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P20676

- NUP1_YEAST

UniProt

P20676 - NUP1_YEAST

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Protein

Nucleoporin NUP1

Gene

NUP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP1 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP2 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP1 binds through its C-terminus to KAP95, thus accelerating the release of KAP95 and, indirectly, of the nuclear localization signal (NLS)-containing cargo from the SRP1-KAP95-cargo complex.9 Publications

GO - Molecular functioni

  1. nucleocytoplasmic transporter activity Source: SGD
  2. structural constituent of nuclear pore Source: SGD

GO - Biological processi

  1. NLS-bearing protein import into nucleus Source: SGD
  2. poly(A)+ mRNA export from nucleus Source: SGD
  3. protein import into nucleus Source: SGD
  4. ribosomal large subunit export from nucleus Source: SGD
  5. transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33631-MONOMER.

Protein family/group databases

TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NUP1
Alternative name(s):
Nuclear pore protein NUP1
Gene namesi
Name:NUP1
Ordered Locus Names:YOR098C
ORF Names:YOR3182C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOR098c.
SGDiS000005624. NUP1.

Subcellular locationi

GO - Cellular componenti

  1. nuclear pore Source: SGD
  2. nuclear pore central transport channel Source: SGD
  3. nuclear pore nuclear basket Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10761075Nucleoporin NUP1PRO_0000204902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei54 – 541Phosphoserine1 Publication
Modified residuei161 – 1611Phosphoserine1 Publication
Modified residuei381 – 3811Phosphothreonine1 Publication
Modified residuei383 – 3831Phosphoserine1 Publication
Modified residuei637 – 6371Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by CDC28.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP20676.
PaxDbiP20676.

Expressioni

Gene expression databases

GenevestigatoriP20676.

Interactioni

Subunit structurei

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. Interacts through its FG repeats with nuclear transport receptors. Binds to the nuclear basket of the NPC through NUP60. Interacts with KAP122.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KAP95Q061426EBI-12392,EBI-9145

Protein-protein interaction databases

BioGridi34496. 69 interactions.
DIPiDIP-81N.
IntActiP20676. 47 interactions.
MINTiMINT-1759946.
STRINGi4932.YOR098C.

Structurei

Secondary structure

1
1076
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1004 – 10063
Turni1007 – 10093

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BPTX-ray1.99B974-1012[»]
4C31X-ray3.00C/F/X/Y322-355[»]
4MBEX-ray2.61G/H/X/Y316-340[»]
ProteinModelPortaliP20676.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati336 – 3383FXF 1
Repeati384 – 3863FXF 2
Repeati406 – 4094FXFG 1
Repeati422 – 4254FXFG 2
Repeati448 – 4514FXFG 3
Repeati484 – 4874FXFG 4
Repeati510 – 5134FXFG 5
Repeati525 – 5284FXFG 6
Repeati543 – 5464FXFG 7
Repeati571 – 5744FXFG 8
Repeati591 – 5933FXF 3
Repeati614 – 6163FXF 4
Repeati636 – 6383FXF 5
Repeati657 – 6593FXF 6
Repeati671 – 6744FXFG 9
Repeati689 – 6913FXF 7
Repeati708 – 7114FXFG 10
Repeati727 – 7304FXFG 11
Repeati753 – 7553FXF 8
Repeati800 – 8034FXFG 12
Repeati819 – 8213FXF 9
Repeati866 – 8683FXF 10
Repeati885 – 8884FXFG 13
Repeati929 – 9313FXF 11
Repeati1008 – 10092FG 1
Repeati1027 – 10282FG 2
Repeati1038 – 10392FG 3

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1040 – 107637Interaction with KAP95Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi81 – 844Poly-Asn
Compositional biasi718 – 7236Poly-Thr
Compositional biasi830 – 8334Poly-Thr
Compositional biasi881 – 1022142Asn-richAdd
BLAST

Domaini

Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side: FXFG repeats are especially abundant in NUPs on the nucleoplasmic side (in a highly charged environment and enriched in Ser and Thr).

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00730000111010.
InParanoidiP20676.
OMAiENTERPP.
OrthoDBiEOG7BW0ST.

