NUP82_YEAST
ID NUP82_YEAST Reviewed; 713 AA.
AC P40368; D6VWC1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Nucleoporin NUP82 {ECO:0000312|SGD:S000003597};
DE AltName: Full=Nuclear pore protein NUP82;
GN Name=NUP82; OrderedLocusNames=YJL061W; ORFNames=HRB187, J1135;
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].
RC STRAIN=ATCC 200912 / DF5;
RX PubMed=7559751; DOI=10.1083/jcb.130.6.1275;
RA Hurwitz M.E., Blobel G.;
RT "NUP82 is an essential yeast nucleoporin required for poly(A)+ RNA
RT export.";
RL J. Cell Biol. 130:1275-1281(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN MRNA EXPORT.
RX PubMed=7559750; DOI=10.1083/jcb.130.6.1263;
RA Grandi P., Emig S., Weise C., Hucho F., Pohl T.M., Hurt E.C.;
RT "A novel nuclear pore protein Nup82p which specifically binds to a fraction
RT of Nsp1p.";
RL J. Cell Biol. 130:1263-1273(1995).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762302; DOI=10.1002/yea.320110108;
RA Vandenbol M., Durand P., Dion C., Portetelle D., Hilger F.;
RT "Sequence of a 17.1 kb DNA fragment from chromosome X of Saccharomyces
RT cerevisiae includes the mitochondrial ribosomal protein L8.";
RL Yeast 11:57-60(1995).
RN [6]
RP FUNCTION, AND INTERACTION WITH NUP159 AND NSP1.
RX PubMed=9843582; DOI=10.1091/mbc.9.12.3475;
RA Belgareh N., Snay-Hodge C., Pasteau F., Dagher S., Cole C.N., Doye V.;
RT "Functional characterization of a Nup159p-containing nuclear pore
RT subcomplex.";
RL Mol. Biol. Cell 9:3475-3492(1998).
RN [7]
RP FUNCTION, AND NUP82 NPC SUBCOMPLEX.
RX PubMed=10801828; DOI=10.1074/jbc.m001963200;
RA Bailer S.M., Balduf C., Katahira J., Podtelejnikov A., Rollenhagen C.,
RA Mann M., Pante N., Hurt E.C.;
RT "Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex.";
RL J. Biol. Chem. 275:23540-23548(2000).
RN [8]
RP CHARACTERIZATION, AND NPC SUBUNIT 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 [9]
RP FUNCTION, AND INTERACTION WITH NUP116.
RX PubMed=10891509; DOI=10.1128/mcb.20.15.5736-5748.2000;
RA Ho A.K., Shen T.X., Ryan K.J., Kiseleva E., Levy M.A., Allen T.D.,
RA Wente S.R.;
RT "Assembly and preferential localization of Nup116p on the cytoplasmic face
RT of the nuclear pore complex by interaction with Nup82p.";
RL Mol. Cell. Biol. 20:5736-5748(2000).
RN [10]
RP FUNCTION, AND PRE-RIBOSOME EXPORT.
RX PubMed=11739405; DOI=10.1083/jcb.200108142;
RA Gleizes P.-E., Noaillac-Depeyre J., Leger-Silvestre I., Teulieres F.,
RA Dauxois J.-Y., Pommet D., Azum-Gelade M.-C., Gas N.;
RT "Ultrastructural localization of rRNA shows defective nuclear export of
RT preribosomes in mutants of the Nup82p complex.";
RL J. Cell Biol. 155:923-936(2001).
RN [11]
RP FUNCTION, AND NPC ASSEMBLY.
RX PubMed=11689687; DOI=10.1128/mcb.21.23.7944-7955.2001;
RA Bailer S.M., Balduf C., Hurt E.C.;
RT "The Nsp1p carboxy-terminal domain is organized into functionally distinct
RT coiled-coil regions required for assembly of nucleoporin subcomplexes and
RT nucleocytoplasmic transport.";
RL Mol. Cell. Biol. 21:7944-7955(2001).
RN [12]
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 [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17546040; DOI=10.1038/ncb1604;
RA Stelter P., Kunze R., Flemming D., Hoepfner D., Diepholz M., Philippsen P.,
RA Boettcher B., Hurt E.;
RT "Molecular basis for the functional interaction of dynein light chain with
RT the nuclear-pore complex.";
RL Nat. Cell Biol. 9:788-796(2007).
