RED1_SCHPO
ID RED1_SCHPO Reviewed; 712 AA.
AC Q9UTR8; Q9UTX3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=NURS complex subunit red1 {ECO:0000305};
GN Name=red1 {ECO:0000312|PomBase:SPAC1006.03c};
GN Synonyms=iss3 {ECO:0000312|PomBase:SPAC1006.03c};
GN ORFNames=SPAC1006.03c {ECO:0000312|PomBase:SPAC1006.03c};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 238-416, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
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 FUNCTION, REVISION OF GENE MODEL, INTERACTION WITH MMI1; PLA1 AND RRP6,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-637.
RX PubMed=21317872; DOI=10.1038/emboj.2011.32;
RA Sugiyama T., Sugioka-Sugiyama R.;
RT "Red1 promotes the elimination of meiosis-specific mRNAs in vegetatively
RT growing fission yeast.";
RL EMBO J. 30:1027-1039(2011).
RN [5]
RP FUNCTION, 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).
CC -!- FUNCTION: Promotes the exosome-mediated degradation of mRNAs containing
CC a DSR (determinant of selective removal) signal sequence from mitotic
CC cells. {ECO:0000269|PubMed:21317872, ECO:0000269|PubMed:26942678}.
CC -!- SUBUNIT: Interacts with mmi1, pla1 and rrp6.
CC {ECO:0000269|PubMed:21317872}.
CC -!- INTERACTION:
CC Q9UTR8; O74958: mmi1; NbExp=5; IntAct=EBI-1117407, EBI-7997069;
CC Q9UTR8; Q10295: pla1; NbExp=3; IntAct=EBI-1117407, EBI-7997221;
CC Q9UTR8; O13799: SPAC17H9.02; NbExp=4; IntAct=EBI-1117407, EBI-8993901;
CC Q9UTR8; O14269: SPAC7D4.14c; NbExp=3; IntAct=EBI-1117407, EBI-8993923;
CC Q9UTR8; Q9USP9: SPBC902.04; NbExp=3; IntAct=EBI-1117407, EBI-8993741;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:21317872}.
CC Note=Localizes to distinct foci in the nucleus in mitotic cells, which
CC disassemble during meiosis, although the protein is still present.
CC -!- DISRUPTION PHENOTYPE: Cold sensitive (PubMed:26942678). Decreases
CC degradation of mRNA containing a DSR (determinant of selective removal)
CC region (PubMed:26942678). Abnormal meiRNA nuclear dot formation in
CC zygote (PubMed:26942678). meiRNA dot formation in haploid cells
CC (PubMed:26942678). {ECO:0000269|PubMed:26942678}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB60233.2; -; Genomic_DNA.
DR EMBL; AB027946; BAA87250.1; -; Genomic_DNA.
DR RefSeq; NP_594850.2; NM_001020279.2.
DR AlphaFoldDB; Q9UTR8; -.
DR BioGRID; 279682; 255.
DR DIP; DIP-36608N; -.
DR IntAct; Q9UTR8; 24.
DR MINT; Q9UTR8; -.
DR STRING; 4896.SPAC1006.03c.1; -.
DR iPTMnet; Q9UTR8; -.
DR MaxQB; Q9UTR8; -.
DR PaxDb; Q9UTR8; -.
DR PRIDE; Q9UTR8; -.
DR EnsemblFungi; SPAC1006.03c.1; SPAC1006.03c.1:pep; SPAC1006.03c.
DR GeneID; 2543254; -.
DR KEGG; spo:SPAC1006.03c; -.
DR PomBase; SPAC1006.03c; red1.
DR VEuPathDB; FungiDB:SPAC1006.03c; -.
DR eggNOG; KOG4839; Eukaryota.
DR HOGENOM; CLU_393872_0_0_1; -.
DR InParanoid; Q9UTR8; -.
DR OMA; CKYETTG; -.
DR PRO; PR:Q9UTR8; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0071920; C:cleavage body; IDA:PomBase.
DR GO; GO:0000178; C:exosome (RNase complex); 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:1990477; C:MTREC complex; IDA:PomBase.
DR GO; GO:0016604; C:nuclear body; IDA:PomBase.
DR GO; GO:1990251; C:nuclear exosome focus; IDA:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:PomBase.
DR GO; GO:0033621; P:nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IMP:PomBase.
DR GO; GO:1902802; P:regulation of siRNA-dependent facultative heterochromatin assembly; IMP:PomBase.
DR GO; GO:1902801; P:regulation of siRNA-independent facultative heterochromatin assembly; IMP:PomBase.
DR GO; GO:1902794; P:siRNA-independent facultative heterochromatin assembly; IMP:PomBase.
DR GO; GO:0043144; P:sno(s)RNA processing; IMP:PomBase.
DR InterPro; IPR019607; Putative_zinc-finger_domain.
DR InterPro; IPR039278; Red1.
DR PANTHER; PTHR21563; PTHR21563; 1.
DR Pfam; PF10650; zf-C3H1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..712
FT /note="NURS complex subunit red1"
FT /id="PRO_0000362152"
FT ZN_FING 618..639
FT /note="C3H1-type"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..32
FT /evidence="ECO:0000255"
FT COILED 351..379
FT /evidence="ECO:0000255"
FT COILED 471..501
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 637
FT /note="H->I: Reduces the mRNA elimination activity of the
FT protein, but has no impact on localization."
FT /evidence="ECO:0000269|PubMed:21317872"
SQ SEQUENCE 712 AA; 79489 MW; 7386E73363CC1AF6 CRC64;
MSRSINLDEL RKKALESKKK NEEDESNDSD KEDGEISEDD PVIDQSNSVP PMKVPTFPEQ
IPQLPPFDRF PGTNANFFPF GAPFMLPPAL MFGPNTVPFF PQTASSNKTF SKRKRSSENS
FNNRNKAKSS ETSDSSNTSQ SFKENRALKD TATSRPLALS SDTSYQKSEK AKSEKSPFLS
TSKNSDANYS KTTNQKEAEK AVSQLFEVGV RFNDFIAEGI EPSVVHTLFL KLGLDSSSAS
SQGSLTLSAD KAARSAKLRK IDSNLSDTHI LPGDNGTPTV LPERKNLISL PLLKQDDWLS
SSKPFGSSTP NVVIEFDSDD DGDDFSNSKI EQSNLEKPPS NSENGLTMSR SDYLALLRNK
EEEIRRMTKL ILRLESNKKP YRSPTSAADM KLPSVPVAAV DNKSKTHLDT FEKVVDLSSK
ADFVEAGPSI SSSGASSSAA TTNSDTTEQI LEAPWLRKTE QIAVVHEEHP AQIKKSEIDI
LNNLIEKEEG ELTKYQTLVK SKTEILTQLY TRKKQLLEQQ GKGNVACLPK ESDLSMDSIT
EVSAQADENS SQILSSKTSN APNGTTETDF EDKVPLVDYI SPFYRFKSYR FNQQFVERVP
LKYRSLTYSN KIEPMKVFCK YETTGGVCND DHCEASHFRD IKMTDDEIIQ DLSRYIEGND
EIEKESYKSG LDIVMKNTDE NTDFVDVATR IVEYHNLWKS ERMTIPVAKV SI
