P46673 (NUP85_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleoporin NUP85

Alternative name(s):
Nuclear pore protein NUP85

Gene names

Name:	NUP85
Synonyms:	RAT9
Ordered Locus Names:	YJR042W
ORF Names:	J1624

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	744 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11
Subunit structure	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, SEH1 and SEC1. 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. Ref.6 Ref.7 Ref.9
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. Ref.12
Sequence similarities	Belongs to the nucleoporin Nup85 family.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Membrane Nuclear pore complex Nucleus
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	NLS-bearing substrate import into nucleus Traceable author statement. Source: SGD mRNA export from nucleus Inferred from mutant phenotype. Source: SGD mRNA-binding (hnRNP) protein import into nucleus Traceable author statement. Source: SGD nuclear envelope organization Inferred from mutant phenotype. Source: SGD nuclear pore organization Traceable author statement. Source: SGD protein export from nucleus Traceable author statement. Source: SGD rRNA export from nucleus Traceable author statement. Source: SGD ribosomal large subunit export from nucleus Inferred from mutant phenotype Ref.8. Source: SGD ribosomal protein import into nucleus Traceable author statement. Source: SGD snRNA export from nucleus Traceable author statement. Source: SGD snRNP protein import into nucleus Traceable author statement. Source: SGD tRNA export from nucleus Traceable author statement. Source: SGD
Cellular component	Nup107-160 complex Inferred from direct assay Ref.10. Source: SGD nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct structural molecule activity Traceable author statement. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NUP145	P49687	3	EBI-12345,EBI-11730
SEH1	P53011	5	EBI-12345,EBI-16940

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 744

744

Nucleoporin NUP85

PRO_0000204885

Regions

Compositional bias

646 – 652

7

Poly-Leu

Experimental info

Sequence conflict

101

1

S → T in AAB48943. Ref.1

Sequence conflict

471

1

F → L in AAB48943. Ref.1

Secondary structure

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744

Helix Strand Turn

Details...

