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Nucleoporin NUP85 (Nuclear pore protein NUP85)

 NUP85_YEAST             Reviewed;         744 AA.
P46673; D6VWL3;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
12-SEP-2018, entry version 158.
RecName: Full=Nucleoporin NUP85;
AltName: Full=Nuclear pore protein NUP85;
Name=NUP85; Synonyms=RAT9; OrderedLocusNames=YJR042W; ORFNames=J1624;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN NUCLEAR MRNA
EXPORT; NPC ASSEMBLY AND DISTRIBUTION.
STRAIN=ATCC 90840 / EAY235 / FY23;
PubMed=8816998; DOI=10.1091/mbc.7.6.917;
Goldstein A.L., Snay C.A., Heath C.V., Cole C.N.;
"Pleiotropic nuclear defects associated with a conditional allele of
the novel nucleoporin Rat9p/Nup85p.";
Mol. Biol. Cell 7:917-934(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-39; 123-138
AND 708-718, AND NUCLEAR ENVELOPE ORGANIZATION.
PubMed=8565072; DOI=10.1016/S0092-8674(00)80981-2;
Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C.,
Emig S., Segref A., Hurt E.C.;
"A novel complex of nucleoporins, which includes Sec13p and a Sec13p
homolog, is essential for normal nuclear pores.";
Cell 84:265-275(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7668047; DOI=10.1002/yea.320110809;
Huang M.-E., Chuat J.-C., Galibert F.;
"Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA
genes and 14 new open reading frames including a gene most probably
belonging to the family of ubiquitin-protein ligases.";
Yeast 11:775-781(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8641269;
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
X.";
EMBO J. 15:2031-2049(1996).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
FUNCTION, AND INTERACTION WITH MTR2.
PubMed=9774696; DOI=10.1128/MCB.18.11.6826;
Santos-Rosa H., Moreno H., Simos G., Segref A., Fahrenkrog B.,
Pante N., Hurt E.C.;
"Nuclear mRNA export requires complex formation between Mex67p and
Mtr2p at the nuclear pores.";
Mol. Cell. Biol. 18:6826-6838(1998).
[7]
CHARACTERIZATION, AND NPC SUBUNIT LOCATION.
PubMed=10684247; DOI=10.1083/jcb.148.4.635;
Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y.,
Chait B.T.;
"The yeast nuclear pore complex: composition, architecture, and
transport mechanism.";
J. Cell Biol. 148:635-651(2000).
[8]
FUNCTION, AND PRE-RIBOSOME EXPORT.
PubMed=11071906; DOI=10.1091/mbc.11.11.3777;
Stage-Zimmermann T., Schmidt U., Silver P.A.;
"Factors affecting nuclear export of the 60S ribosomal subunit in
vivo.";
Mol. Biol. Cell 11:3777-3789(2000).
[9]
FUNCTION, AND INTERACTION WITH NUP116 GLFG REPEATS.
PubMed=12543930; DOI=10.1074/mcp.T200012-MCP200;
Allen N.P., Patel S.S., Huang L., Chalkley R.J., Burlingame A.,
Lutzmann M., Hurt E.C., Rexach M.;
"Deciphering networks of protein interactions at the nuclear pore
complex.";
Mol. Cell. Proteomics 1:930-946(2002).
[10]
FUNCTION, AND NUP84 NPC SUBCOMPLEX ASSEMBLY/STRUCTURE.
PubMed=11823431; DOI=10.1093/emboj/21.3.387;
Lutzmann M., Kunze R., Buerer A., Aebi U., Hurt E.C.;
"Modular self-assembly of a Y-shaped multiprotein complex from seven
nucleoporins.";
EMBO J. 21:387-397(2002).
[11]
FUNCTION, AND NUCLEAR GSP1 IMPORT.
PubMed=12730220; DOI=10.1074/jbc.M301607200;
Gao H., Sumanaweera N., Bailer S.M., Stochaj U.;
"Nuclear accumulation of the small GTPase Gsp1p depends on
nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-
CoA carboxylase Acc1p.";
J. Biol. Chem. 278:25331-25340(2003).
[12]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[13]
REVIEW.
PubMed=12791264; DOI=10.1016/S1534-5807(03)00162-X;
Suntharalingam M., Wente S.R.;
"Peering through the pore: nuclear pore complex structure, assembly,
and function.";
Dev. Cell 4:775-789(2003).
