MMI1_SCHPO
ID MMI1_SCHPO Reviewed; 488 AA.
AC O74958;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=RNA binding exosome specificity factor Mmi1 {ECO:0000305};
DE AltName: Full=Meiotic mRNA interception protein 1;
DE AltName: Full=YTH domain-containing protein mmi1;
GN Name=mmi1; ORFNames=SPCC736.12c;
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, INTERACTION WITH RRP6, AND SUBCELLULAR LOCATION.
RX PubMed=16823445; DOI=10.1038/nature04881;
RA Harigaya Y., Tanaka H., Yamanaka S., Tanaka K., Watanabe Y., Tsutsumi C.,
RA Chikashige Y., Hiraoka Y., Yamashita A., Yamamoto M.;
RT "Selective elimination of messenger RNA prevents an incidence of untimely
RT meiosis.";
RL Nature 442:45-50(2006).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-176; SER-178; SER-230;
RP SER-231; SER-261; SER-263; SER-265; SER-311 AND THR-312, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE
RP ERH1-MMI1 COMPLEX, INTERACTION WITH ERH1, AND DISRUPTION PHENOTYPE.
RX PubMed=26942678; DOI=10.1016/j.molcel.2016.01.029;
RA Sugiyama T., Thillainadesan G., Chalamcharla V.R., Meng Z.,
RA Balachandran V., Dhakshnamoorthy J., Zhou M., Grewal S.I.S.;
RT "Enhancer of Rudimentary Cooperates with Conserved RNA-Processing Factors
RT to Promote Meiotic mRNA Decay and Facultative Heterochromatin Assembly.";
RL Mol. Cell 61:747-759(2016).
RN [6]
RP FUNCTION, AND INTERACTION WITH ERH1.
RX PubMed=31974447; DOI=10.1038/s41598-020-57872-4;
RA Hazra D., Andric V., Palancade B., Rougemaille M., Graille M.;
RT "Formation of S. pombe Erh1 homodimer mediates gametogenic gene silencing
RT and meiosis progression.";
RL Sci. Rep. 10:1034-1034(2020).
RN [7] {ECO:0007744|PDB:6AKJ}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 96-122 IN COMPLEX WITH ERH1,
RP FUNCTION, IDENTIFICATION IN THE ERH1-MMI1 COMPLEX, INTERACTION WITH ERH1,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TYR-97; PHE-99; TRP-112 AND
RP ARG-119.
RX PubMed=30651569; DOI=10.1038/s41467-018-08273-9;
RA Xie G., Vo T.V., Thillainadesan G., Holla S., Zhang B., Jiang Y., Lv M.,
RA Xu Z., Wang C., Balachandran V., Shi Y., Li F., Grewal S.I.S.;
RT "A conserved dimer interface connects ERH and YTH family proteins to
RT promote gene silencing.";
RL Nat. Commun. 10:251-251(2019).
CC -!- FUNCTION: RNA-binding protein that recognizes and binds N6-
CC methyladenosine (m6A)-containing RNAs, a modification present at
CC internal sites of mRNAs and some non-coding RNAs (By similarity).
CC Functions alone and as part of the erh1-mmi1 complex, to recruit the
CC CCR4-NOT complex and the NURS complex to target RNAs (PubMed:26942678,
CC PubMed:30651569, PubMed:31974447). Suppresses the meiotic program
CC during vegetative growth and promotes the meiotic program during mating
CC (PubMed:31974447). Binds to DSR (determinant of selective removal)
CC regions in meiotic mRNA, and recruits the NURS complex to targets
CC (PubMed:16823445, PubMed:26942678). Recruitment of NURS complex to
CC target mRNAs promotes mRNA decay by engagement of the nuclear exosome,
CC and formation of heterochromatin islands at meiotic genes silenced by
CC the exosome (PubMed:16823445, PubMed:26942678). Recruitment of the
CC CCR4-NOT complex to target RNAs promotes heterochromatin formation at
CC RNAi-dependent heterochromatin domains (HOODs), including a subset of
CC meiotic genes, lncRNAs and retrotransposons (PubMed:26942678).
CC Recruitment of the CCR4-NOT complex to rDNA promotes rDNA
CC heterochromatin assembly (PubMed:26942678). Promotes non-canonical
CC transcription termination at meiotic genes and prevents lncRNA
CC transcription from invading and repressing adjacent genes
CC (PubMed:16823445, PubMed:30651569). {ECO:0000250|UniProtKB:Q06390,
CC ECO:0000269|PubMed:16823445, ECO:0000269|PubMed:26942678,
CC ECO:0000269|PubMed:30651569, ECO:0000269|PubMed:31974447}.
