NU170_YEAST
ID NU170_YEAST Reviewed; 1502 AA.
AC P38181; D6VPS4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Nucleoporin NUP170;
DE AltName: Full=Nuclear pore protein NUP170;
GN Name=NUP170; Synonyms=NLE3; OrderedLocusNames=YBL079W; ORFNames=YBL0725;
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 204508 / S288c;
RX PubMed=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 117-133 AND 153-166.
RX PubMed=8522578; DOI=10.1083/jcb.131.5.1133;
RA Aitchison J.D., Rout M.P., Marelli M., Blobel G., Wozniak R.W.;
RT "Two novel related yeast nucleoporins Nup170p and Nup157p: complementation
RT with the vertebrate homologue Nup155p and functional interactions with the
RT yeast nuclear pore-membrane protein Pom152p.";
RL J. Cell Biol. 131:1133-1148(1995).
RN [5]
RP FUNCTION, AND SUBCOMPLEX WITH NUP59 AND NUP53.
RX PubMed=9864357; DOI=10.1083/jcb.143.7.1813;
RA Marelli M., Aitchison J.D., Wozniak R.W.;
RT "Specific binding of the karyopherin Kap121p to a subunit of the nuclear
RT pore complex containing Nup53p, Nup59p, and Nup170p.";
RL J. Cell Biol. 143:1813-1830(1998).
RN [6]
RP FUNCTION, AND COMPETITION WITH NUP53 FOR PSE1 BINDING.
RX PubMed=12403813; DOI=10.1083/jcb.200203079;
RA Lusk C.P., Makhnevych T., Marelli M., Aitchison J.D., Wozniak R.W.;
RT "Karyopherins in nuclear pore biogenesis: a role for Kap121p in the
RT assembly of Nup53p into nuclear pore complexes.";
RL J. Cell Biol. 159:267-278(2002).
RN [7]
RP FUNCTION, MITOTIC PSE1 TRANSPORT INHIBITION, AND NPC ASSEMBLY.
RX PubMed=14697200; DOI=10.1016/s0092-8674(03)00986-3;
RA Makhnevych T., Lusk C.P., Anderson A.M., Aitchison J.D., Wozniak R.W.;
RT "Cell cycle regulated transport controlled by alterations in the nuclear
RT pore complex.";
RL Cell 115:813-823(2003).
RN [8]
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 [9]
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 [10]
RP FUNCTION, AND CHROMOSOME TRANSMISSION FIDELITY.
RX PubMed=11290711; DOI=10.1093/genetics/157.4.1543;
RA Kerscher O., Hieter P., Winey M., Basrai M.A.;
RT "Novel role for a Saccharomyces cerevisiae nucleoporin, Nup170p, in
RT chromosome segregation.";
RL Genetics 157:1543-1553(2001).
RN [11]
RP FUNCTION, AND INTERACTION WITH NUP157 AND NUP53.
RX PubMed=12473689; DOI=10.1083/jcb.200205068;
RA Iouk T., Kerscher O., Scott R.J., Basrai M.A., Wozniak R.W.;
RT "The yeast nuclear pore complex functionally interacts with components of
RT the spindle assembly checkpoint.";
RL J. Cell Biol. 159:807-819(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 980-1502.
RX PubMed=19674973; DOI=10.1074/jbc.m109.023580;
RA Whittle J.R., Schwartz T.U.;
RT "Architectural nucleoporins Nup157/170 and Nup133 are structurally related
RT and descend from a second ancestral element.";
RL J. Biol. Chem. 284:28442-28452(2009).
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. NUP170 probably plays an important role in NPC assembly and
CC organization. In addition it is required for chromosome transmission
CC fidelity. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11290711,
CC ECO:0000269|PubMed:12403813, ECO:0000269|PubMed:12473689,
CC ECO:0000269|PubMed:14697200, ECO:0000269|PubMed:9864357}.
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 During mitosis NUP53 changes its binding partner within the NPC from
CC NUP170 to NIC96, exposing a high affinity binding site for the
CC karyopherin PSE1, and retaining it in the NPC.
CC {ECO:0000269|PubMed:10684247}.
