RNA1_SCHPO
ID RNA1_SCHPO Reviewed; 386 AA.
AC P41391;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ran GTPase-activating protein 1;
DE Short=Protein rna1;
GN Name=rna1; ORFNames=SPAC22E12.07;
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 PARTIAL PROTEIN SEQUENCE.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8374168; DOI=10.1091/mbc.4.6.569;
RA Melchior F., Weber K., Gerke V.;
RT "A functional homologue of the RNA1 gene product in Schizosaccharomyces
RT pombe: purification, biochemical characterization, and identification of a
RT leucine-rich repeat motif.";
RL Mol. Biol. Cell 4:569-581(1993).
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 CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=972 / ATCC 24843;
RX PubMed=7878053; DOI=10.1073/pnas.92.5.1749;
RA Bischoff F.R., Krebber H., Kempf T., Hermes I., Ponstingl H.;
RT "Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p
RT involved in mRNA processing and transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1749-1753(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS).
RX PubMed=10394366; DOI=10.1016/s1097-2765(01)80010-1;
RA Hillig R.C., Renault L., Vetter I.R., Drell T. IV, Wittinghofer A.,
RA Becker J.;
RT "The crystal structure of rna1p: a new fold for a GTPase-activating
RT protein.";
RL Mol. Cell 3:781-791(1999).
CC -!- FUNCTION: GTPase activator for the nuclear Ras-related regulatory
CC protein spi1 (Ran), converting it to the putatively inactive GDP-bound
CC state.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region
CC {ECO:0000305}. Note=Possibly enriched in the nuclear periphery.
CC -!- SIMILARITY: Belongs to the RNA1 family. {ECO:0000305}.
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DR EMBL; X69882; CAA49509.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93894.1; -; Genomic_DNA.
DR PIR; S37691; S37691.
DR RefSeq; NP_594833.1; NM_001020262.2.
DR PDB; 1K5D; X-ray; 2.70 A; C/F/I/L=1-386.
DR PDB; 1K5G; X-ray; 3.10 A; C/F/I/L=1-386.
DR PDB; 1YRG; X-ray; 2.66 A; A/B=2-386.
DR PDB; 2CA6; X-ray; 2.20 A; A/B=1-386.
DR PDBsum; 1K5D; -.
DR PDBsum; 1K5G; -.
DR PDBsum; 1YRG; -.
DR PDBsum; 2CA6; -.
DR AlphaFoldDB; P41391; -.
DR SMR; P41391; -.
DR BioGRID; 278353; 16.
DR IntAct; P41391; 1.
DR STRING; 4896.SPAC22E12.07.1; -.
DR iPTMnet; P41391; -.
DR MaxQB; P41391; -.
DR PaxDb; P41391; -.
DR PRIDE; P41391; -.
DR EnsemblFungi; SPAC22E12.07.1; SPAC22E12.07.1:pep; SPAC22E12.07.
DR GeneID; 2541863; -.
DR KEGG; spo:SPAC22E12.07; -.
DR PomBase; SPAC22E12.07; rna1.
DR VEuPathDB; FungiDB:SPAC22E12.07; -.
DR eggNOG; KOG1909; Eukaryota.
DR HOGENOM; CLU_028747_3_0_1; -.
DR InParanoid; P41391; -.
DR OMA; WGVDELD; -.
DR PhylomeDB; P41391; -.
DR Reactome; R-SPO-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-SPO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR EvolutionaryTrace; P41391; -.
DR PRO; PR:P41391; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IDA:PomBase.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IBA:GO_Central.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IDA:PomBase.
DR Gene3D; 3.80.10.10; -; 1.
DR IDEAL; IID50116; -.
DR InterPro; IPR032675; LRR_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; GTPase activation;
KW Leucine-rich repeat; Reference proteome; Repeat.
FT CHAIN 1..386
FT /note="Ran GTPase-activating protein 1"
FT /id="PRO_0000056741"
FT REPEAT 23..48
FT /note="LRR 1"
FT REPEAT 85..112
FT /note="LRR 2"
FT REPEAT 113..141
FT /note="LRR 3"
FT REPEAT 179..206
FT /note="LRR 4"
FT REPEAT 207..235
FT /note="LRR 5"
FT REPEAT 236..264
FT /note="LRR 6"
FT REPEAT 265..293
FT /note="LRR 7"
FT REPEAT 294..322
FT /note="LRR 8"
FT REGION 333..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..375
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 74
FT /note="Critical residue for GTP hydrolysis"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1K5D"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:2CA6"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2CA6"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 135..156
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:2CA6"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2CA6"
FT HELIX 320..332
FT /evidence="ECO:0007829|PDB:2CA6"
SQ SEQUENCE 386 AA; 43236 MW; 8E1C9C506988A7F1 CRC64;
MSRFSIEGKS LKLDAITTED EKSVFAVLLE DDSVKEIVLS GNTIGTEAAR WLSENIASKK
DLEIAEFSDI FTGRVKDEIP EALRLLLQAL LKCPKLHTVR LSDNAFGPTA QEPLIDFLSK
HTPLEHLYLH NNGLGPQAGA KIARALQELA VNKKAKNAPP LRSIICGRNR LENGSMKEWA
KTFQSHRLLH TVKMVQNGIR PEGIEHLLLE GLAYCQELKV LDLQDNTFTH LGSSALAIAL
KSWPNLRELG LNDCLLSARG AAAVVDAFSK LENIGLQTLR LQYNEIELDA VRTLKTVIDE
KMPDLLFLEL NGNRFSEEDD VVDEIREVFS TRGRGELDEL DDMEELTDEE EEDEEEEAES
QSPEPETSEE EKEDKELADE LSKAHI
