NUP42_YEAST
ID NUP42_YEAST Reviewed; 430 AA.
AC P49686; D6VSH5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Nucleoporin NUP42;
DE AltName: Full=Nuclear pore protein NUP42;
GN Name=NUP42; Synonyms=RIP1, UIP1; OrderedLocusNames=YDR192C;
GN ORFNames=YD9346.04C;
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=7634338; DOI=10.1016/0092-8674(95)90438-7;
RA Stutz F., Neville M., Rosbash M.;
RT "Identification of a novel nuclear pore-associated protein as a functional
RT target of the HIV-1 Rev protein in yeast.";
RL Cell 82:495-506(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [5]
RP FUNCTION, AND INTERACTION WITH GLE1.
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 [6]
RP FUNCTION, AND INTERACTION WITH CRM1 AND GFD1.
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 [7]
RP FUNCTION, AND INTERACTION WITH MEX67/MTR2 HETERODIMER.
RX PubMed=10952996; DOI=10.1083/jcb.150.4.695;
RA Straesser K., Bassler J., Hurt E.C.;
RT "Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat
RT nucleoporins is essential for nuclear mRNA export.";
RL J. Cell Biol. 150:695-706(2000).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [9]
RP FUNCTION IN MRNA EXPORT.
RX PubMed=10805742; DOI=10.1128/mcb.20.11.3996-4005.2000;
RA Vainberg I.E., Dower K., Rosbash M.;
RT "Nuclear export of heat shock and non-heat-shock mRNA occurs via similar
RT pathways.";
RL Mol. Cell. Biol. 20:3996-4005(2000).
RN [10]
RP FUNCTION, AND NUCLEOPORIN INTERACTING PROTEINS.
RX PubMed=11387327; DOI=10.1074/jbc.m102629200;
RA Allen N.P., Huang L., Burlingame A., Rexach M.;
RT "Proteomic analysis of nucleoporin interacting proteins.";
RL J. Biol. Chem. 276:29268-29274(2001).
RN [11]
RP FUNCTION, AND AFFINITY GRADIENT FOR KARYOPHERIN KAP95.
RX PubMed=12917401; DOI=10.1074/jbc.m307135200;
RA Pyhtila B., Rexach M.;
RT "A gradient of affinity for the karyopherin Kap95p along the yeast nuclear
RT pore complex.";
RL J. Biol. Chem. 278:42699-42709(2003).
RN [12]
RP FUNCTION, AND FG REPEAT STRUCTURE.
RX PubMed=12604785; DOI=10.1073/pnas.0437902100;
RA Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.;
RT "Disorder in the nuclear pore complex: the FG repeat regions of
RT nucleoporins are natively unfolded.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003).
RN [13]
RP FUNCTION, AND FG REPEATS IN NPC TRANSPORT.
RX PubMed=15039779; DOI=10.1038/ncb1097;
RA Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.;
RT "Minimal nuclear pore complexes define FG repeat domains essential for
RT transport.";
RL Nat. Cell Biol. 6:197-206(2004).
RN [14]
RP REVIEW.
RX PubMed=12791264; DOI=10.1016/s1534-5807(03)00162-x;
RA Suntharalingam M., Wente S.R.;
RT "Peering through the pore: nuclear pore complex structure, assembly, and
RT function.";
RL Dev. Cell 4:775-789(2003).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-298, 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 [16]
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: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. Active directional transport is assured by both, a Phe-Gly
CC (FG) repeat affinity gradient for these transport factors across the
CC NPC and a transport cofactor concentration gradient across the nuclear
CC envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in
CC the nucleus, with GDP in the cytoplasm). NUP42 is specifically
CC important for nuclear protein and mRNA export.
CC {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322,
CC ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:10805742,
CC ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11387327,
CC ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401,
CC ECO:0000269|PubMed:15039779}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC) (PubMed:10684247).
CC NPC constitutes the exclusive means of nucleocytoplasmic transport.
CC NPCs allow the passive diffusion of ions and small molecules and the
CC active, nuclear transport receptor-mediated bidirectional transport of
CC macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and
CC ribosomal subunits across the nuclear envelope. Due to its 8-fold
CC rotational symmetry, all subunits are present with 8 copies or
CC multiples thereof. NUP42 interacts with the NUP82 subcomplex. It
CC interacts directly with GLE1, and through its FG repeats with GFD1, the
CC heterodimeric mRNA transport factor MEX67/MTR2, and the karyopherin
CC CRM1. {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322,
CC ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:10952996}.
CC -!- INTERACTION:
CC P49686; Q12315: GLE1; NbExp=7; IntAct=EBI-12310, EBI-7635;
CC P49686; Q06142: KAP95; NbExp=2; IntAct=EBI-12310, EBI-9145;
CC P49686; Q02629: NUP100; NbExp=2; IntAct=EBI-12310, EBI-11698;
CC P49686; Q02630: NUP116; NbExp=2; IntAct=EBI-12310, EBI-11703;
CC P49686; P48837: NUP57; NbExp=2; IntAct=EBI-12310, EBI-12324;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane
CC protein; Cytoplasmic side.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC FG repeat types and their physico-chemical environment change across
CC the NPC from the nucleoplasmic to the cytoplasmic side: SXFG/PXFG
CC repeats are especially abundant in NUPs on the cytoplasmic side.
