NUP85_YEAST
ID NUP85_YEAST Reviewed; 744 AA.
AC P46673; D6VWL3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Nucleoporin NUP85;
DE AltName: Full=Nuclear pore protein NUP85;
GN Name=NUP85; Synonyms=RAT9; OrderedLocusNames=YJR042W; ORFNames=J1624;
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 AND DISTRIBUTION.
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=8816998; DOI=10.1091/mbc.7.6.917;
RA Goldstein A.L., Snay C.A., Heath C.V., Cole C.N.;
RT "Pleiotropic nuclear defects associated with a conditional allele of the
RT novel nucleoporin Rat9p/Nup85p.";
RL Mol. Biol. Cell 7:917-934(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-39; 123-138 AND
RP 708-718, 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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7668047; DOI=10.1002/yea.320110809;
RA Huang M.-E., Chuat J.-C., Galibert F.;
RT "Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA
RT genes and 14 new open reading frames including a gene most probably
RT belonging to the family of ubiquitin-protein ligases.";
RL Yeast 11:775-781(1995).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH MTR2.
RX PubMed=9774696; DOI=10.1128/mcb.18.11.6826;
RA Santos-Rosa H., Moreno H., Simos G., Segref A., Fahrenkrog B., Pante N.,
RA Hurt E.C.;
RT "Nuclear mRNA export requires complex formation between Mex67p and Mtr2p at
RT the nuclear pores.";
RL Mol. Cell. Biol. 18:6826-6838(1998).
RN [7]
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 [8]
RP FUNCTION, AND PRE-RIBOSOME EXPORT.
RX PubMed=11071906; DOI=10.1091/mbc.11.11.3777;
RA Stage-Zimmermann T., Schmidt U., Silver P.A.;
RT "Factors affecting nuclear export of the 60S ribosomal subunit in vivo.";
RL Mol. Biol. Cell 11:3777-3789(2000).
RN [9]
RP FUNCTION, AND INTERACTION WITH NUP116 GLFG REPEATS.
RX PubMed=12543930; DOI=10.1074/mcp.t200012-mcp200;
RA Allen N.P., Patel S.S., Huang L., Chalkley R.J., Burlingame A.,
RA Lutzmann M., Hurt E.C., Rexach M.;
RT "Deciphering networks of protein interactions at the nuclear pore
RT complex.";
RL Mol. Cell. Proteomics 1:930-946(2002).
RN [10]
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 [11]
RP FUNCTION, AND NUCLEAR GSP1 IMPORT.
RX PubMed=12730220; DOI=10.1074/jbc.m301607200;
RA Gao H., Sumanaweera N., Bailer S.M., Stochaj U.;
RT "Nuclear accumulation of the small GTPase Gsp1p depends on nucleoporins
RT Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-CoA carboxylase
RT Acc1p.";
RL J. Biol. Chem. 278:25331-25340(2003).
RN [12]
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 [13]
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).
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. NUP85 is involved in nuclear poly(A)+ RNA and pre-ribosome
CC export, in GSP1 nuclear import, in NPC assembly and distribution, as
CC well as in nuclear envelope organization. {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11823431,
CC ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12730220,
CC ECO:0000269|PubMed:8816998, ECO:0000269|PubMed:9774696}.
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 NUP85 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC
CC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1).
CC NUP85 also interacts directly with the GLFG repeats of NUP116 and
CC directly or indirectly with the mRNA transport factor MTR2.
CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:12543930,
CC ECO:0000269|PubMed:9774696}.
CC -!- INTERACTION:
CC P46673; Q02629: NUP100; NbExp=4; IntAct=EBI-12345, EBI-11698;
CC P46673; Q02630: NUP116; NbExp=3; IntAct=EBI-12345, EBI-11703;
CC P46673; P35729: NUP120; NbExp=21; IntAct=EBI-12345, EBI-11713;
CC P46673; P49687: NUP145; NbExp=12; IntAct=EBI-12345, EBI-11730;
CC P46673; P53011: SEH1; NbExp=10; IntAct=EBI-12345, EBI-16940;
CC P46673; Q8WUM0: NUP133; Xeno; NbExp=5; IntAct=EBI-12345, EBI-295695;
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 7920 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nucleoporin Nup85 family. {ECO:0000305}.
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DR EMBL; U36469; AAB48943.1; -; Genomic_DNA.
DR EMBL; X90995; CAA62481.1; -; Genomic_DNA.
DR EMBL; L36344; AAA88744.1; -; Genomic_DNA.
DR EMBL; Z49542; CAA89569.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08829.1; -; Genomic_DNA.
DR PIR; S57061; S57061.
DR RefSeq; NP_012576.1; NM_001181700.1.
DR PDB; 3EWE; X-ray; 3.50 A; B/D=1-564.
DR PDB; 3F3F; X-ray; 2.90 A; C/D/G/H=1-570.
DR PDB; 3F3G; X-ray; 3.75 A; C/D/G/H=1-570.
DR PDB; 3F3P; X-ray; 3.20 A; C/D/G/H/K/L=1-570.
