ERH_SCHPO
ID ERH_SCHPO Reviewed; 104 AA.
AC G2TRN4; K7PD52;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Enhancer of rudimentary homolog 1 {ECO:0000305};
GN Name=erh1 {ECO:0000312|PomBase:SPAC19G12.17};
GN Synonyms=new10 {ECO:0000312|PomBase:SPAC19G12.17}; ORFNames=SPAC19G12.17;
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] {ECO:0000312|EMBL:AFK79846.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=972 / ATCC 24843 {ECO:0000312|EMBL:AFK79846.1};
RX PubMed=23145069; DOI=10.1371/journal.pone.0049059;
RA Krzyzanowski M.K., Kozlowska E., Kozlowski P.;
RT "Identification and Functional Analysis of the erh1(+) Gene Encoding
RT Enhancer of Rudimentary Homolog from the Fission Yeast Schizosaccharomyces
RT pombe.";
RL PLoS ONE 7:E49059-E49059(2012).
RN [2]
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 [3]
RP IDENTIFICATION.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [4]
RP IDENTIFICATION.
RX PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA Hagan I.M., Miller C.J.;
RT "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT additional genes required for growth and viability.";
RL Genetics 187:1207-1217(2011).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE
RP ERH1-MMI1 COMPLEX, INTERACTION WITH MMI1, SUBCELLULAR LOCATION, AND
RP 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] {ECO:0007744|PDB:6AKJ}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH MMI1, FUNCTION,
RP SUBUNIT, IDENTIFICATION IN THE ERH1-MMI1 COMPLEX, INTERACTION WITH MMI1,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-68.
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).
RN [7] {ECO:0007744|PDB:6S2W}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), FUNCTION, SUBUNIT, AND MUTAGENESIS
RP OF 11-ILE--LEU-13.
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).
CC -!- FUNCTION: Forms part of the erh1-mmi1 complex that recruits the CCR4-
CC 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). Recruitment of the NURS complex to target mRNAs
CC promotes mRNA decay by engagement of the nuclear exosome, and formation
CC of heterochromatin islands at meiotic genes silenced by the exosome
CC (PubMed:26942678). Recruitment of the CCR4-NOT complex to target RNAs
CC promotes heterochromatin formation at RNAi-dependent heterochromatin
CC domains (HOODs), including a subset of meiotic genes, lncRNAs and
CC retrotransposons (PubMed:26942678). Recruitment of the CCR4-NOT complex
CC to rDNA promotes rDNA heterochromatin assembly (PubMed:26942678).
CC {ECO:0000269|PubMed:26942678, ECO:0000269|PubMed:30651569,
CC ECO:0000269|PubMed:31974447}.
CC -!- SUBUNIT: Homodimer (PubMed:30651569, PubMed:31974447). Component of the
CC erh1-mmi1 complex (PubMed:26942678, PubMed:30651569). Interacts with
CC mmi1 (via N-terminus) in a 2:2 stoichiometry (PubMed:26942678,
CC PubMed:30651569, PubMed:31974447). {ECO:0000269|PubMed:26942678,
CC ECO:0000269|PubMed:30651569, ECO:0000269|PubMed:31974447}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23145069,
CC ECO:0000269|PubMed:26942678}. Cytoplasm {ECO:0000269|PubMed:23145069}.
CC Note=Localizes to chromatin regions during vegetative growth, localizes
CC to mei2 nuclear dots during meiosis. {ECO:0000269|PubMed:26942678}.
CC -!- DISRUPTION PHENOTYPE: Abnormal poly(A)-site selection of ssm4
CC (PubMed:30651569). Decreases degradation of mRNA containing a DSR
CC (determinant of selective removal) region (PubMed:26942678). Increases
CC levels of mating and meiosis specific transcripts (PubMed:26942678,
CC PubMed:30651569, PubMed:31974447). Increases expression of ncRNAs
CC responsive to environmental and developmental signals
CC (PubMed:30651569). Decreases expression of antisense RNAs, intergenic
CC RNAs, tRNAs and 5S rRNA (PubMed:30651569). Decreases heterochromatin
CC formation at meiotic heterochromatin islands (PubMed:26942678,
CC PubMed:30651569). Decreases heterochromatin formation at rDNA
CC (PubMed:26942678). Decreases mating efficiency (PubMed:26942678,
CC PubMed:30651569). Decreases vegetative cell population growth
CC (PubMed:23145069, PubMed:26942678, PubMed:31974447). Sensitive to cold
CC (PubMed:26942678, PubMed:30651569, PubMed:31974447). Sensitive to
CC sorbitol (PubMed:23145069). Sensitive to hydroxyurea (PubMed:23145069).
