RNA1_YEAST
ID RNA1_YEAST Reviewed; 407 AA.
AC P11745; D6W061;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Ran GTPase-activating protein 1;
DE AltName: Full=Protein involved in RNA production/processing;
GN Name=RNA1; OrderedLocusNames=YMR235C; ORFNames=YM9959.17C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX PubMed=2674676; DOI=10.1128/mcb.9.7.2989-2999.1989;
RA Traglia H.M., Atkinson N.S., Hopper A.K.;
RT "Structural and functional analyses of Saccharomyces cerevisiae wild-type
RT and mutant RNA1 genes.";
RL Mol. Cell. Biol. 9:2989-2999(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SL560-3A;
RA Koh S.S., Young S.R., Young H.S., Hyen S.K.;
RL Submitted (DEC-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 188-407.
RC STRAIN=ATCC 204510 / AB320;
RA Crouch R.J.;
RL Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DOMAINS LEUCINE-RICH REPEATS.
RX PubMed=1603072; DOI=10.1007/bf00587594;
RA Schneider R., Schweiger M.;
RT "The yeast RNA1 protein, necessary for RNA processing, is homologous to the
RT human ribonuclease/angiogenin inhibitor (RAI).";
RL Mol. Gen. Genet. 233:315-318(1992).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: GTPase activator for the nuclear Ras-related regulatory
CC protein GSP1 (Ran), converting it to the putatively inactive GDP-bound
CC state.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISRUPTION PHENOTYPE: Causes conditional lethality. Strains bearing
CC this mutation do not grow at temperatures exceeding 30 degrees Celsius.
CC {ECO:0000269|PubMed:2674676}.
CC -!- MISCELLANEOUS: Present with 52200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNA1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35248.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M27143; AAA34985.1; -; Genomic_DNA.
DR EMBL; M27142; AAA34983.1; -; Genomic_DNA.
DR EMBL; X17376; CAA35248.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z49939; CAA90206.1; -; Genomic_DNA.
DR EMBL; X57160; CAA40449.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10135.1; -; Genomic_DNA.
DR PIR; A32492; BVBYN1.
DR RefSeq; NP_013962.1; NM_001182742.1.
DR AlphaFoldDB; P11745; -.
DR SMR; P11745; -.
DR BioGRID; 35413; 701.
DR DIP; DIP-2509N; -.
DR IntAct; P11745; 12.
DR MINT; P11745; -.
DR STRING; 4932.YMR235C; -.
DR iPTMnet; P11745; -.
DR MaxQB; P11745; -.
DR PaxDb; P11745; -.
DR PRIDE; P11745; -.
DR EnsemblFungi; YMR235C_mRNA; YMR235C; YMR235C.
DR GeneID; 855275; -.
DR KEGG; sce:YMR235C; -.
DR SGD; S000004848; RNA1.
DR VEuPathDB; FungiDB:YMR235C; -.
DR eggNOG; KOG1909; Eukaryota.
DR GeneTree; ENSGT00440000039203; -.
DR HOGENOM; CLU_028747_3_0_1; -.
DR InParanoid; P11745; -.
DR OMA; WGVDELD; -.
DR BioCyc; YEAST:G3O-32916-MON; -.
DR Reactome; R-SCE-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-SCE-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:P11745; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P11745; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0031267; F:small GTPase binding; IDA:SGD.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IDA:SGD.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IMP:SGD.
DR GO; GO:0006404; P:RNA import into nucleus; IMP:SGD.
DR GO; GO:0006407; P:rRNA export from nucleus; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13516; LRR_6; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Leucine-rich repeat; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..407
FT /note="Ran GTPase-activating protein 1"
FT /id="PRO_0000056742"
FT REPEAT 11..39
FT /note="LRR 1"
FT REPEAT 40..67
FT /note="LRR 2"
FT REPEAT 68..101
FT /note="LRR 3"
FT REPEAT 102..133
FT /note="LRR 4"
FT REPEAT 134..166
FT /note="LRR 5"
FT REPEAT 167..197
FT /note="LRR 6"
FT REPEAT 198..226
FT /note="LRR 7"
FT REPEAT 227..256
FT /note="LRR 8"
FT REPEAT 257..285
FT /note="LRR 9"
FT REPEAT 286..315
FT /note="LRR 10"
FT REPEAT 316..346
FT /note="LRR 11"
FT REGION 353..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT VARIANT 17
FT /note="S -> F (in mutant RNA1-1)"
FT VARIANT 194
FT /note="A -> V (in mutant RNA1-1)"
FT CONFLICT 42
FT /note="K -> E (in Ref. 2; CAA35248)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="L -> S (in Ref. 5; CAA40449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 45816 MW; D77029B6783FFF09 CRC64;
MATLHFVPQH EEEQVYSISG KALKLTTSDD IKPYLEELAA LKTCTKLDLS GNTIGTEASE
ALAKCIAENT QVRESLVEVN FADLYTSRLV DEVVDSLKFL LPVLLKCPHL EIVNLSDNAF
GLRTIELLED YIAHAVNIKH LILSNNGMGP FAGERIGKAL FHLAQNKKAA SKPFLETFIC
GRNRLENGSA VYLALGLKSH SEGLKVVKLY QNGIRPKGVA TLIHYGLQYL KNLEILDLQD
NTFTKHASLI LAKALPTWKD SLFELNLNDC LLKTAGSDEV FKVFTEVKFP NLHVLKFEYN
EMAQETIEVS FLPAMEKGNL PELEKLEING NRLDEDSDAL DLLQSKFDDL EVDDFEEVDS
EDEEGEDEED EDEDEKLEEI ETERLEKELL EVQVDDLAER LAETEIK
