GFD1_YEAST
ID GFD1_YEAST Reviewed; 188 AA.
AC Q04839; D6W081;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=mRNA transport factor GFD1;
DE AltName: Full=Good for full DBP5 activity protein 1;
GN Name=GFD1; OrderedLocusNames=YMR255W; ORFNames=YM9920.09;
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=9698782; DOI=10.1590/s0100-879x1998000300004;
RA Nobrega M.P., Graminha M.A., Troitskaya E.N., Nobrega F.G.;
RT "Study of a region on yeast chromosome XIII that complements pet G199
RT mutants (COX7) and carries a new non-essential gene.";
RL Braz. J. Med. Biol. Res. 31:355-363(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 FUNCTION, AND INTERACTION WITH GLE1 AND NUP42.
RX PubMed=10610322; DOI=10.1093/emboj/18.20.5761;
RA Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M.,
RA Stutz F.;
RT "The RNA export factor Gle1p is located on the cytoplasmic fibrils of the
RT NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box
RT protein Rat8p/Dbp5p and a new protein Ymr255p.";
RL EMBO J. 18:5761-5777(1999).
RN [5]
RP FUNCTION, INTERACTION WITH DBP5, AND SUBCELLULAR LOCATION.
RX PubMed=10523319; DOI=10.1093/emboj/18.20.5778;
RA Hodge C.A., Colot H.V., Stafford P., Cole C.N.;
RT "Rat8p/Dbp5p is a shuttling transport factor that interacts with
RT Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1
RT cells.";
RL EMBO J. 18:5778-5788(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH NAB2.
RX PubMed=15208322; DOI=10.1074/jbc.m402044200;
RA Suntharalingam M., Alcazar-Roman A.R., Wente S.R.;
RT "Nuclear export of the yeast mRNA-binding protein Nab2 is linked to a
RT direct interaction with Gfd1 and to Gle1 function.";
RL J. Biol. Chem. 279:35384-35391(2004).
RN [7]
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 [8]
RP INTERACTION WITH ZDS1.
RX PubMed=15619606; DOI=10.1074/jbc.m413025200;
RA Estruch F., Hodge C.A., Rodriguez-Navarro S., Cole C.N.;
RT "Physical and genetic interactions link the yeast protein Zds1p with mRNA
RT nuclear export.";
RL J. Biol. Chem. 280:9691-9697(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-106 AND SER-111, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-106, 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 [12]
RP 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).
CC -!- FUNCTION: High-copy suppressor of mutant alleles of ATP-dependent RNA
CC helicase DBP5, which is involved in mRNA export from the nucleus. It
CC may also play an important role in a late stage of NAB2-mRNA export.
CC {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322,
CC ECO:0000269|PubMed:15208322}.
CC -!- SUBUNIT: Interacts with GLE1, NUP42, NAB2, ZDS1 and probably DBP5.
CC Forms a complex with GLE1 and NAB2. {ECO:0000269|PubMed:10523319,
CC ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:15208322,
CC ECO:0000269|PubMed:15619606}.
CC -!- INTERACTION:
CC Q04839; P20449: DBP5; NbExp=2; IntAct=EBI-27549, EBI-5617;
CC Q04839; P32505: NAB2; NbExp=7; IntAct=EBI-27549, EBI-11770;
CC Q04839; P50111: ZDS1; NbExp=3; IntAct=EBI-27549, EBI-29626;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10523319}. Nucleus,
CC nuclear pore complex {ECO:0000269|PubMed:10523319}. Nucleus membrane
CC {ECO:0000269|PubMed:10523319}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10523319}; Cytoplasmic side
CC {ECO:0000269|PubMed:10523319}.
CC -!- MISCELLANEOUS: Present with 2733 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; AF007064; AAC50003.1; -; Genomic_DNA.
DR EMBL; Z48639; CAA88582.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10155.1; -; Genomic_DNA.
DR PIR; S53077; S53077.
DR RefSeq; NP_013982.1; NM_001182762.1.
DR PDB; 3LCN; X-ray; 2.00 A; C/D=123-151.
DR PDBsum; 3LCN; -.
DR AlphaFoldDB; Q04839; -.
DR SMR; Q04839; -.
DR BioGRID; 35433; 61.
DR DIP; DIP-1254N; -.
DR IntAct; Q04839; 9.
DR MINT; Q04839; -.
DR STRING; 4932.YMR255W; -.
DR iPTMnet; Q04839; -.
DR MaxQB; Q04839; -.
DR PaxDb; Q04839; -.
DR PRIDE; Q04839; -.
DR EnsemblFungi; YMR255W_mRNA; YMR255W; YMR255W.
DR GeneID; 855297; -.
DR KEGG; sce:YMR255W; -.
DR SGD; S000004868; GFD1.
DR VEuPathDB; FungiDB:YMR255W; -.
DR eggNOG; ENOG502SDHJ; Eukaryota.
DR HOGENOM; CLU_1442138_0_0_1; -.
DR InParanoid; Q04839; -.
DR OMA; ESKWADA; -.
DR BioCyc; YEAST:G3O-32931-MON; -.
DR EvolutionaryTrace; Q04839; -.
DR PRO; PR:Q04839; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04839; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IGI:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR IDEAL; IID50178; -.
DR InterPro; IPR020401; mRNA_transport_factor_GFD1.
DR Pfam; PF17331; GFD1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..188
FT /note="mRNA transport factor GFD1"
FT /id="PRO_0000087477"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..164
FT /evidence="ECO:0000255"
FT COMPBIAS 42..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT HELIX 127..149
FT /evidence="ECO:0007829|PDB:3LCN"
SQ SEQUENCE 188 AA; 21571 MW; 6C835BD4BD048EB9 CRC64;
MPLESIWADA PDEEPIKKQK PSHKRSNNNK KNNNSRWSNE SSSNNKKKDS VNKVKNNKGN
HESKTKNKIK ETLPREKKPP HSQGKISPVS ESLAINPFSQ KATEISPPPV SPSKMKTTKT
QSKQDTASKM KLLKKKIEEQ REILQKTHHK NQQQQVLMDF LNDEGSSNWV DDDEEELILQ
RLKTSLKI
