GPN3_YEAST
ID GPN3_YEAST Reviewed; 272 AA.
AC Q06543; D6VYP1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=GPN-loop GTPase 3 {ECO:0000303|PubMed:21532343};
DE EC=3.6.5.- {ECO:0000305};
GN Name=GPN3 {ECO:0000303|PubMed:21532343};
GN OrderedLocusNames=YLR243W {ECO:0000312|SGD:S000004233};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
RP GENE NAME.
RX PubMed=21532343; DOI=10.4161/cc.10.11.15763;
RA Alonso B., Chaussinand G., Armengaud J., Godon C.;
RT "A role for GPN-loop GTPase yGPN1 in sister chromatid cohesion.";
RL Cell Cycle 10:1828-1837(2011).
RN [4]
RP FUNCTION, INTERACTION WITH NPA3, AND MUTAGENESIS OF GLU-110.
RX PubMed=23324351; DOI=10.4161/cc.23367;
RA Alonso B., Beraud C., Meguellati S., Chen S.W., Pellequer J.L.,
RA Armengaud J., Godon C.;
RT "Eukaryotic GPN-loop GTPases paralogs use a dimeric assembly reminiscent of
RT archeal GPN.";
RL Cell Cycle 12:463-472(2013).
RN [5]
RP FUNCTION, AND INTERACTION WITH GPN2.
RX PubMed=23267056; DOI=10.1534/genetics.112.148726;
RA Minaker S.W., Filiatrault M.C., Ben-Aroya S., Hieter P., Stirling P.C.;
RT "Biogenesis of RNA polymerases II and III requires the conserved GPN small
RT GTPases in Saccharomyces cerevisiae.";
RL Genetics 193:853-864(2013).
CC -!- FUNCTION: Small GTPase required for proper nuclear localization of RNA
CC polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly
CC step prior to nuclear import (PubMed:23267056). Promotes sister
CC chromatid separation during anaphase (PubMed:23324351).
CC {ECO:0000269|PubMed:23267056, ECO:0000269|PubMed:23324351}.
CC -!- SUBUNIT: Heterodimers with NPA3/GPN1 or GPN2 (PubMed:23324351,
CC PubMed:23267056). Binds to RNA polymerase II (RNAPII) (By similarity).
CC {ECO:0000250|UniProtKB:Q9UHW5, ECO:0000269|PubMed:23267056,
CC ECO:0000269|PubMed:23324351}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR EMBL; U20865; AAB67394.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09557.1; -; Genomic_DNA.
DR PIR; S59389; S59389.
DR RefSeq; NP_013344.1; NM_001182130.1.
DR AlphaFoldDB; Q06543; -.
DR SMR; Q06543; -.
DR BioGRID; 31510; 201.
DR DIP; DIP-1911N; -.
DR IntAct; Q06543; 5.
DR MINT; Q06543; -.
DR STRING; 4932.YLR243W; -.
DR MaxQB; Q06543; -.
DR PaxDb; Q06543; -.
DR PRIDE; Q06543; -.
DR EnsemblFungi; YLR243W_mRNA; YLR243W; YLR243W.
DR GeneID; 850944; -.
DR KEGG; sce:YLR243W; -.
DR SGD; S000004233; GPN3.
DR VEuPathDB; FungiDB:YLR243W; -.
DR eggNOG; KOG1534; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR HOGENOM; CLU_037460_0_0_1; -.
DR InParanoid; Q06543; -.
DR OMA; CFEYLLQ; -.
DR BioCyc; YEAST:G3O-32350-MON; -.
DR PRO; PR:Q06543; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06543; protein.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030228; Gpn3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231; PTHR21231; 1.
DR PANTHER; PTHR21231:SF7; PTHR21231:SF7; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..272
FT /note="GPN-loop GTPase 3"
FT /id="PRO_0000255597"
FT MOTIF 70..72
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 13..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 173..176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 72
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT MUTAGEN 110
FT /note="E->K,A: Impairs heterodimer formation with
FT NPA3/GPN1."
FT /evidence="ECO:0000269|PubMed:23324351"
SQ SEQUENCE 272 AA; 30653 MW; 96E478B8DD5988BB CRC64;
MSRVGVMVLG PAGAGKSTFC NSIISHMQTV GRRAHIVNLD PAAEATKYEF TIDIRDLISL
DDVMEEMDLG PNGALIYCFE YLLKNLDWLD EEIGDFNDEY LIFDCPGQIE LYTHIPVLPN
IVRHLTQQLN FNLCATYLLE APFVIDSSKF FSGALSAMSA MILLELPHIN VLSKLDLIKG
DINKKKLKRF LNPDAMLLME TEGMNQASNP KFLRLNQCIA NLVDDFGMVQ FLPLESNNPD
SIETILSYVD DITQWAEGQE QKEPNDQIDV EE