RN [15]
RP NUP82 NPC SUBCOMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=25646085; DOI=10.1083/jcb.201411003;
RA Gaik M., Flemming D., von Appen A., Kastritis P., Muecke N., Fischer J.,
RA Stelter P., Ori A., Bui K.H., Bassler J., Barbar E., Beck M., Hurt E.;
RT "Structural basis for assembly and function of the Nup82 complex in the
RT nuclear pore scaffold.";
RL J. Cell Biol. 208:283-297(2015).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-452 IN COMPLEX WITH NUP116 AND
RP NUP159, AND SUBUNIT.
RX PubMed=21930948; DOI=10.1073/pnas.1112846108;
RA Yoshida K., Seo H.S., Debler E.W., Blobel G., Hoelz A.;
RT "Structural and functional analysis of an essential nucleoporin
RT heterotrimer on the cytoplasmic face of the nuclear pore complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:16571-16576(2011).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-452 IN COMPLEX WITH NUP159 AND
RP THE MOUSE ORTHOLOG OF NUP145, AND SUBUNIT.
RX PubMed=22480613; DOI=10.1016/j.jmb.2012.03.024;
RA Stuwe T., von Borzyskowski L.S., Davenport A.M., Hoelz A.;
RT "Molecular basis for the anchoring of proto-oncoprotein Nup98 to the
RT cytoplasmic face of the nuclear pore complex.";
RL J. Mol. Biol. 419:330-346(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. It is specifically involved as part of the NUP82-NUP159-NSP1
CC subcomplex in nuclear mRNA and pre-ribosome export by acting as a
CC linker tethering nucleoporins that are directly involved in nuclear
CC transport to the NPC via its coiled-coil domain.
CC {ECO:0000269|PubMed:10801828, ECO:0000269|PubMed:10891509,
CC ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:11739405,
CC ECO:0000269|PubMed:7559750, ECO:0000269|PubMed:9843582}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC) (PubMed:11689687).
CC NPC constitutes the exclusive means of nucleocytoplasmic transport.
CC NPCs allow the passive diffusion of ions and small molecules and the
CC active, nuclear transport receptor-mediated bidirectional transport of
CC macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and
CC ribosomal subunits across the nuclear envelope. Due to its 8-fold
CC rotational symmetry, all subunits are present with 8 copies or
CC multiples thereof. NUP82 is part of the NUP82 subcomplex. This
CC subcomplex is the base for interactions with NUP116 and GLE2, with
CC NUP42 and GLE1 and with DYN2. {ECO:0000269|PubMed:11689687,
CC ECO:0000269|PubMed:21930948, ECO:0000269|PubMed:22480613,
CC ECO:0000269|PubMed:25646085}.
CC -!- INTERACTION:
CC P40368; P14907: NSP1; NbExp=7; IntAct=EBI-12331, EBI-12265;
CC P40368; Q02630: NUP116; NbExp=3; IntAct=EBI-12331, EBI-11703;
CC P40368; P40477: NUP159; NbExp=5; IntAct=EBI-12331, EBI-11747;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:10801828}. Nucleus
CC membrane; Peripheral membrane protein; Cytoplasmic side.
CC -!- MISCELLANEOUS: Present with 9470 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U31543; AAA85504.1; -; Genomic_DNA.
DR EMBL; X85970; CAA59957.1; -; Genomic_DNA.
DR EMBL; Z49336; CAA89352.1; -; Genomic_DNA.
DR EMBL; Z34288; CAA84062.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08737.1; -; Genomic_DNA.
DR PIR; S56833; S56833.
DR RefSeq; NP_012474.1; NM_001181494.1.
DR PDB; 3PBP; X-ray; 2.60 A; A/D/G/J=1-452.
DR PDB; 3TKN; X-ray; 3.40 A; A/D/G=1-452.
DR PDB; 7N9F; EM; 37.00 A; u/v=1-713.
DR PDBsum; 3PBP; -.
DR PDBsum; 3TKN; -.
