GRN1_SCHPO
ID GRN1_SCHPO Reviewed; 470 AA.
AC O74791;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=GTPase grn1 {ECO:0000312|EMBL:CAA21100.1};
DE AltName: Full=GTPase in ribosomal export from the nucleolus protein 1 {ECO:0000303|PubMed:16251348};
DE AltName: Full=Nuclear GTP-binding protein grn1 {ECO:0000250|UniProtKB:P40010};
GN Name=grn1 {ECO:0000312|EMBL:CAA21100.1}; ORFNames=SPBC26H8.08c;
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] {ECO:0000312|EMBL:CAA21100.1}
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 6-LYS--LYS-22;
RP 6-LYS--LYS-36; 60-ILE--GLU-90; 164-ASP--PRO-175; 195-LYS--PRO-208;
RP 276-GLY--SER-283; 326-ASP--GLY-329 AND 405-ALA--GLY-415, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16251348; DOI=10.1091/mbc.e05-09-0848;
RA Du X., Rao M.R.K.S., Chen X.Q., Wu W., Mahalingam S., Balasundaram D.;
RT "The homologous putative GTPases Grn1p from fission yeast and the human
RT GNL3L are required for growth and play a role in processing of nucleolar
RT pre-rRNA.";
RL Mol. Biol. Cell 17:460-474(2006).
RN [3] {ECO:0000305}
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 optimal growth. Required for normal processing
CC of ribosomal pre-rRNA. Required for nuclear export of ribosomal protein
CC rpl2501. {ECO:0000269|PubMed:16251348}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16251348,
CC ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern. {ECO:0000250|UniProtKB:P40010}.
CC -!- DISRUPTION PHENOTYPE: 20-40% of cells exhibit morphogenetic aberrations
CC represented by irregular, uneven, or overdeposition of septum material
CC as well as septation and cell separation defects, often resulting in
CC pseudofilamentous or multiseptated cells, suggesting a failure of
CC cytokinesis in those cells. Cultures of null mutant cells did not
CC appear to exhibit a growth arrest. {ECO:0000269|PubMed:16251348}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; CU329671; CAA21100.1; -; Genomic_DNA.
DR PIR; T40020; T40020.
DR RefSeq; NP_596651.1; NM_001022573.2.
DR AlphaFoldDB; O74791; -.
DR SMR; O74791; -.
DR BioGRID; 276997; 10.
DR STRING; 4896.SPBC26H8.08c.1; -.
DR iPTMnet; O74791; -.
DR MaxQB; O74791; -.
DR PaxDb; O74791; -.
DR PRIDE; O74791; -.
DR EnsemblFungi; SPBC26H8.08c.1; SPBC26H8.08c.1:pep; SPBC26H8.08c.
DR GeneID; 2540469; -.
DR KEGG; spo:SPBC26H8.08c; -.
DR PomBase; SPBC26H8.08c; grn1.
DR VEuPathDB; FungiDB:SPBC26H8.08c; -.
DR eggNOG; KOG2484; Eukaryota.
DR HOGENOM; CLU_011106_5_5_1; -.
DR InParanoid; O74791; -.
DR OMA; FKLDGLW; -.
DR PhylomeDB; O74791; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:O74791; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005525; F:GTP binding; TAS:PomBase.
DR GO; GO:0003924; F:GTPase activity; ISM:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IMP:PomBase.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR014813; Gnl3_N_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF08701; GN3L_Grn1; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Nucleotide-binding; Nucleus; Protein transport;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing;
KW Transport.
FT CHAIN 1..470
FT /note="GTPase grn1"
FT /id="PRO_0000348611"
FT DOMAIN 153..333
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..415
FT /note="RNA-binding"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:16251348"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 202..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P40010, ECO:0000255"
FT BINDING 276..283
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P40010, ECO:0000255"
FT BINDING 326..329
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P40010, ECO:0000255"
FT MUTAGEN 6..36
FT /note="Missing: Fails to localize to the nucleolus."
FT /evidence="ECO:0000269|PubMed:16251348"
FT MUTAGEN 6..22
FT /note="Missing: Fails to localize to the nucleolus."
FT /evidence="ECO:0000269|PubMed:16251348"
FT MUTAGEN 60..90
FT /note="Missing: Fully complements the null mutant. No
FT growth defect. Normal protein level."
FT /evidence="ECO:0000269|PubMed:16251348"
FT MUTAGEN 164..175
FT /note="Missing: Null phenotype. Nuclear/nucleolar border
FT localization consistent with the lack of nucleolar export
FT of pre-ribosomes accompanied by a distortion of nucleolar
FT structure. Extremely low protein level."
FT /evidence="ECO:0000269|PubMed:16251348"
FT MUTAGEN 195..208
FT /note="Missing: Null phenotype. Nuclear/nucleolar border
FT localization consistent with the lack of nucleolar export
FT of pre-ribosomes accompanied by a distortion of nucleolar
FT structure. Extremely low protein level."
FT /evidence="ECO:0000269|PubMed:16251348"
FT MUTAGEN 276..283
FT /note="Missing: Null phenotype. Nuclear/nucleolar border
FT localization consistent with the lack of nucleolar export
FT of pre-ribosomes accompanied by a distortion of nucleolar
FT structure. Extremely low protein level."
FT /evidence="ECO:0000269|PubMed:16251348"
FT MUTAGEN 326..329
FT /note="Missing: Null phenotype. Nuclear/nucleolar border
FT localization consistent with the lack of nucleolar export
FT of pre-ribosomes accompanied by a distortion of nucleolar
FT structure. Extremely low protein level."
FT /evidence="ECO:0000269|PubMed:16251348"
FT MUTAGEN 405..415
FT /note="Missing: Null phenotype. Nuclear/nucleolar border
FT localization consistent with the lack of nucleolar export
FT of pre-ribosomes accompanied by a distortion of nucleolar
FT structure. Extremely low protein level."
FT /evidence="ECO:0000269|PubMed:16251348"
SQ SEQUENCE 470 AA; 52434 MW; 3C97A801C59DE083 CRC64;
MVSLKKKSKR RTTRLRSRIE KKAAESKRKQ KRADKKNPQW KSRIPKDPGI PNSFPYKDKI
LAEIEEQKRI REEEKLARRA SGQVDAAMEE EDAVDENGSL MISKIAEAAQ ASNPDDEEEF
VMEEDNLGEA PLLVDSESYE ASVKADTSRK AYDKEFKKVV EASDVILYVL DARDPEGTRS
KDVERQVLAS SAEEKRLIFV INKIDLVPSE VLNKWVTYLR NFFPTIPMRS ASGSGNSNLK
HQSASASSTI SNLLKSLKSY SAKKKLKSSL TVGVIGYPNV GKSSVINALV NRSANGRSAP
CPAGNVAGMT TSLREVKLDN KLRLVDSPGI VFPSSDSKDD LYRLVMLNAV SSTKVDDPVA
VASYILQFLS RVPGQLERMF QRYELPPLLN TSDIDTATDF LVNIARKRGR LGRGGIPNLN
AAANIVINDW HAGRIEWWAE PEVINEKNSS EVQDTQIVTE WAKEFDLNDF