CC -!- SUBUNIT: Component of the erh1-mmi1 complex composed of mmi1 and erh1
CC (PubMed:26942678, PubMed:31974447, PubMed:30651569). Interacts (via N-
CC terminus) with erh1 in a 2:2 stoichiometry (PubMed:26942678,
CC PubMed:31974447, PubMed:30651569). Interacts with rrp6
CC (PubMed:16823445). {ECO:0000269|PubMed:16823445,
CC ECO:0000269|PubMed:26942678, ECO:0000269|PubMed:30651569,
CC ECO:0000269|PubMed:31974447}.
CC -!- INTERACTION:
CC O74958; O14327: pab2; NbExp=4; IntAct=EBI-7997069, EBI-7997255;
CC O74958; Q10295: pla1; NbExp=3; IntAct=EBI-7997069, EBI-7997221;
CC O74958; Q9UTR8: red1; NbExp=5; IntAct=EBI-7997069, EBI-1117407;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:16823445}.
CC -!- DISRUPTION PHENOTYPE: Read-through transcription of regulatory lncRNAs
CC (long non-coding RNAs) (PubMed:30651569). Decreases premature pre-mRNA
CC 3'-end formation of ssm4 (PubMed:30651569). Increases levels and
CC cytoplasmic localization of mating and meiosis specific transcripts
CC during vegetative growth (PubMed:30651569). Decreases heterochromatin
CC formation at meiotic heterochromatin islands (PubMed:26942678).
CC {ECO:0000269|PubMed:26942678, ECO:0000269|PubMed:30651569}.
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DR EMBL; CU329672; CAA19276.3; -; Genomic_DNA.
DR PIR; T41569; T41569.
DR RefSeq; NP_587783.2; NM_001022776.3.
DR PDB; 5DNO; X-ray; 1.80 A; A=322-488.
DR PDB; 5DNP; X-ray; 2.30 A; A/B=322-488.
DR PDB; 5EIM; X-ray; 1.54 A; A/B=326-488.
DR PDB; 5EIP; X-ray; 1.49 A; A/B=349-477.
DR PDB; 5H8A; X-ray; 1.75 A; A/B/C/D=311-488.
DR PDB; 5HFZ; X-ray; 1.96 A; A/B/C/D=319-488.
DR PDB; 5O8M; X-ray; 1.45 A; A/B/C/D=347-488.
DR PDB; 6AKJ; X-ray; 2.70 A; A/B=96-122.
DR PDB; 6FPP; X-ray; 1.93 A; A/B=327-488.
DR PDB; 6FPQ; X-ray; 1.42 A; A=299-488.
DR PDB; 6FPX; X-ray; 1.97 A; A/C/E=299-488.
DR PDBsum; 5DNO; -.
DR PDBsum; 5DNP; -.
DR PDBsum; 5EIM; -.
DR PDBsum; 5EIP; -.
DR PDBsum; 5H8A; -.
DR PDBsum; 5HFZ; -.
DR PDBsum; 5O8M; -.
DR PDBsum; 6AKJ; -.
DR PDBsum; 6FPP; -.
DR PDBsum; 6FPQ; -.
DR PDBsum; 6FPX; -.
DR AlphaFoldDB; O74958; -.
DR SMR; O74958; -.
DR BioGRID; 276102; 68.
DR IntAct; O74958; 7.
DR MINT; O74958; -.
DR STRING; 4896.SPCC736.12c.1; -.
DR iPTMnet; O74958; -.
DR MaxQB; O74958; -.
DR PaxDb; O74958; -.
DR PRIDE; O74958; -.
DR EnsemblFungi; SPCC736.12c.1; SPCC736.12c.1:pep; SPCC736.12c.
DR GeneID; 2539540; -.
DR KEGG; spo:SPCC736.12c; -.
DR PomBase; SPCC736.12c; mmi1.
DR VEuPathDB; FungiDB:SPCC736.12c; -.
DR eggNOG; KOG1901; Eukaryota.
DR HOGENOM; CLU_570057_0_0_1; -.
DR InParanoid; O74958; -.
DR OMA; SRYFIML; -.
DR PRO; PR:O74958; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR GO; GO:0033620; C:Mei2 nuclear dot complex; IDA:PomBase.
DR GO; GO:1990251; C:nuclear exosome focus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:1905762; F:CCR4-NOT complex binding; IDA:PomBase.
DR GO; GO:0003729; F:mRNA binding; IDA:PomBase.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IBA:GO_Central.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IPI:PomBase.
DR GO; GO:0140517; F:protein-RNA adaptor activity; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:PomBase.
DR GO; GO:0110064; P:lncRNA catabolic process; IMP:PomBase.
