GenomeNet

Database: UniProt
Entry: P41838
LinkDB: P41838
Original site: P41838 
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   27-MAR-2024, entry version 158.
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}.
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; 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; 284812.P41838; -.
DR   iPTMnet; P41838; -.
DR   SwissPalm; P41838; -.
DR   MaxQB; P41838; -.
DR   PaxDb; 4896-SPBC16A3-05c-1; -.
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-4085377; SUMOylation of SUMOylation 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; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR10971; MRNA EXPORT FACTOR AND BUB3; 1.
DR   PANTHER; PTHR10971:SF11; MRNA EXPORT FACTOR RAE1; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; WD40 repeat-like; 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
//
DBGET integrated database retrieval system