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DR EMBL; U30614; AAA87033.1; -; Genomic_DNA.
DR EMBL; Z48784; CAA88706.1; -; Genomic_DNA.
DR EMBL; AY723779; AAU09696.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12035.1; -; Genomic_DNA.
DR PIR; S52700; S52700.
DR RefSeq; NP_010478.3; NM_001180500.3.
DR PDB; 6B4E; X-ray; 1.75 A; C/D=397-430.
DR PDBsum; 6B4E; -.
DR AlphaFoldDB; P49686; -.
DR SMR; P49686; -.
DR BioGRID; 32245; 130.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2313N; -.
DR IntAct; P49686; 17.
DR MINT; P49686; -.
DR STRING; 4932.YDR192C; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P49686; -.
DR MaxQB; P49686; -.
DR PaxDb; P49686; -.
DR PRIDE; P49686; -.
DR EnsemblFungi; YDR192C_mRNA; YDR192C; YDR192C.
DR GeneID; 851774; -.
DR KEGG; sce:YDR192C; -.
DR SGD; S000002600; NUP42.
DR VEuPathDB; FungiDB:YDR192C; -.
DR eggNOG; KOG0845; Eukaryota.
DR HOGENOM; CLU_638015_0_0_1; -.
DR InParanoid; P49686; -.
DR OMA; GTANTMT; -.
DR BioCyc; YEAST:G3O-29780-MON; -.
DR PRO; PR:P49686; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P49686; protein.
DR GO; GO:0005635; C:nuclear envelope; IC:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0044613; C:nuclear pore central transport channel; IDA:SGD.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IGI:SGD.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0071472; P:cellular response to salt stress; IMP:SGD.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IMP:SGD.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IGI:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IGI:SGD.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport.
FT CHAIN 1..430
FT /note="Nucleoporin NUP42"
FT /id="PRO_0000204866"
FT REPEAT 2..5
FT /note="SXFG 1"
FT REPEAT 38..46
FT /note="SAFGXPXFG 1"
FT REPEAT 58..66
FT /note="SAFGXPXFG 2"
FT REPEAT 78..81
FT /note="SXFG 2"
FT REPEAT 90..98
FT /note="SAFGXPXFG 3"
FT REPEAT 112..120
FT /note="SAFGXPXFG 4"
FT REPEAT 124..125
FT /note="FG 1"
FT REPEAT 134..135
FT /note="FG 2"
FT REPEAT 143..151
FT /note="SAFGXPXFG 5"
FT REPEAT 168..171
FT /note="SXFG 3"
FT REPEAT 182..185
FT /note="SXFG 4"
FT REPEAT 200..208
FT /note="SAFGXPXFG 6"
FT REPEAT 215..218
FT /note="SXFG 5"
FT REPEAT 232..235
FT /note="SXFG 6"
FT REPEAT 259..262
FT /note="SXFG 7"
FT REPEAT 277..280
FT /note="SXFG 8"
FT REPEAT 296..297
FT /note="FG 3"
FT REPEAT 312..315
FT /note="SXFG 9"
FT REPEAT 319..322
FT /note="FG 4"
FT REPEAT 339..340
FT /note="FG 5"
FT REPEAT 361..364
FT /note="FG 6"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..230
FT /note="Interactions with CRM1 and GFD1"
FT REGION 180..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..430
FT /note="Interaction with GLE1"
FT /evidence="ECO:0000269|PubMed:10610322"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 331
FT /note="K -> Q (in Ref. 1; AAA87033)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="V -> D (in Ref. 1; AAA87033)"
FT /evidence="ECO:0000305"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 403..410
FT /evidence="ECO:0007829|PDB:6B4E"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:6B4E"
SQ SEQUENCE 430 AA; 42778 MW; 357F94914A5261F4 CRC64;
MSAFGNPFTS GAKPNLSNTS GINPFTNNAA STNNMGGSAF GRPSFGTANT MTGGTTTSAF
GMPQFGTNTG NTGNTSISAF GNTSNAAKPS AFGAPAFGSS APINVNPPST TSAFGAPSFG
STGFGAMAAT SNPFGKSPGS MGSAFGQPAF GANKTAIPSS SVSNSNNSAF GAASNTPLTT
TSPFGSLQQN ASQNASSTSS AFGKPTFGAA TNTQSPFGTI QNTSTSSGTG VSPFGTFGTN
SNNKSPFSNL QSGAGAGSSP FGTTTSKANN NNNVGSSAFG TTNNQSPFSG GSGGTFGSAS
NLNKNTNGNF QSSFGNKGFS FGITPQNDAN KVSQSNPSFG QTMPNTDPNI SLKSNGNATS
FGFGQQQMNA TNVNANTATG KIRFVQGLSS EKDGILELAD LAEETLKIFR ANKFELGLVP
DIPPPPALVA