DR GO; GO:0061157; P:mRNA destabilization; IBA:GO_Central.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IMP:PomBase.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:PomBase.
DR GO; GO:0071031; P:nuclear mRNA surveillance of mRNA 3'-end processing; IMP:PomBase.
DR GO; GO:0071030; P:nuclear mRNA surveillance of spliceosomal pre-mRNA splicing; IMP:PomBase.
DR GO; GO:0071029; P:nuclear ncRNA surveillance; IMP:PomBase.
DR GO; GO:0033621; P:nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IMP:PomBase.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IDA:PomBase.
DR GO; GO:0090053; P:positive regulation of pericentric heterochromatin assembly; IMP:PomBase.
DR GO; GO:1904595; P:positive regulation of termination of RNA polymerase II transcription; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:2000804; P:regulation of termination of RNA polymerase II transcription, poly(A)-coupled; IMP:UniProtKB.
DR GO; GO:1902794; P:siRNA-independent facultative heterochromatin assembly; IMP:PomBase.
DR DisProt; DP01975; -.
DR InterPro; IPR007275; YTH_domain.
DR InterPro; IPR045168; YTH_prot.
DR PANTHER; PTHR12357; PTHR12357; 1.
DR Pfam; PF04146; YTH; 1.
DR PROSITE; PS50882; YTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..488
FT /note="RNA binding exosome specificity factor Mmi1"
FT /id="PRO_0000372616"
FT DOMAIN 350..476
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 25..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..122
FT /note="Interaction with erh1"
FT /evidence="ECO:0000269|PubMed:30651569"
FT REGION 163..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 97
FT /note="Y->A: Decreases interaction with erh1."
FT /evidence="ECO:0000269|PubMed:30651569"
FT MUTAGEN 99
FT /note="F->A: Decreases interaction with erh1."
FT /evidence="ECO:0000269|PubMed:30651569"
FT MUTAGEN 112
FT /note="W->A: Abolishes interaction with erh1. Abnormal
FT poly(A)-site selection of ssm4. Increases the level and
FT cytoplasmic localization of mating and meiosis specific
FT transcripts. Decreases H3K9me2 levels at meiotic
FT heterochromatin islands, decreases mating efficiency, cold
FT sensitive, normal growth at high temperature."
FT /evidence="ECO:0000269|PubMed:30651569"
FT MUTAGEN 119
FT /note="R->A: Decreases interaction with erh1."
FT /evidence="ECO:0000269|PubMed:30651569"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:6AKJ"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6AKJ"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6AKJ"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:6AKJ"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6FPQ"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:6FPQ"
FT STRAND 348..357
FT /evidence="ECO:0007829|PDB:6FPQ"
FT HELIX 360..369
FT /evidence="ECO:0007829|PDB:6FPQ"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:6FPQ"
FT HELIX 376..386
FT /evidence="ECO:0007829|PDB:6FPQ"
FT STRAND 389..397
FT /evidence="ECO:0007829|PDB:6FPQ"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:6FPQ"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:6FPQ"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:6FPQ"
FT STRAND 426..440
FT /evidence="ECO:0007829|PDB:6FPQ"
FT HELIX 443..450
FT /evidence="ECO:0007829|PDB:6FPQ"
FT HELIX 466..481
FT /evidence="ECO:0007829|PDB:6FPQ"
SQ SEQUENCE 488 AA; 54539 MW; 329704519DE3AE4A CRC64;
MSNTNFSTSR SSKSIPELPN LEALRSLWPP PSLNESGDTR SVWTTHTGEP VASSVLSTSG
SNNFSSPLKR PAPESHDAPI GRRLMVDDPR LIKHGKYDFS RHCTDYGHSY EWPYFRSLRR
ESMLYHTSGS YPESQPPYSS YSTDAPHYYH AGSESSAYYD SRSRLHGIQP PPKRRTLSPP
PRRLADPVVV GSSRYVEEEV YRRPPYTLAS EVPSSASAYQ AGYSSYPVRS SPQLSHEDTR
HGIASSGSTR YPFVPANTRA SHSPSLLEPY AHSLPSSVAP VGAYPEKSSY LLSNSSNDSA
SRKEKPKARA STPPPLNFSR ASEHRNEKGE RISMINPRVV LDENGISHRS RYFIMLCDNE
TAIAHAKKTS IWAVKKDSSK RISDAYKKAS VYFIFVAQQT YNALGYAQVV SDLNSTELPF
WSDSSHAGGV RIKWIKTCNL FSAEISEIVS HMDHGSEARD GMEMMYDEGS RLCTLINYAI
MKRIGRDR