CC -!- INTERACTION:
CC P38181; P49687: NUP145; NbExp=3; IntAct=EBI-11756, EBI-11730;
CC P38181; Q03790: NUP53; NbExp=5; IntAct=EBI-11756, EBI-27321;
CC P38181; P11978: SIR4; NbExp=3; IntAct=EBI-11756, EBI-17237;
CC P38181; P32597: STH1; NbExp=3; IntAct=EBI-11756, EBI-18410;
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 {ECO:0000269|PubMed:10684247}.
CC -!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the non-repetitive/WGA-negative nucleoporin
CC family. {ECO:0000305}.
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DR EMBL; X79489; CAA56029.1; -; Genomic_DNA.
DR EMBL; Z35840; CAA84900.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07044.1; -; Genomic_DNA.
DR PIR; S45429; S45429.
DR RefSeq; NP_009474.1; NM_001178319.1.
DR PDB; 3I5P; X-ray; 3.20 A; A=980-1502.
DR PDB; 3I5Q; X-ray; 2.20 A; A/B=1253-1502.
DR PDB; 7N85; EM; 7.60 A; 0/Y=1-1502.
DR PDB; 7N9F; EM; 37.00 A; 0/Y=1-1502.
DR PDB; 7WOO; EM; 3.71 A; D=1-1502.
DR PDB; 7WOT; EM; 3.73 A; D/P=1-1502.
DR PDBsum; 3I5P; -.
DR PDBsum; 3I5Q; -.
DR PDBsum; 7N85; -.
DR PDBsum; 7N9F; -.
DR PDBsum; 7WOO; -.
DR PDBsum; 7WOT; -.
DR AlphaFoldDB; P38181; -.
DR SMR; P38181; -.
DR BioGRID; 32624; 446.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2450N; -.
DR IntAct; P38181; 22.
DR MINT; P38181; -.
DR STRING; 4932.YBL079W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P38181; -.
DR MaxQB; P38181; -.
DR PaxDb; P38181; -.
DR PRIDE; P38181; -.
DR EnsemblFungi; YBL079W_mRNA; YBL079W; YBL079W.
DR GeneID; 852199; -.
DR KEGG; sce:YBL079W; -.
DR SGD; S000000175; NUP170.
DR VEuPathDB; FungiDB:YBL079W; -.
DR eggNOG; KOG1900; Eukaryota.
DR GeneTree; ENSGT00390000016532; -.
DR HOGENOM; CLU_000429_0_1_1; -.
DR InParanoid; P38181; -.
DR OMA; EYYSRMI; -.
DR BioCyc; YEAST:G3O-28970-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; P38181; -.
DR PRO; PR:P38181; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38181; 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:0044611; C:nuclear pore inner ring; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IMP:SGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051292; P:nuclear pore complex assembly; IGI:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0036228; P:protein localization to nuclear inner membrane; IMP:SGD.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0034398; P:telomere tethering at nuclear periphery; IMP:SGD.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR Gene3D; 1.25.40.440; -; 1.
DR Gene3D; 1.25.40.450; -; 1.
DR InterPro; IPR007187; Nucleoporin_Nup133/Nup155_C.
DR InterPro; IPR014908; Nucleoporin_Nup133/Nup155_N.
DR InterPro; IPR004870; Nucleoporin_Nup155.
DR InterPro; IPR042533; Nucleoporin_Nup155_C_1.
DR InterPro; IPR042537; Nucleoporin_Nup155_C_2.
DR PANTHER; PTHR10350; PTHR10350; 1.
DR Pfam; PF03177; Nucleoporin_C; 1.