DR PDB; 4XMM; X-ray; 7.38 A; D=44-744.
DR PDB; 4XMN; X-ray; 7.60 A; D=73-743.
DR PDB; 6X08; X-ray; 4.19 A; B=1-564.
DR PDB; 7N84; EM; 11.60 A; b/m=1-744.
DR PDB; 7N9F; EM; 37.00 A; b/i=1-744.
DR PDBsum; 3EWE; -.
DR PDBsum; 3F3F; -.
DR PDBsum; 3F3G; -.
DR PDBsum; 3F3P; -.
DR PDBsum; 4XMM; -.
DR PDBsum; 4XMN; -.
DR PDBsum; 6X08; -.
DR PDBsum; 7N84; -.
DR PDBsum; 7N9F; -.
DR AlphaFoldDB; P46673; -.
DR SMR; P46673; -.
DR BioGRID; 33793; 246.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-5818N; -.
DR IntAct; P46673; 22.
DR MINT; P46673; -.
DR STRING; 4932.YJR042W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P46673; -.
DR MaxQB; P46673; -.
DR PaxDb; P46673; -.
DR PRIDE; P46673; -.
DR ABCD; P46673; 1 sequenced antibody.
DR DNASU; 853499; -.
DR EnsemblFungi; YJR042W_mRNA; YJR042W; YJR042W.
DR GeneID; 853499; -.
DR KEGG; sce:YJR042W; -.
DR SGD; S000003803; NUP85.
DR VEuPathDB; FungiDB:YJR042W; -.
DR eggNOG; KOG2271; Eukaryota.
DR GeneTree; ENSGT00390000000204; -.
DR HOGENOM; CLU_019986_0_0_1; -.
DR InParanoid; P46673; -.
DR OMA; CAKWRLP; -.
DR BioCyc; YEAST:G3O-31677-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; P46673; -.
DR PRO; PR:P46673; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P46673; 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:0031080; C:nuclear pore outer ring; IDA:SGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0051664; P:nuclear pore localization; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR DisProt; DP02156; -.
DR InterPro; IPR011502; Nucleoporin_Nup85.
DR PANTHER; PTHR13373; PTHR13373; 1.
DR Pfam; PF07575; Nucleopor_Nup85; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Translocation; Transport.
FT CHAIN 1..744
FT /note="Nucleoporin NUP85"
FT /id="PRO_0000204885"
FT CONFLICT 101
FT /note="S -> T (in Ref. 1; AAB48943)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="F -> L (in Ref. 1; AAB48943)"
FT /evidence="ECO:0000305"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:3F3P"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 135..164
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 170..189
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:3F3F"
FT TURN 266..271
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 300..318
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 326..340
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 391..398
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 414..427
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 461..474
FT /evidence="ECO:0007829|PDB:3F3F"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 482..491
FT /evidence="ECO:0007829|PDB:3F3F"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 497..507
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 516..529
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 532..543
FT /evidence="ECO:0007829|PDB:3F3F"
FT HELIX 545..548
FT /evidence="ECO:0007829|PDB:3F3F"
SQ SEQUENCE 744 AA; 84898 MW; 4C0A4AD3DB57A023 CRC64;
MTIDDSNRLL MDVDQFDFLD DGTAQLSNNK TDEEEQLYKR DPVSGAILVP MTVNDQPIEK
NGDKMPLKFK LGPLSYQNMA FITAKDKYKL YPVRIPRLDT SKEFSAYVSG LFEIYRDLGD
DRVFNVPTIG VVNSNFAKEH NATVNLAMEA ILNELEVFIG RVKDQDGRVN RFYELEESLT
VLNCLRTMYF ILDGQDVEEN RSEFIESLLN WINRSDGEPD EEYIEQVFSV KDSTAGKKVF
ETQYFWKLLN QLVLRGLLSQ AIGCIERSDL LPYLSDTCAV SFDAVSDSIE LLKQYPKDSS
STFREWKNLV LKLSQAFGSS ATDISGELRD YIEDFLLVIG GNQRKILQYS RTWYESFCGF
LLYYIPSLEL SAEYLQMSLE ANVVDITNDW EQPCVDIISG KIHSILPVME SLDSCTAAFT
AMICEAKGLI ENIFEGEKNS DDYSNEDNEM LEDLFSYRNG MASYMLNSFA FELCSLGDKE
LWPVAIGLIA LSATGTRSAK KMVIAELLPH YPFVTNDDIE WMLSICVEWR LPEIAKEIYT
TLGNQMLSAH NIIESIANFS RAGKYELVKS YSWLLFEASC MEGQKLDDPV LNAIVSKNSP
AEDDVIIPQD ILDCVVTNSM RQTLAPYAVL SQFYELRDRE DWGQALRLLL LLIEFPYLPK
HYLVLLVAKF LYPIFLLDDK KLMDEDSVAT VIEVIETKWD DADEKSSNLY ETIIEADKSL
PSSMATLLKN LRKKLNFKLC QAFM
