NUP84_YEAST
ID NUP84_YEAST Reviewed; 726 AA.
AC P52891; D6VRN4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Nucleoporin NUP84;
DE AltName: Full=Nuclear pore protein NUP84;
GN Name=NUP84; OrderedLocusNames=YDL116W;
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], AND FUNCTION IN NUCLEAR MRNA EXPORT; NPC
RP ASSEMBLY; NPC DISTRIBUTION AND NUCLEAR ENVELOPE ORGANIZATION.
RX PubMed=8565072; DOI=10.1016/s0092-8674(00)80981-2;
RA Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C.,
RA Emig S., Segref A., Hurt E.C.;
RT "A novel complex of nucleoporins, which includes Sec13p and a Sec13p
RT homolog, is essential for normal nuclear pores.";
RL Cell 84:265-275(1996).
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 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 [5]
RP FUNCTION, AND NUP84 NPC SUBCOMPLEX ASSEMBLY/STRUCTURE.
RX PubMed=11823431; DOI=10.1093/emboj/21.3.387;
RA Lutzmann M., Kunze R., Buerer A., Aebi U., Hurt E.C.;
RT "Modular self-assembly of a Y-shaped multiprotein complex from seven
RT nucleoporins.";
RL EMBO J. 21:387-397(2002).
RN [6]
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 [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 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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. NUP84 is involved in nuclear poly(A)+ RNA export, in NPC
CC assembly and distribution, as well as in nuclear envelope organization.
CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11823431,
CC ECO:0000269|PubMed:8565072}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope. Due to its 8-fold rotational
CC symmetry, all subunits are present with 8 copies or multiples thereof.
CC NUP84 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC
CC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1).
CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11823431}.
CC -!- INTERACTION:
CC P52891; Q02629: NUP100; NbExp=2; IntAct=EBI-12337, EBI-11698;
CC P52891; P35729: NUP120; NbExp=12; IntAct=EBI-12337, EBI-11713;
CC P52891; P49687: NUP145; NbExp=17; IntAct=EBI-12337, EBI-11730;
CC P52891; P52891: NUP84; NbExp=3; IntAct=EBI-12337, EBI-12337;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane
CC protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane
CC protein; Nucleoplasmic side. Note=Symmetric distribution.
CC -!- MISCELLANEOUS: Present with 8580 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Nup84/Nup107 nucleoporin family.
CC {ECO:0000305}.
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DR EMBL; X90993; CAA62479.1; -; Genomic_DNA.
DR EMBL; Z74164; CAA98684.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11744.1; -; Genomic_DNA.
DR PIR; S62180; S62180.
DR RefSeq; NP_010167.1; NM_001180175.1.
DR PDB; 3IKO; X-ray; 3.20 A; C/F/I=1-460.
DR PDB; 3JRO; X-ray; 4.00 A; C=1-424.
DR PDB; 4XMM; X-ray; 7.38 A; F=1-451.
DR PDB; 4XMN; X-ray; 7.60 A; F=2-451.
DR PDB; 6X02; X-ray; 6.38 A; A=1-726.
DR PDB; 6X03; X-ray; 7.30 A; A=1-726.
DR PDB; 7N84; EM; 11.60 A; f/q=1-726.
DR PDB; 7N9F; EM; 37.00 A; f/m=1-726.
DR PDBsum; 3IKO; -.
DR PDBsum; 3JRO; -.
DR PDBsum; 4XMM; -.
DR PDBsum; 4XMN; -.
DR PDBsum; 6X02; -.
DR PDBsum; 6X03; -.
DR PDBsum; 7N84; -.
DR PDBsum; 7N9F; -.
DR AlphaFoldDB; P52891; -.
DR SMR; P52891; -.
DR BioGRID; 31946; 355.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2430N; -.
DR IntAct; P52891; 41.
DR MINT; P52891; -.
DR STRING; 4932.YDL116W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P52891; -.
DR MaxQB; P52891; -.
DR PaxDb; P52891; -.
DR PRIDE; P52891; -.
DR DNASU; 851441; -.
DR EnsemblFungi; YDL116W_mRNA; YDL116W; YDL116W.
DR GeneID; 851441; -.
DR KEGG; sce:YDL116W; -.
DR SGD; S000002274; NUP84.
DR VEuPathDB; FungiDB:YDL116W; -.
DR eggNOG; KOG1964; Eukaryota.
DR GeneTree; ENSGT00390000012080; -.
DR HOGENOM; CLU_023045_0_0_1; -.
DR InParanoid; P52891; -.
DR OMA; MAHIVLF; -.
DR BioCyc; YEAST:G3O-29516-MON; -.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR EvolutionaryTrace; P52891; -.
DR PRO; PR:P52891; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P52891; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
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:0031080; C:nuclear pore outer ring; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IMP:SGD.
DR GO; GO:0051664; P:nuclear pore localization; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:SGD.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IDA:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0034398; P:telomere tethering at nuclear periphery; IMP:SGD.
DR InterPro; IPR007252; Nup84/Nup107.
DR PANTHER; PTHR13003; PTHR13003; 1.
DR Pfam; PF04121; Nup84_Nup100; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..726
FT /note="Nucleoporin NUP84"
FT /id="PRO_0000204884"
FT COILED 563..583
FT /evidence="ECO:0000255"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 36..55
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 61..87
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 171..189
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:3IKO"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:3IKO"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3IKO"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:3IKO"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 282..304
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 336..340
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 344..351
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 383..399
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 406..422
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 437..441
FT /evidence="ECO:0007829|PDB:3IKO"
SQ SEQUENCE 726 AA; 83635 MW; F45BAAF9B976EEFE CRC64;
MELSPTYQTE RFTKFSDTLK EFKIEQNNEQ NPIDPFNIIR EFRSAAGQLA LDLANSGDES
NVISSKDWEL EARFWHLVEL LLVFRNADLD LDEMELHPYN SRGLFEKKLM QDNKQLYQIW
IVMVWLKENT YVMERPKNVP TSKWLNSITS GGLKSCDLDF PLRENTNVLD VKDKEEDHIF
FKYIYELILA GAIDEALEEA KLSDNISICM ILCGIQEYLN PVIDTQIANE FNTQQGIKKH
SLWRRTVYSL SQQAGLDPYE RAIYSYLSGA IPNQEVLQYS DWESDLHIHL NQILQTEIEN
YLLENNQVGT DELILPLPSH ALTVQEVLNR VASRHPSESE HPIRVLMASV ILDSLPSVIH
SSVEMLLDVV KGTEASNDII DKPYLLRIVT HLAICLDIIN PGSVEEVDKS KLITTYISLL
KLQGLYENIP IYATFLNESD CLEACSFILS SLEDPQVRKK QIETINFLRL PASNILRRTT
QRVFDETEQE YSPSNEISIS FDVNNIDMHL IYGVEWLIEG KLYVDAVHSI IALSRRFLLN
GRVKALEQFM ERNNIGEICK NYELEKIADN ISKDENEDQF LEEITQYEHL IKGIREYEEW
QKSVSLLSSE SNIPTLIEKL QGFSKDTFEL IKTFLVDLTS SNFADSADYE ILYEIRALYT
PFLLMELHKK LVEAAKLLKI PKFISEALAF TSLVANENDK IYLLFQSSGK LKEYLDLVAR
TATLSN
