MOG1_YEAST
ID MOG1_YEAST Reviewed; 218 AA.
AC P47123; D6VWP4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Nuclear import protein MOG1;
DE AltName: Full=Multicopy suppressor of GSP1;
GN Name=MOG1; OrderedLocusNames=YJR074W; ORFNames=J1827;
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], FUNCTION, INTERACTION WITH GSP1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9860978; DOI=10.1073/pnas.95.26.15388;
RA Oki M., Nishimoto T.;
RT "A protein required for nuclear-protein import, Mog1p, directly interacts
RT with GTP-Gsp1p, the Saccharomyces cerevisiae ran homologue.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15388-15393(1998).
RN [2]
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 [3]
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 [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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11509570; DOI=10.1074/jbc.m106060200;
RA Baker R.P., Harreman M.T., Eccleston J.F., Corbett A.H., Stewart M.;
RT "Interaction between Ran and Mog1 is required for efficient nuclear protein
RT import.";
RL J. Biol. Chem. 276:41255-41262(2001).
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 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-218.
RX PubMed=10860733; DOI=10.1006/jmbi.2000.3733;
RA Stewart M., Baker R.P.;
RT "1.9-A resolution crystal structure of the Saccharomyces cerevisiae Ran-
RT binding protein Mog1p.";
RL J. Mol. Biol. 299:213-223(2000).
CC -!- FUNCTION: Involved in the Ran-GTPase system for nuclear protein import
CC and poly(A)+ mRNA export. {ECO:0000269|PubMed:11509570,
CC ECO:0000269|PubMed:9860978}.
CC -!- SUBUNIT: Interacts with GSP1. {ECO:0000269|PubMed:9860978}.
CC -!- INTERACTION:
CC P47123; P32836: GSP2; NbExp=3; IntAct=EBI-11145, EBI-7934;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11509570,
CC ECO:0000269|PubMed:9860978}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MOG1 family. {ECO:0000305}.
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DR EMBL; AB015285; BAA28825.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39299.1; -; Genomic_DNA.
DR EMBL; Z49574; CAA89602.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08860.1; -; Genomic_DNA.
DR PIR; S57093; S57093.
DR RefSeq; NP_012608.1; NM_001181732.1.
DR PDB; 1EQ6; X-ray; 1.90 A; A=30-218.
DR PDB; 1JHS; X-ray; 1.90 A; A=31-218.
DR PDBsum; 1EQ6; -.
DR PDBsum; 1JHS; -.
DR AlphaFoldDB; P47123; -.
DR SMR; P47123; -.
DR BioGRID; 33830; 1082.
DR DIP; DIP-1356N; -.
DR IntAct; P47123; 6.
DR MINT; P47123; -.
DR STRING; 4932.YJR074W; -.
DR iPTMnet; P47123; -.
DR MaxQB; P47123; -.
DR PaxDb; P47123; -.
DR PRIDE; P47123; -.
DR EnsemblFungi; YJR074W_mRNA; YJR074W; YJR074W.
DR GeneID; 853537; -.
DR KEGG; sce:YJR074W; -.
DR SGD; S000003835; MOG1.
DR VEuPathDB; FungiDB:YJR074W; -.
DR eggNOG; KOG3329; Eukaryota.
DR GeneTree; ENSGT00390000013834; -.
DR HOGENOM; CLU_081345_1_0_1; -.
DR InParanoid; P47123; -.
DR OMA; QEVWIDK; -.
DR BioCyc; YEAST:G3O-31705-MON; -.
DR EvolutionaryTrace; P47123; -.
DR PRO; PR:P47123; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47123; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IDA:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR CDD; cd00224; Mog1; 1.
DR InterPro; IPR007681; Mog1.
DR InterPro; IPR016123; Mog1/PsbP_a/b/a-sand.
DR PANTHER; PTHR15837; PTHR15837; 1.
DR Pfam; PF04603; Mog1; 1.
DR SUPFAM; SSF55724; SSF55724; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA transport; Nucleus; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..218
FT /note="Nuclear import protein MOG1"
FT /id="PRO_0000215203"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1EQ6"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1EQ6"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1EQ6"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1EQ6"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1EQ6"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1EQ6"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1EQ6"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1EQ6"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:1EQ6"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1EQ6"
FT STRAND 117..129
FT /evidence="ECO:0007829|PDB:1EQ6"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1EQ6"
FT STRAND 133..143
FT /evidence="ECO:0007829|PDB:1EQ6"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:1EQ6"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1EQ6"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:1EQ6"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:1EQ6"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:1EQ6"
FT HELIX 193..207
FT /evidence="ECO:0007829|PDB:1EQ6"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1EQ6"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1EQ6"
SQ SEQUENCE 218 AA; 24307 MW; 980156FF01A1542D CRC64;
MKIEKASHIS QPVQLSTCTL IDTYPGHQGS MNNKEVELYG GAITTVVPPG FIDASTLREV
PDTQEVYVNS RRDEEEFEDG LATNESIIVD LLETVDKSDL KEAWQFHVED LTELNGTTKW
EALQEDTVQQ GTKFTGLVME VANKWGKPDL AQTVVIGVAL IRLTQFDTDV VISINVPLTK
EEASQASNKE LPARCHAVYQ LLQEMVRKFH VVDTSLFA