Beta strand

67 – 71

5

Beta strand

77 – 82

6

Beta strand

89 – 91

3

Helix

102 – 108

7

Helix

112 – 117

6

Helix

135 – 158

24

Turn

162 – 164

3

Helix

170 – 189

20

Helix

197 – 200

4

Helix

201 – 215

15

Helix

221 – 227

7

Helix

243 – 254

12

Helix

258 – 261

4

Turn

266 – 271

6

Helix

272 – 276

5

Helix

279 – 292

14

Helix

300 – 316

17

Helix

328 – 338

11

Helix

343 – 348

6

Helix

353 – 357

5

Turn

361 – 364

4

Helix

368 – 370

3

Helix

371 – 381

11

Beta strand

388 – 390

3

Helix

391 – 398

8

Helix

403 – 405

3

Helix

406 – 412

7

Helix

414 – 426

13

Beta strand

454 – 457

4

Helix

462 – 474

13

Turn

479 – 481

3

Helix

482 – 485

4

Turn

489 – 491

3

Helix

497 – 507

11

Helix

508 – 510

3

Helix

516 – 529

14

Helix

532 – 541

10

Sequences

	Sequence		Length	Mass (Da)
	P46673 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 4C0A4AD3DB57A023	FASTA	744	84,898
	10 20 30 40 50 60 MTIDDSNRLL MDVDQFDFLD DGTAQLSNNK TDEEEQLYKR DPVSGAILVP MTVNDQPIEK 70 80 90 100 110 120 NGDKMPLKFK LGPLSYQNMA FITAKDKYKL YPVRIPRLDT SKEFSAYVSG LFEIYRDLGD 130 140 150 160 170 180 DRVFNVPTIG VVNSNFAKEH NATVNLAMEA ILNELEVFIG RVKDQDGRVN RFYELEESLT 190 200 210 220 230 240 VLNCLRTMYF ILDGQDVEEN RSEFIESLLN WINRSDGEPD EEYIEQVFSV KDSTAGKKVF 250 260 270 280 290 300 ETQYFWKLLN QLVLRGLLSQ AIGCIERSDL LPYLSDTCAV SFDAVSDSIE LLKQYPKDSS 310 320 330 340 350 360 STFREWKNLV LKLSQAFGSS ATDISGELRD YIEDFLLVIG GNQRKILQYS RTWYESFCGF 370 380 390 400 410 420 LLYYIPSLEL SAEYLQMSLE ANVVDITNDW EQPCVDIISG KIHSILPVME SLDSCTAAFT 430 440 450 460 470 480 AMICEAKGLI ENIFEGEKNS DDYSNEDNEM LEDLFSYRNG MASYMLNSFA FELCSLGDKE 490 500 510 520 530 540 LWPVAIGLIA LSATGTRSAK KMVIAELLPH YPFVTNDDIE WMLSICVEWR LPEIAKEIYT 550 560 570 580 590 600 TLGNQMLSAH NIIESIANFS RAGKYELVKS YSWLLFEASC MEGQKLDDPV LNAIVSKNSP 610 620 630 640 650 660 AEDDVIIPQD ILDCVVTNSM RQTLAPYAVL SQFYELRDRE DWGQALRLLL LLIEFPYLPK 670 680 690 700 710 720 HYLVLLVAKF LYPIFLLDDK KLMDEDSVAT VIEVIETKWD DADEKSSNLY ETIIEADKSL 730 740 PSSMATLLKN LRKKLNFKLC QAFM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p." Goldstein A.L., Snay C.A., Heath C.V., Cole C.N. Mol. Biol. Cell 7:917-934(1996) [PubMed: 8816998] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN NUCLEAR MRNA EXPORT; NPC ASSEMBLY AND DISTRIBUTION. Strain: ATCC 90840 / EAY235 / FY23.
[2]	"A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores." Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C., Emig S., Segref A., Hurt E.C. Cell 84:265-275(1996) [PubMed: 8565072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-39; 123-138 AND 708-718, NUCLEAR ENVELOPE ORGANIZATION.
[3]	"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." Huang M.-E., Chuat J.-C., Galibert F. Yeast 11:775-781(1995) [PubMed: 7668047] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." 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. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Nuclear mRNA export requires complex formation between Mex67p and Mtr2p at the nuclear pores." Santos-Rosa H., Moreno H., Simos G., Segref A., Fahrenkrog B., Pante N., Hurt E.C. Mol. Cell. Biol. 18:6826-6838(1998) [PubMed: 9774696] [Abstract] Cited for: FUNCTION, INTERACTION WITH MTR2.
[7]	"The yeast nuclear pore complex: composition, architecture, and transport mechanism." Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T. J. Cell Biol. 148:635-651(2000) [PubMed: 10684247] [Abstract] Cited for: CHARACTERIZATION, NPC SUBUNIT LOCATION.
[8]	"Factors affecting nuclear export of the 60S ribosomal subunit in vivo." Stage-Zimmermann T., Schmidt U., Silver P.A. Mol. Biol. Cell 11:3777-3789(2000) [PubMed: 11071906] [Abstract] Cited for: FUNCTION, PRE-RIBOSOME EXPORT.
[9]	"Deciphering networks of protein interactions at the nuclear pore complex." Allen N.P., Patel S.S., Huang L., Chalkley R.J., Burlingame A., Lutzmann M., Hurt E.C., Rexach M. Mol. Cell. Proteomics 1:930-946(2002) [PubMed: 12543930] [Abstract] Cited for: FUNCTION, INTERACTION WITH NUP116 GLFG REPEATS.
[10]	"Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins." Lutzmann M., Kunze R., Buerer A., Aebi U., Hurt E.C. EMBO J. 21:387-397(2002) [PubMed: 11823431] [Abstract] Cited for: FUNCTION, NUP84 NPC SUBCOMPLEX ASSEMBLY/STRUCTURE.
[11]	"Nuclear accumulation of the small GTPase Gsp1p depends on nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-CoA carboxylase Acc1p." Gao H., Sumanaweera N., Bailer S.M., Stochaj U. J. Biol. Chem. 278:25331-25340(2003) [PubMed: 12730220] [Abstract] Cited for: FUNCTION, NUCLEAR GSP1 IMPORT.
[12]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]	"Peering through the pore: nuclear pore complex structure, assembly, and function." Suntharalingam M., Wente S.R. Dev. Cell 4:775-789(2003) [PubMed: 12791264] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U36469 Genomic DNA. Translation: AAB48943.1.
X90995 Genomic DNA. Translation: CAA62481.1.
L36344 Genomic DNA. Translation: AAA88744.1.
Z49542 Genomic DNA. Translation: CAA89569.1.
BK006943 Genomic DNA. Translation: DAA08829.1.

PIR

S57061.

RefSeq

NP_012576.1. NM_001181700.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EWE	X-ray	3.50	B/D	1-564	[»]
3F3F	X-ray	2.90	C/D/G/H	1-570	[»]
3F3G	X-ray	3.75	C/D/G/H	1-570	[»]
3F3P	X-ray	3.20	C/D/G/H/K/L	1-570	[»]

ProteinModelPortal

P46673.

SMR

P46673. Positions 44-549.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5818N.

IntAct

P46673. 22 interactions.

MINT

MINT-648452.

STRING

P46673.

Protein family/group databases

TCDB

9.A.14.1.1. nuclear pore complex (NPC) family.

Proteomic databases

PeptideAtlas

P46673.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YJR042W; YJR042W; YJR042W.

GeneID

853499.

KEGG

sce:YJR042W.

NMPDR

fig|4932.3.peg.3550.

Organism-specific databases

CYGD

YJR042w.

SGD

S000003803. NUP85.

Phylogenomic databases

eggNOG

fuNOG04459.

GeneTree

EFGT00050000008623.

HOGENOM

HBG202237.

OMA

TNDDIEW.

OrthoDB

EOG4N33Z1.

Gene expression databases

ArrayExpress

P46673.

Genevestigator

P46673.

GermOnline

YJR042W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011502. Nucleoporin_Nup85.
[Graphical view]

Pfam

PF07575. Nucleopor_Nup85. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

974140.

Entry information

Entry name

NUP85_YEAST

Accession

Primary (citable) accession number: P46673
Secondary accession number(s): D6VWL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program