DR PDBsum; 7N9F; -.
DR AlphaFoldDB; P40368; -.
DR SMR; P40368; -.
DR BioGRID; 33693; 181.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-913N; -.
DR IntAct; P40368; 24.
DR MINT; P40368; -.
DR STRING; 4932.YJL061W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P40368; -.
DR MaxQB; P40368; -.
DR PaxDb; P40368; -.
DR PRIDE; P40368; -.
DR EnsemblFungi; YJL061W_mRNA; YJL061W; YJL061W.
DR GeneID; 853385; -.
DR KEGG; sce:YJL061W; -.
DR SGD; S000003597; NUP82.
DR VEuPathDB; FungiDB:YJL061W; -.
DR eggNOG; ENOG502T8MV; Eukaryota.
DR HOGENOM; CLU_398512_0_0_1; -.
DR InParanoid; P40368; -.
DR OMA; FHYSIDE; -.
DR BioCyc; YEAST:G3O-31523-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; P40368; -.
DR PRO; PR:P40368; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40368; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
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:0044614; C:nuclear pore cytoplasmic filaments; IDA:SGD.
DR GO; GO:0044612; C:nuclear pore linkers; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IC:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006611; P:protein export from nucleus; IMP: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 GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:SGD.
DR InterPro; IPR037700; NUP88/NUP82.
DR PANTHER; PTHR13257; PTHR13257; 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..713
FT /note="Nucleoporin NUP82"
FT /id="PRO_0000204883"
FT REGION 1..409
FT /note="Interaction with NUP116"
FT /evidence="ECO:0000269|PubMed:10891509"
FT REGION 463..713
FT /note="Interaction with NSP1 and NUP159"
FT /evidence="ECO:0000269|PubMed:9843582"
FT COILED 582..713
FT /evidence="ECO:0000255"
FT MOTIF 607..623
FT /note="Bipartite nuclear localization signal"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3TKN"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:3TKN"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3PBP"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:3PBP"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:3PBP"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:3PBP"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:3PBP"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3TKN"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:3PBP"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3PBP"
FT HELIX 220..235
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3PBP"
FT HELIX 243..262
FT /evidence="ECO:0007829|PDB:3PBP"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3PBP"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3PBP"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:3PBP"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 378..385
FT /evidence="ECO:0007829|PDB:3PBP"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:3PBP"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:3PBP"
SQ SEQUENCE 713 AA; 82085 MW; C379B5E111E26B50 CRC64;
MSQSSRLSAL PIFQASLSAS QSPRYIFSSQ NGTRIVFIQD NIIRWYNVLT DSLYHSLNFS
RHLVLDDTFH VISSTSGDLL CLFNDNEIFV MEVPWGYSNV EDVSIQDAFQ IFHYSIDEEE
VGPKSSIKKV LFHPKSYRDS CIVVLKEDDT ITMFDILNSQ EKPIVLNKPN NSFGLDARVN
DITDLEFSKD GLTLYCLNTT EGGDIFAFYP FLPSVLLLNE KDLNLILNKS LVMYESLDST
TDVIVKRNVI KQLQFVSKLH ENWNSRFGKV DIQKEYRLAK VQGPFTINPF PGELYDYTAT
NIATILIDNG QNEIVCVSFD DGSLILLFKD LEMSMSWDVD NYVYNNSLVL IERVKLQREI
KSLITLPEQL GKLYVISDNI IQQVNFMSWA STLSKCINES DLNPLAGLKF ESKLEDIATI
ERIPNLAYIN WNDQSNLALM SNKTLTFQNI SSDMKPQSTA AETSISTEKS DTVGDGFKMS
FTQPINEILI LNDNFQKACI SPCERIIPSA DRQIPLKNEA SENQLEIFTD ISKEFLQRIV
KAQTLGVSIH NRIHEQQFEL TRQLQSTCKI ISKDDDLRRK FEAQNKKWDA QLSRQSELME
RFSKLSKKLS QIAESNKFKE KKISHGEMKW FKEIRNQILQ FNSFVHSQKS LQQDLSYLKS
ELTRIEAETI KVDKKSQNEW DELRKMLEID SKIIKECNEE LLQVSQEFTT KTQ
