GPN1_YEAST
ID GPN1_YEAST Reviewed; 385 AA.
AC P47122; D6VWP2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=GPN-loop GTPase 1 {ECO:0000303|PubMed:21532343};
DE EC=3.6.5.- {ECO:0000305|PubMed:21844196};
DE AltName: Full=Essential PCL1-interacting ATPase 1 {ECO:0000303|PubMed:15082539};
DE AltName: Full=GPN-loop GTPase NPA3 {ECO:0000305};
DE AltName: Full=Nucleolar preribosomal-associated protein 3 {ECO:0000303|PubMed:15226434};
GN Name=NPA3 {ECO:0000303|PubMed:15226434};
GN Synonyms=EPA1 {ECO:0000303|PubMed:15082539},
GN GPN1 {ECO:0000303|PubMed:21532343};
GN OrderedLocusNames=YJR072C {ECO:0000312|SGD:S000003833}; ORFNames=J1821;
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 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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=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 [5]
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 [6]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH PCL1.
RX PubMed=15082539; DOI=10.1534/genetics.166.3.1177;
RA Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr.;
RT "The identification of Pcl1-interacting proteins that genetically interact
RT with Cla4 may indicate a link between G1 progression and mitotic exit.";
RL Genetics 166:1177-1186(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15226434; DOI=10.1128/mcb.24.14.6324-6337.2004;
RA Dez C., Froment C., Noaillac-Depeyre J., Monsarrat B.,
RA Caizergues-Ferrer M., Henry Y.;
RT "Npa1p, a component of very early pre-60S ribosomal particles, associates
RT with a subset of small nucleolar RNPs required for peptidyl transferase
RT center modification.";
RL Mol. Cell. Biol. 24:6324-6337(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313 AND SER-352, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-308; SER-313 AND
RP SER-352, AND IDENTIFICATION BY 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).
RN [10]
RP FUNCTION, AND BINDING TO RNA POYMERASE II.
RX PubMed=20855544; DOI=10.1074/mcp.m110.003616;
RA Forget D., Lacombe A.A., Cloutier P., Al-Khoury R., Bouchard A.,
RA Lavallee-Adam M., Faubert D., Jeronimo C., Blanchette M., Coulombe B.;
RT "The protein interaction network of the human transcription machinery
RT reveals a role for the conserved GTPase RPAP4/GPN1 and microtubule assembly
RT in nuclear import and biogenesis of RNA polymerase II.";
RL Mol. Cell. Proteomics 9:2827-2839(2010).
RN [11]
RP FUNCTION.
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 [12]
RP FUNCTION, BINDING TO RNA POYMERASE II, INTERACTION WITH NUP133 AND CRM1,
RP AND MUTAGENESIS OF ASP-106 AND GLN-110.
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 [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-369, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [14]
RP INTERACTION WITH GPN2 AND GPN3, 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 [15]
RP 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 import of RNA
CC polymerase II (RNAPII) (PubMed:20855544, PubMed:21844196). May act at
CC an RNAP assembly step prior to nuclear import (PubMed:23267056).
CC Promotes sister chromatid separation during anaphase (PubMed:21532343).
CC {ECO:0000269|PubMed:15082539, ECO:0000269|PubMed:20855544,
CC ECO:0000269|PubMed:21532343, ECO:0000269|PubMed:21844196,
CC ECO:0000305|PubMed:23267056}.
CC -!- SUBUNIT: Heterodimers with GPN2 or GPN3 (PubMed:23324351,
CC PubMed:23267056). Binds to RNA polymerase II (RNAPII) in a GTP-
CC dependent manner (PubMed:20855544, PubMed:21844196). Interacts with
CC nuclear pore protein NUP133 and nuclear export factor CRM1
CC (PubMed:21844196). Interacts with PCL1 (PubMed:15082539).
CC {ECO:0000269|PubMed:15082539, ECO:0000269|PubMed:20855544,
CC ECO:0000269|PubMed:21844196, ECO:0000269|PubMed:23267056,
CC ECO:0000269|PubMed:23324351}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15226434}.
CC -!- PTM: Phosphorylated by the cyclin-CDK PCL1-PHO85.