-!- FUNCTION: Functions as a component of the nuclear pore complex
(NPC). NPC components, collectively referred to as nucleoporins
(NUPs), can play the role of both NPC structural components and of
docking or interaction partners for transiently associated nuclear
transport factors. NUP85 is involved in nuclear poly(A)+ RNA and
pre-ribosome export, in GSP1 nuclear import, in NPC assembly and
distribution, as well as in nuclear envelope organization.
{ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11823431,
ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12730220,
ECO:0000269|PubMed:8816998, ECO:0000269|PubMed:9774696}.
-!- SUBUNIT: The nuclear pore complex (NPC) constitutes the exclusive
means of nucleocytoplasmic transport. NPCs allow the passive
diffusion of ions and small molecules and the active, nuclear
transport receptor-mediated bidirectional transport of
macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs),
and ribosomal subunits across the nuclear envelope. The 55-60 MDa
NPC is composed of at least 31 different subunits: ASM4, CDC31,
GLE1, GLE2, NDC1, NIC96, NSP1, NUP1, NUP2, NUP100, NUP116, NUP120,
NUP133, NUP145, NUP157, NUP159, NUP170, NUP188, NUP192, NUP42,
NUP49, NUP53, NUP57, NUP60, NUP82, NUP84, NUP85, POM152, POM34,
SEC13 and SEH1. Due to its 8-fold rotational symmetry, all
subunits are present with 8 copies or multiples thereof. NUP85 is
part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex
(NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1). NUP85
also interacts directly with the GLFG repeats of NUP116 and
directly or indirectly with the mRNA transport factor MTR2.
{ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:9774696}.
-!- INTERACTION:
Q02629:NUP100; NbExp=4; IntAct=EBI-12345, EBI-11698;
Q02630:NUP116; NbExp=3; IntAct=EBI-12345, EBI-11703;
P35729:NUP120; NbExp=21; IntAct=EBI-12345, EBI-11713;
Q8WUM0:NUP133 (xeno); NbExp=5; IntAct=EBI-12345, EBI-295695;
P49687:NUP145; NbExp=12; IntAct=EBI-12345, EBI-11730;
P53011:SEH1; NbExp=10; IntAct=EBI-12345, EBI-16940;
-!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus
membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus
membrane; Peripheral membrane protein; Nucleoplasmic side.
Note=Symmetric distribution.
-!- MISCELLANEOUS: Present with 7920 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the nucleoporin Nup85 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U36469; AAB48943.1; -; Genomic_DNA.
EMBL; X90995; CAA62481.1; -; Genomic_DNA.
EMBL; L36344; AAA88744.1; -; Genomic_DNA.
EMBL; Z49542; CAA89569.1; -; Genomic_DNA.
EMBL; BK006943; DAA08829.1; -; Genomic_DNA.
PIR; S57061; S57061.
RefSeq; NP_012576.1; NM_001181700.1.
PDB; 3EWE; X-ray; 3.50 A; B/D=1-564.
PDB; 3F3F; X-ray; 2.90 A; C/D/G/H=1-570.
PDB; 3F3G; X-ray; 3.75 A; C/D/G/H=1-570.
PDB; 3F3P; X-ray; 3.20 A; C/D/G/H/K/L=1-570.
PDB; 4XMM; X-ray; 7.38 A; D=44-744.
PDB; 4XMN; X-ray; 7.60 A; D=73-743.
PDBsum; 3EWE; -.
PDBsum; 3F3F; -.
PDBsum; 3F3G; -.
PDBsum; 3F3P; -.
PDBsum; 4XMM; -.
PDBsum; 4XMN; -.
ProteinModelPortal; P46673; -.
SMR; P46673; -.
BioGrid; 33793; 238.
ComplexPortal; CPX-824; Nuclear pore complex.
DIP; DIP-5818N; -.
IntAct; P46673; 22.
MINT; P46673; -.
STRING; 4932.YJR042W; -.
TCDB; 1.I.1.1.1; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; P46673; -.
MaxQB; P46673; -.
PaxDb; P46673; -.
PRIDE; P46673; -.
DNASU; 853499; -.
EnsemblFungi; YJR042W; YJR042W; YJR042W.
