TAS3_SCHPO
ID TAS3_SCHPO Reviewed; 549 AA.
AC O94687;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=RNA-induced transcriptional silencing complex protein tas3;
DE Short=RITS protein tas3;
GN Name=tas3; ORFNames=SPBC83.03c;
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, COMPOSITION OF THE RDRC AND RITS COMPLEXES, SUBCELLULAR LOCATION,
RP 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 [3]
RP FUNCTION, COMPOSITION OF THE RITS COMPLEX, AND INTERACTION WITH CHP1.
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 [4]
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).
CC -!- FUNCTION: Has a role in the RNA interference (RNAi) pathway which is
CC important for heterochromatin formation and accurate chromosome
CC segregation. A member of the RNA-induced transcriptional silencing
CC (RITS) complex which is involved in the biosynthesis of dsRNA from
CC primer siRNAs provided by the RNA-directed RNA polymerase (RDRC)
CC complex. {ECO:0000269|PubMed:14704433, ECO:0000269|PubMed:15607976}.
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.
CC {ECO:0000269|PubMed:14704433}.
CC -!- INTERACTION:
CC O94687; O74957: ago1; NbExp=5; IntAct=EBI-423002, EBI-422882;
CC O94687; Q10103: chp1; NbExp=10; IntAct=EBI-423002, EBI-421832;
CC O94687; O74465: hrr1; NbExp=2; IntAct=EBI-423002, EBI-15624169;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body.
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DR EMBL; CU329671; CAB36865.1; -; Genomic_DNA.
DR PIR; T40692; T40692.
DR RefSeq; NP_595635.1; NM_001021529.2.
DR PDB; 3D1B; X-ray; 1.70 A; A/B/C=426-545.
DR PDB; 3D1D; X-ray; 2.60 A; A/B/C/D/E/F=426-545.
DR PDB; 3TIX; X-ray; 2.90 A; A/C=9-83.
DR PDBsum; 3D1B; -.
DR PDBsum; 3D1D; -.
DR PDBsum; 3TIX; -.
DR AlphaFoldDB; O94687; -.
DR SMR; O94687; -.
DR BioGRID; 277258; 313.
DR DIP; DIP-29302N; -.
DR IntAct; O94687; 4.
DR STRING; 4896.SPBC83.03c.1; -.
DR iPTMnet; O94687; -.
DR MaxQB; O94687; -.
DR PaxDb; O94687; -.
DR PRIDE; O94687; -.
DR EnsemblFungi; SPBC83.03c.1; SPBC83.03c.1:pep; SPBC83.03c.
DR GeneID; 2540735; -.
DR KEGG; spo:SPBC83.03c; -.
DR PomBase; SPBC83.03c; tas3.
DR VEuPathDB; FungiDB:SPBC83.03c; -.
DR HOGENOM; CLU_496214_0_0_1; -.
DR OMA; EWAESIN; -.
DR EvolutionaryTrace; O94687; -.
DR PRO; PR:O94687; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0030958; C:RITS complex; IDA:PomBase.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:PomBase.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:PomBase.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IGI:PomBase.
DR InterPro; IPR019486; Argonaute_hook_dom.
DR Pfam; PF10427; Ago_hook; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Chromosome partition; Cytoplasm; Cytoskeleton;
KW Nucleus; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..549
FT /note="RNA-induced transcriptional silencing complex
FT protein tas3"
FT /id="PRO_0000256153"
FT REGION 89..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 29..49
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 58..79
FT /evidence="ECO:0007829|PDB:3TIX"
FT HELIX 435..444
FT /evidence="ECO:0007829|PDB:3D1B"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:3D1B"
FT HELIX 453..467
FT /evidence="ECO:0007829|PDB:3D1B"
FT HELIX 473..481
FT /evidence="ECO:0007829|PDB:3D1B"
FT HELIX 495..505
FT /evidence="ECO:0007829|PDB:3D1B"
FT HELIX 510..526
FT /evidence="ECO:0007829|PDB:3D1B"
FT HELIX 530..543
FT /evidence="ECO:0007829|PDB:3D1B"
SQ SEQUENCE 549 AA; 63056 MW; 4569CF59851A22A0 CRC64;
MEKGIKKYLP SLPFLACISD FPENHGTSRR SATVSLERVH ELFTEHWLSN LKNRREKRQE
LAEEAVYCRS EMLSQRKLLA AVDFPQQLKN SPAKAKATHT SSGVTKEVRA SKKYTSSNVE
FPLVTDGKEK PVKSKQLRKN SVTEFEKPIE TKKSKHRKSR NKFLDKSSGS MEIESWDNST
SDSIIESSSR LHESISLREN DIRSSDSKSV GWDDNSTGFR ESSKSLDHTD TSMFMELDSN
SDPQFRPKYQ AKSSWFAPDD PEASWGNLDD GWGETNGSWS STDDTKHYKN EWAESINLDN
FNRPSQQEDY DKPKNTQVSR SSNHHRRYDS YHPDSRSDSY RSKREHYDNR DTGPRSKHLE
KSSYVYNQNF EDRTHLSDHG AHFHLGNAND FNMQGSSRKR KASDRQRESR ENELPTKKLN
ASDSHNPLAS LTTDKNDLYI NWLKSLSFFQ TNSSCAEALV KVIPHYHNKL IDFSQVLQLV
FSASEKFPIQ ENQPLPEQLM FLSNLEKQTP FAKAVGSSIY KLVTGKNLSL DFASQILKEA
SILEHKNEK
