GPN2_YEAST
ID GPN2_YEAST Reviewed; 347 AA.
AC Q08726; D6W2W3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=GPN-loop GTPase 2 {ECO:0000303|PubMed:21532343};
DE EC=3.6.5.- {ECO:0000305};
DE AltName: Full=ATP-binding domain 1 family member B homolog {ECO:0000250|UniProtKB:Q9H9Y4};
GN Name=GPN2 {ECO:0000303|PubMed:21532343};
GN OrderedLocusNames=YOR262W {ECO:0000312|SGD:S000005788};
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=18439903; DOI=10.1016/j.molcel.2008.02.021;
RA Ben-Aroya S., Coombes C., Kwok T., O'Donnell K.A., Boeke J.D., Hieter P.;
RT "Toward a comprehensive temperature-sensitive mutant repository of the
RT essential genes of Saccharomyces cerevisiae.";
RL Mol. Cell 30:248-258(2008).
RN [8]
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 [9]
RP INTERACTION WITH NPA3.
RX PubMed=21844196; DOI=10.1074/jbc.m111.286161;
RA Staresincic L., Walker J., Dirac-Svejstrup A.B., Mitter R., Svejstrup J.Q.;
RT "GTP-dependent binding and nuclear transport of RNA polymerase II by Npa3
RT protein.";
RL J. Biol. Chem. 286:35553-35561(2011).
RN [10]
RP INTERACTION WITH NPA3, AND MUTAGENESIS OF GLU-112.
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 [11]
RP FUNCTION, AND INTERACTION WITH NPA3 AND GPN3.
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 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). Required for
CC establishment of sister chromatid cohesion (PubMed:18439903).
CC {ECO:0000269|PubMed:18439903, ECO:0000269|PubMed:23267056}.
CC -!- SUBUNIT: Heterodimers with NPA3/GPN1 or GPN3 (PubMed:21844196,
CC PubMed:23324351). Binds to RNA polymerase II (RNAPII) (By similarity).
CC {ECO:0000250|UniProtKB:Q9H9Y4, ECO:0000269|PubMed:21844196,
CC ECO:0000269|PubMed:23324351}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14690591}.
CC -!- MISCELLANEOUS: Present with 9230 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR EMBL; Z75170; CAA99484.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11029.1; -; Genomic_DNA.
DR PIR; S67159; S67159.
DR RefSeq; NP_014905.1; NM_001183681.1.
DR AlphaFoldDB; Q08726; -.
DR SMR; Q08726; -.
DR BioGRID; 34652; 296.
DR DIP; DIP-1912N; -.
DR IntAct; Q08726; 12.
DR MINT; Q08726; -.
DR STRING; 4932.YOR262W; -.
DR MaxQB; Q08726; -.
DR PaxDb; Q08726; -.
DR PRIDE; Q08726; -.
DR EnsemblFungi; YOR262W_mRNA; YOR262W; YOR262W.
DR GeneID; 854436; -.
DR KEGG; sce:YOR262W; -.
DR SGD; S000005788; GPN2.
DR VEuPathDB; FungiDB:YOR262W; -.
DR eggNOG; KOG1533; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR HOGENOM; CLU_037460_0_2_1; -.
DR InParanoid; Q08726; -.
DR OMA; YAPLPFN; -.
DR BioCyc; YEAST:G3O-33753-MON; -.
DR PRO; PR:Q08726; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08726; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:SGD.
DR GO; GO:0034087; P:establishment of 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; IPR030231; Gpn2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231; PTHR21231; 1.
DR PANTHER; PTHR21231:SF3; PTHR21231:SF3; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..347
FT /note="GPN-loop GTPase 2"
FT /id="PRO_0000245255"
FT MOTIF 69..71
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 12..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 175..178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 71
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT MUTAGEN 112
FT /note="E->K,A: Impairs heterodimer formation with
FT NPA3/GPN1."
FT /evidence="ECO:0000269|PubMed:23324351"
SQ SEQUENCE 347 AA; 39724 MW; 625CC61455FFA7EC CRC64;
MPFAQIVIGP PGSGKSTYCN GCSQFFNAIG RHSQVVNMDP ANDALPYPCA VDIRDFITLE
EIMQEQQLGP NGGLMYAVES LDNSIDLFIL QIKSLVEEEK AYLVFDCPGQ VELFTHHSSL
FNIFKKMEKE LDIRFCVVNL IDCFYMTSPS QYISILLLAL RSMLMMDLPH INVFSKIDML
KSYGELPFRL DYYTEVQDLD YLEPYIEKEG SSVLGKKYSK LTETIKELVS DFNLVSFEVL
SVDDKESMIN LQGVIDKANG YIFGASEVGG DTVWAEASRE GALIANYDIQ DRWIDNKEKY
DKEEEEKRTA LLKEQELQNK AVDVNEEDEW ENALKEWEEK QGMDFVR