Family and domain databases

InterProiIPR018892. Retro-transposon_transp_CS.
[Graphical view]
PfamiPF10599. Nup_retrotrp_bd. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20676-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSNTSSVMS SPRVEKRSFS STLKSFFTNP NKKRPSSKKV FSSNLSYANH
60 70 80 90 100
LEESDVEDTL HVNKRKRVSG TSQHSDSLTQ NNNNAPIIIY GTENTERPPL
110 120 130 140 150
LPILPIQRLR LLREKQRVRN MRELGLIQST EFPSITSSVI LGSQSKSDEG
160 170 180 190 200
GSYLCTSSTP SPIKNGSCTR QLAGKSGEDT NVGLPILKSL KNRSNRKRFH
210 220 230 240 250
SQSKGTVWSA NFEYDLSEYD AIQKKDNKDK EGNAGGDQKT SENRNNIKSS
260 270 280 290 300
ISNGNLATGP NLTSEIEDLR ADINSNRLSN PQKNLLLKGP ASTVAKTAPI
310 320 330 340 350
QESFVPNSER SGTPTLKKNI EPKKDKESIV LPTVGFDFIK DNETPSKKTS
360 370 380 390 400
PKATSSAGAV FKSSVEMGKT DKSTKTAEAP TLSFNFSQKA NKTKAVDNTV
410 420 430 440 450
PSTTLFNFGG KSDTVTSASQ PFKFGKTSEK SENHTESDAP PKSTAPIFSF
460 470 480 490 500
GKQEENGDEG DDENEPKRKR RLPVSEDTNT KPLFDFGKTG DQKETKKGES
510 520 530 540 550
EKDASGKPSF VFGASDKQAE GTPLFTFGKK ADVTSNIDSS AQFTFGKAAT
560 570 580 590 600
AKETHTKPSE TPATIVKKPT FTFGQSTSEN KISEGSAKPT FSFSKSEEER
610 620 630 640 650
KSSPISNEAA KPSFSFPGKP VDVQAPTDDK TLKPTFSFTE PAQKDSSVVS
660 670 680 690 700
EPKKPSFTFA SSKTSQPKPL FSFGKSDAAK EPPGSNTSFS FTKPPANETD
710 720 730 740 750
KRPTPPSFTF GGSTTNNTTT TSTKPSFSFG APESMKSTAS TAAANTEKLS
760 770 780 790 800
NGFSFTKFNH NKEKSNSPTS FFDGSASSTP IPVLGKPTDA TGNTTSKSAF
810 820 830 840 850
SFGTANTNGT NASANSTSFS FNAPATGNGT TTTSNTSGTN IAGTFNVGKP
860 870 880 890 900
DQSIASGNTN GAGSAFGFSS SGTAATGAAS NQSSFNFGNN GAGGLNPFTS
910 920 930 940 950
ATSSTNANAG LFNKPPSTNA QNVNVPSAFN FTGNNSTPGG GSVFNMNGNT
960 970 980 990 1000
NANTVFAGSN NQPHQSQTPS FNTNSSFTPS TVPNINFSGL NGGITNTATN
1010 1020 1030 1040 1050
ALRPSDIFGA NAASGSNSNV TNPSSIFGGA GGVPTTSFGQ PQSAPNQMGM
1060 1070
GTNNGMSMGG GVMANRKIAR MRHSKR
Length:1,076
Mass (Da):113,581
Last modified:February 1, 1991 - v1
Checksum:i4AC23567D2FB53CC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M33632 Genomic DNA. Translation: AAA34822.1.
X94335 Genomic DNA. Translation: CAA64020.1.
Z75006 Genomic DNA. Translation: CAA99295.1.
BK006948 Genomic DNA. Translation: DAA10875.1.
PIRiA35622.
RefSeqiNP_014741.1. NM_001183517.1.

