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GSP2_YEAST
ID   GSP2_YEAST              Reviewed;         220 AA.
AC   P32836; D6W2P1;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=GTP-binding nuclear protein GSP2/CNR2;
GN   Name=GSP2; Synonyms=CNR2; OrderedLocusNames=YOR185C;
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].
RX   PubMed=8455603; DOI=10.1128/mcb.13.4.2152-2161.1993;
RA   Belhumeur P., Lee A., Tam R., Dipaolo T., Fortin N., Clark M.W.;
RT   "GSP1 and GSP2, genetic suppressors of the prp20-1 mutant in Saccharomyces
RT   cerevisiae: GTP-binding proteins involved in the maintenance of nuclear
RT   organization.";
RL   Mol. Cell. Biol. 13:2152-2161(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7687541; DOI=10.1002/j.1460-2075.1993.tb05955.x;
RA   Kadowaki T., Goldfarb D., Spitz L.M., Tartakoff A.M., Ohno M.;
RT   "Regulation of RNA processing and transport by a nuclear guanine nucleotide
RT   release protein and members of the Ras superfamily.";
RL   EMBO J. 12:2929-2937(1993).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
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).
CC   -!- FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport.
CC       Required for the import of protein into the nucleus and also for RNA
CC       export. Not essential for cell viability.
CC   -!- SUBUNIT: Found in a nuclear export complex with RanGTP, exportin and
CC       pre-miRNA (By similarity). {ECO:0000250|UniProtKB:P62825}.
CC   -!- INTERACTION:
CC       P32836; P47123: MOG1; NbExp=3; IntAct=EBI-7934, EBI-11145;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: GSP2 expression exhibits carbon source dependency.
CC   -!- MISCELLANEOUS: Present with 2460 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC       {ECO:0000305}.
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DR   EMBL; L08691; AAA34654.1; -; Genomic_DNA.
DR   EMBL; X71946; CAA50748.1; -; Genomic_DNA.
DR   EMBL; Z75093; CAA99394.1; -; Genomic_DNA.
DR   EMBL; AY693117; AAT93136.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10957.1; -; Genomic_DNA.
DR   PIR; S35505; S35505.
DR   RefSeq; NP_014828.1; NM_001183604.1.
DR   AlphaFoldDB; P32836; -.
DR   SMR; P32836; -.
DR   BioGRID; 34580; 112.
DR   DIP; DIP-1357N; -.
DR   IntAct; P32836; 17.
DR   MINT; P32836; -.
DR   STRING; 4932.YOR185C; -.
DR   BindingDB; P32836; -.
DR   iPTMnet; P32836; -.
DR   MaxQB; P32836; -.
DR   PaxDb; P32836; -.
DR   PRIDE; P32836; -.
DR   EnsemblFungi; YOR185C_mRNA; YOR185C; YOR185C.
DR   GeneID; 854357; -.
DR   KEGG; sce:YOR185C; -.
DR   SGD; S000005711; GSP2.
DR   VEuPathDB; FungiDB:YOR185C; -.
DR   eggNOG; KOG0096; Eukaryota.
DR   GeneTree; ENSGT00940000153786; -.
DR   HOGENOM; CLU_041217_13_0_1; -.
DR   InParanoid; P32836; -.
DR   OMA; TIVFHRK; -.
DR   BioCyc; YEAST:G3O-33695-MON; -.
DR   PRO; PR:P32836; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P32836; protein.
DR   GO; GO:0005737; C:cytoplasm; ISA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISA:SGD.
DR   GO; GO:0006997; P:nucleus organization; IGI:SGD.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; ISA:SGD.
DR   GO; GO:0006606; P:protein import into nucleus; ISA:SGD.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002041; Ran_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   PANTHER; PTHR24071; PTHR24071; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00627; GTPRANTC4.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51418; RAN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P32835"
FT   CHAIN           2..220
FT                   /note="GTP-binding nuclear protein GSP2/CNR2"
FT                   /id="PRO_0000208734"
FT   BINDING         21..28
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62825"
FT   BINDING         71
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62825"
FT   BINDING         125..128
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62825"
FT   BINDING         153..155
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62825"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32835"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32835"
SQ   SEQUENCE   220 AA;  24991 MW;  402EEE0F140B37A1 CRC64;
     MSAPAQNNAE VPTFKLVLVG DGGTGKTTFV KRHLTGEFEK KYIATIGVEV HPLSFYTNFG
     EIKFDVWDTA GQEKFGGLRD GYYINAQCAI IMFDVTSRIT YKNVPNWHRD LVRVCENIPI
     VLCGNKVDVK ERKVKAKTIT FHRKKNLQYY DISAKSNYNF EKPFLWLARK LAGNPQLEFV
     ASPALAPPEV QVDEQLMHQY QQEMDQATAL PLPDEDDADL
 
 
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