHQMDWDTDP YLTQYGMKIQ KKMLEVPARV LETPSIRYGG DCIERPVSGR WNLRGKRFLD 430 440 450 460 470 480 PPRAPIRSWA VMCFTSTRRL PMRGIENFLQ TYVQTLTSLG INFVMKKPPV LYADIRGSVE 490 500 510 520 530 540 ELCITLYKKA EQVGNAPPDY LFFILDKNSP EPYGSIKRVC NTMLGVPSQC AISKHILQSK 550 560 570 580 590 600 PQYCANLGMK INVKVGGINC SLIPKSNPLG NVPTLILGGD VYHPGVGATG VSIASIVASV 610 620 630 640 650 660 DLNGCKYTAV SRSQPRHQEV IEGMKDIVVY LLQGFRAMTK QQPQRIIYFR DGTSEGQFLS 670 680 690 700 710 720 VINDELSQIK EACHSLSPKY NPKILVCTTQ KRHHARFFIK NKSDGDRNGN PLPGTIIEKH 730 740 750 760 770 780 VTHPYQYDFY LISHPSLQGV SVPVHYTVLH DEIQMPPDQF QTLCYNLCYV YARATSAVSL 790 800 810 820 830 VPPVYYAHLV SNLARYQDVT ADDTFVETSE ASMDQEVKPL LALSSKLKTK MWYM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi." Volpe T.A., Kidner C., Hall I.M., Teng G., Grewal S.I.S., Martienssen R.A. Science 297:1833-1837(2002) [PubMed: 12193640] [Abstract] Cited for: FUNCTION.
[3]	"Establishment and maintenance of a heterochromatin domain." Hall I.M., Shankaranarayana G.D., Noma K., Ayoub N., Cohen A., Grewal S.I.S. Science 297:2232-2237(2002) [PubMed: 12215653] [Abstract] Cited for: FUNCTION.
[4]	"RNA interference is required for normal centromere function in fission yeast." Volpe T., Schramke V., Hamilton G.L., White S.A., Teng G., Martienssen R.A., Allshire R.C. Chromosome Res. 11:137-146(2003) [PubMed: 12733640] [Abstract] Cited for: FUNCTION.
[5]	"RNA interference machinery regulates chromosome dynamics during mitosis and meiosis in fission yeast." Hall I.M., Noma K., Grewal S.I.S. Proc. Natl. Acad. Sci. U.S.A. 100:193-198(2003) [PubMed: 12509501] [Abstract] Cited for: FUNCTION.
[6]	"Two RNAi complexes, RITS and RDRC, physically interact and localize to noncoding centromeric RNAs." Motamedi M.R., Verdel A., Colmenares S.U., Gerber S.A., Gygi S.P., Moazed D. Cell 119:789-802(2004) [PubMed: 15607976] [Abstract] Cited for: FUNCTION, COMPOSITION OF THE RDRC AND RITS COMPLEXES, INTERACTION WITH HRR1, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[7]	"A single Argonaute protein mediates both transcriptional and posttranscriptional silencing in Schizosaccharomyces pombe." Sigova A., Rhind N., Zamore P.D. Genes Dev. 18:2359-2367(2004) [PubMed: 15371329] [Abstract] Cited for: FUNCTION.
[8]	"ago1 and dcr1, two core components of the RNA interference pathway, functionally diverge from rdp1 in regulating cell cycle events in Schizosaccharomyces pombe." Carmichael J.B., Provost P., Ekwall K., Hobman T.C. Mol. Biol. Cell 15:1425-1435(2004) [PubMed: 14699070] [Abstract] Cited for: FUNCTION.
[9]	"RNAi-mediated targeting of heterochromatin by the RITS complex." Verdel A., Jia S., Gerber S., Sugiyama T., Gygi S.P., Grewal S.I.S., Moazed D. Science 303:672-676(2004) [PubMed: 14704433] [Abstract] Cited for: FUNCTION, COMPOSITION OF THE RITS COMPLEX.
[10]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]	"Argonaute slicing is required for heterochromatic silencing and spreading." Irvine D.V., Zaratiegui M., Tolia N.H., Goto D.B., Chitwood D.H., Vaughn M.W., Joshua-Tor L., Martienssen R.A. Science 313:1134-1137(2006) [PubMed: 16931764] [Abstract] Cited for: FUNCTION, RNA CLEAVAGE ACTIVITY, MUTAGENESIS OF ASP-580; ASP-651 AND HIS-788.
[12]	"Two different Argonaute complexes are required for siRNA generation and heterochromatin assembly in fission yeast." Buker S.M., Iida T., Buehler M., Villen J., Gygi S.P., Nakayama J., Moazed D. Nat. Struct. Mol. Biol. 14:200-207(2007) [PubMed: 17310250] [Abstract] Cited for: FUNCTION, INTERACTION WITH ARB1, COMPOSITION OF THE ARC COMPLEX, MUTAGENESIS OF PHE-276 AND ASP-580.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329672 Genomic DNA. Translation: CAA19275.1.
PIR	T41568.
RefSeq	NP_587782.1. NM_001022775.1.
3D structure databases
ProteinModelPortal	O74957.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29298N.
IntAct	O74957. 4 interactions.
STRING	O74957.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC736.11.1; SPCC736.11.1:pep; SPCC736.11.
GeneID	2539403.
GenomeReviews	Gene locus ago1 in contig CU329672_GR.
KEGG	spo:SPCC736.11.
NMPDR	fig|4896.1.peg.120.
Organism-specific databases
GeneDB_Spombe	SPCC736.11.
Phylogenomic databases
eggNOG	fuNOG05862.
GeneTree	EFGT00050000000579.
HOGENOM	HBG717005.
OMA	NWACINF.
OrthoDB	EOG4B8NN4.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002139-MONOMER.
Gene expression databases
ArrayExpress	O74957.
Family and domain databases
InterPro	IPR014811. DUF1785. IPR003100. PAZ. IPR003165. Piwi. IPR012337. RNaseH-like_dom. [Graphical view]
KO	K11596.
Pfam	PF08699. DUF1785. 1 hit. PF02170. PAZ. 1 hit. PF02171. Piwi. 1 hit. [Graphical view]
SMART	SM00949. PAZ. 1 hit. SM00950. Piwi. 1 hit. [Graphical view]
SUPFAM	SSF101690. PAZ. 1 hit. SSF53098. RNaseH_fold. 1 hit.
PROSITE	PS50821. PAZ. 1 hit. PS50822. PIWI. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AGO1_SCHPO

Accession

Primary (citable) accession number: O74957

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	December 14, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program