RAE1L_MOUSE
ID RAE1L_MOUSE Reviewed; 368 AA.
AC Q8C570; Q3UKD4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=mRNA export factor;
DE AltName: Full=Rae1 protein homolog;
DE AltName: Full=mRNA-associated protein mrnp 41;
GN Name=Rae1; Synonyms=Mrnp41;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Liver, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH NUP98.
RX PubMed=10209021; DOI=10.1083/jcb.145.2.237;
RA Pritchard C.E., Fornerod M., Kasper L.H., van Deursen J.M.;
RT "RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98
RT motif at the nuclear pore complex through multiple domains.";
RL J. Cell Biol. 145:237-254(1999).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in mitotic bipolar spindle formation. Binds
CC mRNA. May function in nucleocytoplasmic transport and in directly or
CC indirectly attaching cytoplasmic mRNPs to the cytoskeleton.
CC {ECO:0000250|UniProtKB:P78406}.
CC -!- SUBUNIT: Interacts with NUMA1 (via N-terminal end of the coiled-coil
CC domain); this interaction promotes spindle formation in mitosis (By
CC similarity). Interacts with NUP98 (PubMed:10209021). Interacts with
CC MYCBP2 (By similarity). Interacts with USP11 (By similarity).
CC {ECO:0000250|UniProtKB:P78406, ECO:0000269|PubMed:10209021}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P78406}. Nucleus
CC {ECO:0000250|UniProtKB:P78406}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:P78406}. Note=Recruited from interphase nuclei
CC to spindle MTs during mitosis. {ECO:0000250|UniProtKB:P78406}.
CC -!- SIMILARITY: Belongs to the WD repeat rae1 family. {ECO:0000305}.
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DR EMBL; AK079383; BAC37627.1; -; mRNA.
DR EMBL; AK146058; BAE26867.1; -; mRNA.
DR EMBL; AK156681; BAE33805.1; -; mRNA.
DR EMBL; BC059051; AAH59051.1; -; mRNA.
DR CCDS; CCDS17138.1; -.
DR RefSeq; NP_780321.1; NM_175112.5.
DR RefSeq; XP_006500086.1; XM_006500023.1.
DR RefSeq; XP_006500087.1; XM_006500024.3.
DR PDB; 7BYF; X-ray; 2.50 A; A/D=24-368.
DR PDBsum; 7BYF; -.
DR AlphaFoldDB; Q8C570; -.
DR SMR; Q8C570; -.
DR BioGRID; 211639; 9.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q8C570; 1.
DR STRING; 10090.ENSMUSP00000029013; -.
DR iPTMnet; Q8C570; -.
DR PhosphoSitePlus; Q8C570; -.
DR EPD; Q8C570; -.
DR MaxQB; Q8C570; -.
DR PaxDb; Q8C570; -.
DR PeptideAtlas; Q8C570; -.
DR PRIDE; Q8C570; -.
DR ProteomicsDB; 253167; -.
DR Antibodypedia; 14158; 289 antibodies from 39 providers.
DR DNASU; 66679; -.
DR Ensembl; ENSMUST00000029013; ENSMUSP00000029013; ENSMUSG00000027509.
DR GeneID; 66679; -.
DR KEGG; mmu:66679; -.
DR UCSC; uc008odg.2; mouse.
DR CTD; 8480; -.
DR MGI; MGI:1913929; Rae1.
DR VEuPathDB; HostDB:ENSMUSG00000027509; -.
DR eggNOG; KOG0647; Eukaryota.
DR GeneTree; ENSGT00950000183091; -.
DR HOGENOM; CLU_038526_1_0_1; -.
DR InParanoid; Q8C570; -.
DR OMA; EAMDQSI; -.
DR OrthoDB; 1048963at2759; -.
DR PhylomeDB; Q8C570; -.
DR TreeFam; TF105481; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR BioGRID-ORCS; 66679; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Rae1; mouse.
DR PRO; PR:Q8C570; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C570; protein.
DR Bgee; ENSMUSG00000027509; Expressed in otic placode and 263 other tissues.
DR ExpressionAtlas; Q8C570; baseline and differential.
DR Genevisible; Q8C570; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10971:SF11; PTHR10971:SF11; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..368
FT /note="mRNA export factor"
FT /id="PRO_0000237586"
FT REPEAT 37..79
FT /note="WD 1"
FT REPEAT 84..114
FT /note="WD 2"
FT REPEAT 125..157
FT /note="WD 3"
FT REPEAT 168..206
FT /note="WD 4"
FT REPEAT 215..255
FT /note="WD 5"
FT REPEAT 271..301
FT /note="WD 6"
FT REPEAT 310..346
FT /note="WD 7"
FT REGION 15..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78406"
FT CONFLICT 232
FT /note="A -> T (in Ref. 1; BAE26867)"
FT /evidence="ECO:0000305"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:7BYF"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:7BYF"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:7BYF"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:7BYF"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:7BYF"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:7BYF"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:7BYF"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:7BYF"
SQ SEQUENCE 368 AA; 40965 MW; 5B1AA677E67F2C85 CRC64;
MSLFGSTSGF GTGGTSMFGS TTTDNHNPMK DIEVTSSPDD SIGCLSFSPP TLPGNFLIAG
SWANDVRCWE VQDSGQTIPK AQQMHTGPVL DVCWSDDGSK VFTASCDKTA KMWDLNSNQA
IQIAQHDAPV KTIHWIKAPN YSCVMTGSWD KTLKFWDTRS SNPMMVLQLP ERCYCADVIY
PMAVVATAER GLIVYQLENQ PSEFRRIESP LKHQHRCVAI FKDKQNKPTG FALGSIEGRV
AIHYINPPNP AKDNFTFKCH RSNGTNTSAP QDIYAVNGIA FHPVHGTLAT VGSDGRFSFW
DKDARTKLKT SEQLDQPIAA CCFNHNGNIF AYASSYDWSK GHEFYNPQKK NYIFLRNAAE
ELKPRNKK