Genome annotation databases

EnsemblFungiiYOR098C; YOR098C; YOR098C.
GeneIDi854265.
KEGGisce:YOR098C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M33632 Genomic DNA. Translation: AAA34822.1 .
X94335 Genomic DNA. Translation: CAA64020.1 .
Z75006 Genomic DNA. Translation: CAA99295.1 .
BK006948 Genomic DNA. Translation: DAA10875.1 .
PIRi A35622.
RefSeqi NP_014741.1. NM_001183517.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BPT X-ray 1.99 B 974-1012 [» ]
4C31 X-ray 3.00 C/F/X/Y 322-355 [» ]
4MBE X-ray 2.61 G/H/X/Y 316-340 [» ]
ProteinModelPortali P20676.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34496. 69 interactions.
DIPi DIP-81N.
IntActi P20676. 47 interactions.
MINTi MINT-1759946.
STRINGi 4932.YOR098C.

Protein family/group databases

TCDBi 1.I.1.1.1. the nuclear pore complex (npc) family.

Proteomic databases

MaxQBi P20676.
PaxDbi P20676.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOR098C ; YOR098C ; YOR098C .
GeneIDi 854265.
KEGGi sce:YOR098C.

Organism-specific databases

CYGDi YOR098c.
SGDi S000005624. NUP1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00730000111010.
InParanoidi P20676.
OMAi ENTERPP.
OrthoDBi EOG7BW0ST.

Enzyme and pathway databases

BioCyci YEAST:G3O-33631-MONOMER.

Miscellaneous databases

EvolutionaryTracei P20676.
NextBioi 976209.

Gene expression databases

Genevestigatori P20676.

Family and domain databases

InterProi IPR018892. Retro-transposon_transp_CS.
[Graphical view ]
Pfami PF10599. Nup_retrotrp_bd. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The NUP1 gene encodes an essential component of the yeast nuclear pore complex."
    Davis L.I., Fink G.R.
    Cell 61:965-978(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "The karyopherin Kap122p/Pdr6p imports both subunits of the transcription factor IIA into the nucleus."
    Titov A.A., Blobel G.
    J. Cell Biol. 147:235-246(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KAP122.
  6. "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] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, NPC SUBUNIT LOCATION.
  7. "Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin alpha."
    Solsbacher J., Maurer P., Vogel F., Schlenstedt G.
    Mol. Cell. Biol. 20:8468-8479(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SRP1 RECYCLING.
  8. "Proteomic analysis of nucleoporin interacting proteins."
    Allen N.P., Huang L., Burlingame A., Rexach M.
    J. Biol. Chem. 276:29268-29274(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION THROUGH FG REPEATS.
  9. "The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex."
    Denning D.P., Mykytka B., Allen N.P., Huang L., Burlingame A., Rexach M.
    J. Cell Biol. 154:937-950(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUP60.
  10. "GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta."
    Bayliss R., Littlewood T., Strawn L.A., Wente S.R., Stewart M.
    J. Biol. Chem. 277:50597-50606(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, STRUCTURAL BASIS OF FG REPEAT INTERACTION.
  11. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KARYOPHERINS THROUGH FG REPEATS.
  12. "Accelerating the rate of disassembly of karyopherin-cargo complexes."
    Gilchrist D., Mykytka B., Rexach M.
    J. Biol. Chem. 277:18161-18172(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IMPORT COMPLEX DISASSEMBLY.
  13. "A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex."
    Pyhtila B., Rexach M.
    J. Biol. Chem. 278:42699-42709(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AFFINITY GRADIENT FOR KARYOPHERIN KAP95.
  14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  15. "Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded."
    Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.
    Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FG REPEAT STRUCTURE.
  16. "Minimal nuclear pore complexes define FG repeat domains essential for transport."
    Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.
    Nat. Cell Biol. 6:197-206(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FG REPEATS IN NPC TRANSPORT.
  17. "Peering through the pore: nuclear pore complex structure, assembly, and function."
    Suntharalingam M., Wente S.R.
    Dev. Cell 4:775-789(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  18. Cited for: PHOSPHORYLATION BY CDC28.
  19. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  20. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; THR-381; SER-383 AND SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNUP1_YEAST
AccessioniPrimary (citable) accession number: P20676
Secondary accession number(s): D6W2F9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 29, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 468 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3