RAE1_SCHPO
ID RAE1_SCHPO Reviewed; 352 AA.
AC P41838;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Poly(A)+ RNA export protein;
GN Name=rae1; ORFNames=SPBC16A3.05c;
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], AND MUTAGENESIS OF GLY-219.
RX PubMed=7706287; DOI=10.1074/jbc.270.13.7411;
RA Brown J.A., Bharathi A., Ghosh A., Whalen W., Fitzgerald E., Dhar R.;
RT "A mutation in the Schizosaccharomyces pombe rae1 gene causes defects in
RT poly(A)+ RNA export and in the cytoskeleton.";
RL J. Biol. Chem. 270:7411-7419(1995).
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=9301023;
RX DOI=10.1002/(sici)1097-0061(19970930)13:12<1167::aid-yea154>3.0.co;2-o;
RA Whalen W.A., Bharathi A., Danielewicz D., Dhar R.;
RT "Advancement through mitosis requires rae1 gene function in fission
RT yeast.";
RL Yeast 13:1167-1179(1997).
RN [4]
RP FUNCTION, AND INTERACTION WITH RPN15 AND UAP56.
RX PubMed=15990877; DOI=10.1038/sj.emboj.7600713;
RA Thakurta A.G., Gopal G., Yoon J.H., Kozak L., Dhar R.;
RT "Homolog of BRCA2-interacting Dss1p and Uap56p link Mlo3p and Rae1p for
RT mRNA export in fission yeast.";
RL EMBO J. 24:2512-2523(2005).
RN [5]
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: Required for mitotic cell growth as well as for spore
CC germination. Functions in cell cycle progression through trafficking of
CC proteins required for mitosis. Has a role in the mRNA export process.
CC {ECO:0000269|PubMed:15990877, ECO:0000269|PubMed:9301023}.
CC -!- SUBUNIT: Interacts with rpn15/dss1 and uap56.
CC {ECO:0000269|PubMed:15990877}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC Note=Nuclear periphery.
CC -!- SIMILARITY: Belongs to the WD repeat rae1 family. {ECO:0000305}.
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DR EMBL; U14951; AAA86311.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA16856.1; -; Genomic_DNA.
DR PIR; A56119; A56119.
DR RefSeq; NP_596784.1; NM_001023805.2.
DR AlphaFoldDB; P41838; -.
DR SMR; P41838; -.
DR BioGRID; 276293; 18.
DR DIP; DIP-59117N; -.
DR IntAct; P41838; 1.
DR STRING; 4896.SPBC16A3.05c.1; -.
DR SwissPalm; P41838; -.
DR MaxQB; P41838; -.
DR PaxDb; P41838; -.
DR EnsemblFungi; SPBC16A3.05c.1; SPBC16A3.05c.1:pep; SPBC16A3.05c.
DR GeneID; 2539741; -.
DR KEGG; spo:SPBC16A3.05c; -.
DR PomBase; SPBC16A3.05c; rae1.
DR VEuPathDB; FungiDB:SPBC16A3.05c; -.
DR eggNOG; KOG0647; Eukaryota.
DR HOGENOM; CLU_038526_1_0_1; -.
DR InParanoid; P41838; -.
DR OMA; EAMDQSI; -.
DR PhylomeDB; P41838; -.
DR Reactome; R-SPO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-SPO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-SPO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SPO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SPO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR PRO; PR:P41838; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IGI:PomBase.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:PomBase.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; ISO:PomBase.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037631; Gle2/RAE1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10971:SF11; PTHR10971:SF11; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..352
FT /note="Poly(A)+ RNA export protein"
FT /id="PRO_0000051182"
FT REPEAT 28..58
FT /note="WD 1"
FT REPEAT 72..102
FT /note="WD 2"
FT REPEAT 113..146
FT /note="WD 3"
FT REPEAT 192..229
FT /note="WD 4"
FT REPEAT 252..282
FT /note="WD 5"
FT MUTAGEN 219
FT /note="G->E: Temperature-sensitive mutant that accumulates
FT poly(A)+ RNA in the nucleus."
FT /evidence="ECO:0000269|PubMed:7706287"
SQ SEQUENCE 352 AA; 38626 MW; 42612491181751F4 CRC64;
MSLFGQATTS TVSNATGDLK KDVEVAQPPE DSISDLAFSP QAEYLAASSW DSKVRIYEVQ
ATGQSIGKAL YEHQGPVLSV NWSRDGTKVA SGSVDKSAKV FDIQTGQNQQ VAAHDDAVRC
VRFVEAMGTS PILATGSWDK TLKYWDLRQS TPIATVSLPE RVYAMDCVHP LLTVATAERN
ICVINLSEPT KIFKLAMSPL KFQTRSLACF IKGDGYAIGS VEGRCAIQNI DEKNASQNFS
FRCHRNQAGN SADVYSVNSI AFHPQYGTFS TAGSDGTFSF WDKDSHQRLK SYPNVGGTIS
CSTFNRTGDI FAYAISYDWS KGYTFNNAQL PNKIMLHPVP QDEIKPRPKK GR