DR Pfam; PF08801; Nucleoporin_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..1502
FT /note="Nucleoporin NUP170"
FT /id="PRO_0000204854"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..261
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 1001..1015
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1022..1032
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1045..1056
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1060..1075
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1079..1086
FT /evidence="ECO:0007829|PDB:3I5P"
FT STRAND 1089..1093
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1095..1114
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1146..1149
FT /evidence="ECO:0007829|PDB:3I5P"
FT STRAND 1150..1152
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1155..1167
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1171..1176
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1182..1188
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1196..1201
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1203..1206
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1210..1221
FT /evidence="ECO:0007829|PDB:3I5P"
FT STRAND 1222..1225
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1229..1242
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1262..1264
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1265..1281
FT /evidence="ECO:0007829|PDB:3I5Q"
FT STRAND 1283..1285
FT /evidence="ECO:0007829|PDB:3I5P"
FT HELIX 1287..1299
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1304..1310
FT /evidence="ECO:0007829|PDB:3I5Q"
FT TURN 1311..1316
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1318..1327
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1333..1350
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1357..1378
FT /evidence="ECO:0007829|PDB:3I5Q"
FT TURN 1382..1384
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1387..1401
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1404..1406
FT /evidence="ECO:0007829|PDB:3I5Q"
FT TURN 1409..1412
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1413..1419
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1423..1435
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1442..1458
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1460..1463
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1469..1472
FT /evidence="ECO:0007829|PDB:3I5Q"
FT TURN 1479..1481
FT /evidence="ECO:0007829|PDB:3I5Q"
FT HELIX 1483..1491
FT /evidence="ECO:0007829|PDB:3I5Q"
SQ SEQUENCE 1502 AA; 169475 MW; 3BEA65DAA2A5F99A CRC64;
MFQSFFHNNG PAAAGETFSD SRSYPLTNHQ EVPRNGLNEL ASSATKAQQQ PTHILNSYPI
TGSNPLMRAS AMGATSGSIN PNMSNMNEHI RVSGMGTSKP LDLAGKYIDH LQHKDSNTPV
LDERSYYNSG VDYNFSREKN GLGAFTPFEK QDVFNIPDEI LHEFSTSQTK TDMGIFPELN
RCWITIDNKL ILWNINNDNE YQVVDDMKHT IQKVALVRPK PNTFVPAVKH LLLISTTMEL
FMFAISLDKA TNELSVFNTH LSVPVQGIDV IDIVSHERSG RIFFAGQASG LNIWELHYSG
SDDWFNSKCS KVCLTKSALL SLLPTNMLSQ IPGVDFIQAL FEDNSNGNGG FSQETITQLT
IDQQRGIIYS LSSKSTIRAY VITEKSLEGP MSIEPAYISR IIGTTTARAA PILGPKYLKI
VKISSVAPEE NNNLFLVALT VGGVRLYFNG SMGRFNIEAL RLESIKFPPS SVTPEVIQQE
LLHQQQEQAK RSFPFFSNLM SSEPVLLKFQ KKSSVLLETT KASTIISPGI FFSAVIKSSQ
QTHQQEKKEN SSVTGTTATA GSKTVKQQPV TLQHKLFVSV PDYGILKTHG KYVENATFLE
TAGPVQQIIP LSGLFNATTK PQGFANEFAT QYTSETLRVA VLTSTSIEIY KYRTPDEIFE
DLIDNPLPFV LNYGAAEACS TALFVTCKSN KSEKLRSNAL TFLTMGIPGV VDIKPVYNRY
SVSTVSSLLS KPTLSTATTN LQQSITGFSK PSPANKEDFD LDDVILSPRF YGIALLITRL
LRDIWGRHVF MTFTDNRVTS HAFISSSDPI TPSINNLKSD EISQNRNIIS KVSISKDCIE
YYLSSINILN EFFITYGDSI SQISAPYVLA NNSNGRVIDK TEEVANQAES IAINAMIKMV
QSIKEGLSFL NVLYEESEVE GFDNQYLGFK DIISFVSLDV QKDLVKLDFK DLFAPNDKTK
SLIREILLSI INRNITKGAS IEYTATALQE RCGSFCSASD ILGFRAIEHL RRAKEIGLRN
YDSLNYHLKN ATALLEQIVD DLSIEKLKEA VSMMLSVNYY PKSIEFLLNI ANSMDKGKLA
CQYVANGFLE NDDRKQYYDK RILVYDLVFD TLIKVDELAE KKQSSKTQNQ ISISNDDEVK
LRQKSYEAAL KYNDRLFHYH MYDWLVSQNR EEKLLDIETP FILPYLMEKA GSSLKISNIL
WVYYSRRSKF FESAEILYRL ATSNFDITLF ERIEFLSRAN GFCNSVSPLS QKQRIVQLAS
RIQDACEVAG IQGDILSLVY TDARIDSAIK DELIKTLDGK ILSTSELFND FAVPLSYHEI
ALFIFKIADF RDHEVIMAKW DELFQSLRME FNNTGKKEDS MNFINLLSNV LIKIGKNVQD
SEFIFPIFEL FPIVCNFFYE TLPKEHIVSG SIVSIFITAG VSFNKMYYIL KELIETSDSD
NSVFNKEMTW LIHEWYKSDR KFRDIISYND IIHLKEYKID NDPIEKYVKN SGNNLGICFY
KE