CC {ECO:0000269|PubMed:15082539}.
CC -!- MISCELLANEOUS: Present with 15200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR EMBL; Z49572; CAA89600.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39297.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08858.1; -; Genomic_DNA.
DR PIR; S57091; S57091.
DR RefSeq; NP_012606.3; NM_001181730.3.
DR PDB; 5HCI; X-ray; 2.30 A; A/B/C/D/E/F=2-264.
DR PDB; 5HCN; X-ray; 2.20 A; A=2-264.
DR PDBsum; 5HCI; -.
DR PDBsum; 5HCN; -.
DR AlphaFoldDB; P47122; -.
DR SMR; P47122; -.
DR BioGRID; 33828; 103.
DR DIP; DIP-1676N; -.
DR IntAct; P47122; 75.
DR MINT; P47122; -.
DR STRING; 4932.YJR072C; -.
DR iPTMnet; P47122; -.
DR MaxQB; P47122; -.
DR PaxDb; P47122; -.
DR PRIDE; P47122; -.
DR EnsemblFungi; YJR072C_mRNA; YJR072C; YJR072C.
DR GeneID; 853535; -.
DR KEGG; sce:YJR072C; -.
DR SGD; S000003833; NPA3.
DR VEuPathDB; FungiDB:YJR072C; -.
DR eggNOG; KOG1532; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR HOGENOM; CLU_037460_1_2_1; -.
DR InParanoid; P47122; -.
DR OMA; MIIVFNK; -.
DR BioCyc; YEAST:G3O-31704-MON; -.
DR PRO; PR:P47122; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47122; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA: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; IPR030230; Gpn1/Npa3/XAB1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231; PTHR21231; 1.
DR PANTHER; PTHR21231:SF8; PTHR21231:SF8; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..385
FT /note="GPN-loop GTPase 1"
FT /id="PRO_0000203101"
FT REGION 317..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 70..72
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT COMPBIAS 327..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 369
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 106
FT /note="D->A: Impairs nuclear localization of RNAPII.
FT Completely abolishes RNAPII binding."
FT /evidence="ECO:0000269|PubMed:21844196"
FT MUTAGEN 110
FT /note="Q->L: Impairs nuclear localization of RNAPII, but
FT does not impair RNAPII binding."
FT /evidence="ECO:0000269|PubMed:21844196"
FT MUTAGEN 112
FT /note="E->K: Impairs heterodimer formation with GPN2 and
FT GPN3."
FT /evidence="ECO:0000269|PubMed:23324351"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5HCN"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:5HCN"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5HCN"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5HCN"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:5HCN"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:5HCI"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:5HCN"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:5HCN"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:5HCN"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:5HCN"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:5HCN"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:5HCN"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:5HCN"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:5HCN"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:5HCN"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5HCN"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:5HCN"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:5HCN"
FT HELIX 216..231
FT /evidence="ECO:0007829|PDB:5HCN"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:5HCN"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5HCN"
FT HELIX 245..262
FT /evidence="ECO:0007829|PDB:5HCN"
SQ SEQUENCE 385 AA; 43195 MW; EA271D14EA1FFAEF CRC64;
MSLSTIICIG MAGSGKTTFM QRLNSHLRAE KTPPYVINLD PAVLRVPYGA NIDIRDSIKY
KKVMENYQLG PNGAIVTSLN LFSTKIDQVI RLVEQKKDKF QNCIIDTPGQ IECFVWSASG
AIITESFASS FPTVIAYIVD TPRNSSPTTF MSNMLYACSI LYKTKLPMIV VFNKTDVCKA
DFAKEWMTDF ESFQAAIKED QDLNGDNGLG SGYMSSLVNS MSLMLEEFYS QLDVVGVSSF
TGDGFDEFMQ CVDKKVDEYD QYYKQEREKA LNLKKKKEEM RKQKSLNGLM KDLGLNEKSS
AAASDNDSID AISDLEEDAN DGLVDRDEDE GVEREYTFPG EERTKGEVNE NSAPDLQRRY
QEAMQQVGKT ASSETAENIA KYIRN