CC Sensitive to sodium dodecyl sulfate (PubMed:23145069). Normal growth at
CC high temperature (PubMed:30651569). Curved vegetative cell
CC (PubMed:23145069). Increases cell cycle arrest in mitotic G1 phase in
CC response to nitrogen starvation (PubMed:23145069). Abolishes mei2
CC nuclear dot formation (PubMed:26942678). Simultaneous deletion of mei4
CC suppresses cold sensitivity (PubMed:26942678).
CC {ECO:0000269|PubMed:23145069, ECO:0000269|PubMed:26942678,
CC ECO:0000269|PubMed:30651569, ECO:0000269|PubMed:31974447}.
CC -!- SIMILARITY: Belongs to the E(R) family. {ECO:0000305}.
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DR EMBL; JN194206; AFK79846.1; -; mRNA.
DR EMBL; JN194210; AFK79850.1; -; Genomic_DNA.
DR EMBL; CU329670; CCD31336.1; -; Genomic_DNA.
DR RefSeq; XP_004001791.1; XM_004001742.1.
DR PDB; 6AKJ; X-ray; 2.70 A; A/B=1-104.
DR PDB; 6S2W; X-ray; 1.95 A; A/B/C=1-104.
DR PDBsum; 6AKJ; -.
DR PDBsum; 6S2W; -.
DR AlphaFoldDB; G2TRN4; -.
DR SMR; G2TRN4; -.
DR BioGRID; 4254536; 19.
DR STRING; 4896.SPAC19G12.17.1; -.
DR iPTMnet; G2TRN4; -.
DR MaxQB; G2TRN4; -.
DR PaxDb; G2TRN4; -.
DR EnsemblFungi; SPAC19G12.17.1; SPAC19G12.17.1:pep; SPAC19G12.17.
DR PomBase; SPAC19G12.17; -.
DR VEuPathDB; FungiDB:SPAC19G12.17; -.
DR eggNOG; ENOG502RDB9; Eukaryota.
DR HOGENOM; CLU_2251618_0_0_1; -.
DR InParanoid; G2TRN4; -.
DR OMA; DCVPLVY; -.
DR PRO; PR:G2TRN4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1905754; C:ascospore-type prospore nucleus; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR GO; GO:1990251; C:nuclear exosome focus; IPI:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:PomBase.
DR GO; GO:0140517; F:protein-RNA adaptor activity; IMP:UniProtKB.
DR GO; GO:0033621; P:nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IMP:PomBase.
DR GO; GO:1902801; P:regulation of siRNA-independent facultative heterochromatin assembly; IMP:PomBase.
DR Gene3D; 3.30.2260.10; -; 1.
DR InterPro; IPR035912; EHR_sf.
DR InterPro; IPR000781; ERH.
DR PANTHER; PTHR12373; PTHR12373; 1.
DR Pfam; PF01133; ER; 1.
DR SUPFAM; SSF143875; SSF143875; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..104
FT /note="Enhancer of rudimentary homolog 1"
FT /id="PRO_0000416492"
FT MUTAGEN 11..13
FT /note="ILL->RLR: Abolishes erh1 homodimer formation,
FT abolishes meiRNA dot formation during vegetative growth,
FT increases erh1 protein degradation, interaction with mmi1
FT appears normal, increases levels of several mating and
FT meiosis specific transcripts, decreases mating efficiency."
FT /evidence="ECO:0000269|PubMed:31974447"
FT MUTAGEN 68
FT /note="D->A: Decreases erh1-mmi1 interaction."
FT /evidence="ECO:0000269|PubMed:30651569"
FT STRAND 9..16
FT /evidence="ECO:0007829|PDB:6S2W"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:6AKJ"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:6S2W"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:6S2W"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:6S2W"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:6S2W"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:6S2W"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:6S2W"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6S2W"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:6S2W"
SQ SEQUENCE 104 AA; 12204 MW; 8E9D3A63329B960E CRC64;
MSPPPAESHI ILLIQQGSDP KTRIWSDHCS LRSAIEYIVG VYQTNQAVSE KESIDVSRFF
NFFDEIYDCV PLVYDRHFRA YIPHEKQWLL HHAQEYLTAA RQIP