GeneID; 853499; -.
KEGG; sce:YJR042W; -.
EuPathDB; FungiDB:YJR042W; -.
SGD; S000003803; NUP85.
HOGENOM; HOG000113893; -.
InParanoid; P46673; -.
KO; K14304; -.
OMA; TNDDIEW; -.
OrthoDB; EOG092C2XAD; -.
BioCyc; YEAST:G3O-31677-MONOMER; -.
EvolutionaryTrace; P46673; -.
PRO; PR:P46673; -.
Proteomes; UP000002311; Chromosome X.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005643; C:nuclear pore; IDA:SGD.
GO; GO:0031080; C:nuclear pore outer ring; IDA:SGD.
GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
GO; GO:0031081; P:nuclear pore distribution; IMP:SGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:SGD.
GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
InterPro; IPR011502; Nucleoporin_Nup85.
PANTHER; PTHR13373; PTHR13373; 1.
Pfam; PF07575; Nucleopor_Nup85; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Membrane;
mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
Reference proteome; Translocation; Transport.
CHAIN 1 744 Nucleoporin NUP85.
/FTId=PRO_0000204885.
COMPBIAS 646 652 Poly-Leu.
CONFLICT 101 101 S -> T (in Ref. 1; AAB48943).
{ECO:0000305}.
CONFLICT 471 471 F -> L (in Ref. 1; AAB48943).
{ECO:0000305}.
STRAND 41 51 {ECO:0000244|PDB:3F3P}.
STRAND 67 74 {ECO:0000244|PDB:3F3F}.
STRAND 77 82 {ECO:0000244|PDB:3F3F}.
STRAND 89 91 {ECO:0000244|PDB:3F3F}.
HELIX 102 117 {ECO:0000244|PDB:3F3F}.
HELIX 119 122 {ECO:0000244|PDB:3F3F}.
HELIX 135 164 {ECO:0000244|PDB:3F3F}.
HELIX 170 189 {ECO:0000244|PDB:3F3F}.
STRAND 190 192 {ECO:0000244|PDB:3F3F}.
HELIX 197 200 {ECO:0000244|PDB:3F3F}.
HELIX 201 215 {ECO:0000244|PDB:3F3F}.
HELIX 221 227 {ECO:0000244|PDB:3F3F}.
STRAND 237 240 {ECO:0000244|PDB:3F3F}.
HELIX 243 254 {ECO:0000244|PDB:3F3F}.
HELIX 258 265 {ECO:0000244|PDB:3F3F}.
TURN 266 271 {ECO:0000244|PDB:3F3F}.
HELIX 272 276 {ECO:0000244|PDB:3F3F}.
HELIX 279 292 {ECO:0000244|PDB:3F3F}.
HELIX 300 318 {ECO:0000244|PDB:3F3F}.
HELIX 326 340 {ECO:0000244|PDB:3F3F}.
HELIX 343 348 {ECO:0000244|PDB:3F3F}.
HELIX 353 363 {ECO:0000244|PDB:3F3F}.
HELIX 368 370 {ECO:0000244|PDB:3F3F}.
HELIX 371 381 {ECO:0000244|PDB:3F3F}.
STRAND 388 390 {ECO:0000244|PDB:3F3F}.
HELIX 391 398 {ECO:0000244|PDB:3F3F}.
HELIX 403 405 {ECO:0000244|PDB:3F3F}.
HELIX 406 412 {ECO:0000244|PDB:3F3F}.
HELIX 414 427 {ECO:0000244|PDB:3F3F}.
STRAND 454 459 {ECO:0000244|PDB:3F3F}.
HELIX 461 474 {ECO:0000244|PDB:3F3F}.
TURN 479 481 {ECO:0000244|PDB:3F3F}.
HELIX 482 491 {ECO:0000244|PDB:3F3F}.
STRAND 493 495 {ECO:0000244|PDB:3F3F}.
HELIX 497 507 {ECO:0000244|PDB:3F3F}.
HELIX 508 510 {ECO:0000244|PDB:3F3F}.
HELIX 516 529 {ECO:0000244|PDB:3F3F}.
HELIX 532 543 {ECO:0000244|PDB:3F3F}.
HELIX 545 548 {ECO:0000244|PDB:3F3F}.
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


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