NRD1_SCHPO
ID NRD1_SCHPO Reviewed; 529 AA.
AC Q09702;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Negative regulator of differentiation 1;
DE AltName: Full=Multicopy suppressor of sporulation protein msa2;
GN Name=nrd1; Synonyms=msa2; ORFNames=SPAC2F7.11;
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 [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=9671458; DOI=10.1128/mcb.18.8.4488;
RA Tsukahara K., Yamamoto H., Okayama H.;
RT "An RNA binding protein negatively controlling differentiation in fission
RT yeast.";
RL Mol. Cell. Biol. 18:4488-4498(1998).
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 FUNCTION.
RX PubMed=15166138; DOI=10.1534/genetics.167.1.77;
RA Jeong H.T., Ozoe F., Tanaka K., Nakagawa T., Matsuda H., Kawamukai M.;
RT "A novel gene, msa1, inhibits sexual differentiation in Schizosaccharomyces
RT pombe.";
RL Genetics 167:77-91(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Negative regulator of sexual differentiation. Acts by
CC repressing the transcription of meiosis-inducing, ste11-regulated genes
CC until cells reach a critical level of starvation. RNA-binding protein
CC that preferentially binds poly(U). {ECO:0000269|PubMed:15166138}.
CC -!- INTERACTION:
CC Q09702; Q10281: rkp1; NbExp=4; IntAct=EBI-696291, EBI-696304;
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DR EMBL; AF079876; AAC28857.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA90498.1; -; Genomic_DNA.
DR PIR; T38559; S58155.
DR RefSeq; NP_592982.1; NM_001018382.2.
DR PDB; 2RT3; NMR; -; A=188-284.
DR PDBsum; 2RT3; -.
DR AlphaFoldDB; Q09702; -.
DR SMR; Q09702; -.
DR BioGRID; 278249; 17.
DR IntAct; Q09702; 1.
DR STRING; 4896.SPAC2F7.11.1; -.
DR iPTMnet; Q09702; -.
DR MaxQB; Q09702; -.
DR PaxDb; Q09702; -.
DR PRIDE; Q09702; -.
DR EnsemblFungi; SPAC2F7.11.1; SPAC2F7.11.1:pep; SPAC2F7.11.
DR GeneID; 2541755; -.
DR KEGG; spo:SPAC2F7.11; -.
DR PomBase; SPAC2F7.11; nrd1.
DR VEuPathDB; FungiDB:SPAC2F7.11; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_017390_2_1_1; -.
DR InParanoid; Q09702; -.
DR OMA; GPIESAW; -.
DR PhylomeDB; Q09702; -.
DR PRO; PR:Q09702; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0003729; F:mRNA binding; IDA:PomBase.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IDA:PomBase.
DR GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:PomBase.
DR CDD; cd12520; RRM1_MRN1; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR039171; Cwc2/Slt11.
DR InterPro; IPR034195; Mrn1_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR14089; PTHR14089; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..529
FT /note="Negative regulator of differentiation 1"
FT /id="PRO_0000081687"
FT DOMAIN 115..188
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 206..277
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 323..396
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 414..485
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:2RT3"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2RT3"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:2RT3"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:2RT3"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:2RT3"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:2RT3"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:2RT3"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:2RT3"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:2RT3"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2RT3"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:2RT3"
SQ SEQUENCE 529 AA; 57761 MW; 958D8416D07599DD CRC64;
MSSSSPSSQS RLSVPGRTPH LPPLTIPHTV SAEGLATPNT PHALLPTGLL MGSPFVQSPT
SYTSMHGLPF STTQMAAAPA HPTTGYNVSR VTSPNVANFA PGYFPLPNNT TQPVKTVYVG
NLPPNTPIDE ILSCVRTGPI ESAWILPEKN CAFISFLDPS HATAFFQDAA LKRLTIRGTE
VKVGWGKNSA SNSSVLLAVQ QSGACRNVFL GNLPNGITED EIREDLEPFG PIDQIKIVTE
RNIAFVHFLN IAAAIKAVQE LPLNPKWSKR RIYYGRDRCA VGLKQPAYFS KGQVGVVGGY
PVMGYPPPSP VLQKPDLIMT GNRTVYIGNI HADTTIEEIC NAVRGGLLHN IRYLQEKHIC
FVTFVDPVSA FRFFEMSNIH GLVIRNRRLK IGWGKHSGPL PSNIALAVAG GASRNIYIGN
ADDSLTIERL KEDFEEFGEI EYVNFFREKN CAFVNFTSLA SAINAIDRIK QKKGYENYRI
SYGKDRCGNP PRTNSKSDVL SVSSDMSMPV DLVVPQQGIS GFMPTNSNI
