NU192_YEAST
ID NU192_YEAST Reviewed; 1683 AA.
AC P47054; D6VWE4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Nucleoporin NUP192;
DE AltName: Full=Nuclear pore protein NUP192;
GN Name=NUP192; OrderedLocusNames=YJL039C; ORFNames=J1216;
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 [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 [2]
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 [3]
RP FUNCTION, INTERACTION WITH NIC96, AND LOCATION WITHIN THE NPC.
RX PubMed=10428845; DOI=10.1074/jbc.274.32.22646;
RA Kosova B., Pante N., Rollenhagen C., Hurt E.C.;
RT "Nup192p is a conserved nucleoporin with a preferential location at the
RT inner site of the nuclear membrane.";
RL J. Biol. Chem. 274:22646-22651(1999).
RN [4]
RP FUNCTION, AND NPC DE NOVO ASSEMBLY.
RX PubMed=11121302; DOI=10.1006/jsbi.2000.4305;
RA Gomez-Ospina N., Morgan G., Giddings T.H. Jr., Kosova B., Hurt E.C.,
RA Winey M.;
RT "Yeast nuclear pore complex assembly defects determined by nuclear envelope
RT reconstruction.";
RL J. Struct. Biol. 132:1-5(2000).
RN [5]
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 [6]
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 [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 2-960.
RX PubMed=23499021; DOI=10.1016/j.str.2013.02.005;
RA Sampathkumar P., Kim S.J., Upla P., Rice W.J., Phillips J., Timney B.L.,
RA Pieper U., Bonanno J.B., Fernandez-Martinez J., Hakhverdyan Z.,
RA Ketaren N.E., Matsui T., Weiss T.M., Stokes D.L., Sauder J.M., Burley S.K.,
RA Sali A., Rout M.P., Almo S.C.;
RT "Structure, dynamics, evolution, and function of a major scaffold component
RT in the nuclear pore complex.";
RL Structure 21:560-571(2013).
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. NUP192 is located to the NPC core at the nuclear membrane and
CC is essential for de novo assembly of NPCs.
CC {ECO:0000269|PubMed:10428845, ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11121302}.
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 NUP192 interacts with NIC96. {ECO:0000269|PubMed:10428845,
CC ECO:0000269|PubMed:10684247}.
CC -!- INTERACTION:
CC P47054; Q05166: ASM4; NbExp=3; IntAct=EBI-25846, EBI-3035;
CC P47054; P34077: NIC96; NbExp=3; IntAct=EBI-25846, EBI-12056;
CC P47054; Q02630: NUP116; NbExp=2; IntAct=EBI-25846, EBI-11703;
CC P47054; P49687: NUP145; NbExp=2; IntAct=EBI-25846, EBI-11730;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10684247}. Note=Cytoplasmic and nucleoplasmic side
CC of the nuclear pore complex in the nuclear envelope (symmetric
CC distribution).
CC -!- MISCELLANEOUS: Present with 2520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NUP186/NUP192/NUP205 family. {ECO:0000305}.
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DR EMBL; Z49314; CAA89330.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08760.1; -; Genomic_DNA.
DR PIR; S56811; S56811.
DR RefSeq; NP_012495.1; NM_001181473.1.
DR PDB; 4IFQ; X-ray; 3.25 A; A=2-960.
DR PDB; 7N85; EM; 7.60 A; M/O=1-1683.
DR PDB; 7N9F; EM; 37.00 A; M/O=1-1683.
DR PDB; 7WOO; EM; 3.71 A; F=1-1683.
DR PDB; 7WOT; EM; 3.73 A; F/R=1-1683.
DR PDBsum; 4IFQ; -.
DR PDBsum; 7N85; -.
DR PDBsum; 7N9F; -.
DR PDBsum; 7WOO; -.
DR PDBsum; 7WOT; -.
DR AlphaFoldDB; P47054; -.
DR SMR; P47054; -.
DR BioGRID; 33718; 339.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2442N; -.
DR IntAct; P47054; 24.
DR MINT; P47054; -.
DR STRING; 4932.YJL039C; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P47054; -.
DR MaxQB; P47054; -.
DR PaxDb; P47054; -.
DR PRIDE; P47054; -.
DR DNASU; 853410; -.
DR EnsemblFungi; YJL039C_mRNA; YJL039C; YJL039C.
DR GeneID; 853410; -.
DR KEGG; sce:YJL039C; -.
DR SGD; S000003576; NUP192.
DR VEuPathDB; FungiDB:YJL039C; -.
DR eggNOG; KOG1835; Eukaryota.
DR HOGENOM; CLU_002778_0_0_1; -.
DR InParanoid; P47054; -.
DR OMA; AYGFIEW; -.
DR BioCyc; YEAST:G3O-31505-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 PRO; PR:P47054; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47054; protein.
DR GO; GO:0005635; C:nuclear envelope; IC:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0044611; C:nuclear pore inner ring; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006999; P:nuclear pore organization; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:SGD.
DR DisProt; DP02145; -.
DR InterPro; IPR021827; Nup186/Nup192/Nup205.
DR PANTHER; PTHR31344; PTHR31344; 2.
DR Pfam; PF11894; Nup192; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..1683
FT /note="Nucleoporin NUP192"
FT /id="PRO_0000204858"
FT COILED 31..58
FT /evidence="ECO:0000255"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:4IFQ"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:4IFQ"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:4IFQ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4IFQ"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 102..123
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 139..167
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 173..202
FT /evidence="ECO:0007829|PDB:4IFQ"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 272..289
FT /evidence="ECO:0007829|PDB:4IFQ"
FT TURN 293..299
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 344..348
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 425..445
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 447..460
FT /evidence="ECO:0007829|PDB:4IFQ"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 469..474
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 477..489
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:4IFQ"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 506..514
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 520..533
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 537..548
FT /evidence="ECO:0007829|PDB:4IFQ"
FT STRAND 549..553
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 555..572
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 603..622
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 625..642
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 650..660
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 665..668
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 669..680
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 689..699
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 703..716
FT /evidence="ECO:0007829|PDB:4IFQ"
FT TURN 738..744
FT /evidence="ECO:0007829|PDB:4IFQ"
FT STRAND 745..749
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 750..758
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 761..766
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 770..789
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 794..797
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 815..821
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 824..831
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 834..845
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 861..884
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 886..893
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 909..916
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 921..929
FT /evidence="ECO:0007829|PDB:4IFQ"
FT HELIX 935..949
FT /evidence="ECO:0007829|PDB:4IFQ"
SQ SEQUENCE 1683 AA; 191535 MW; FD2D61FDEA5451C4 CRC64;
MKWSAIPFQT LYRSIESGEF DFDLFKEVLP DLQNLNLNTD KLKNNASRSQ LEKGEIELSD
GSTFKVNQEF IFEAISLSDE LNLDEIVACE LILSGDTTAN NGKVQYFLRR QYILQIVSFI
VNCFHEDTEL YQELIKNGAL VSNILSAFKF IHTQLSEIKQ QINKAQILEN YNALFQQNIK
FRRDFLLREY DILSQILYGL VDKGAIMKNK DFILSLLHHV SELDSNDFFI IYYTPAFFHL
FASLRVLPDA DVKLLHSQFM KDLKDDSIYT KPVKVALIFI FFAYFIGWCK EDPKRRADTM
DFKTDVDEPM TSAVELGAIE QILIFAADTS IVEQDKSMEL FYDIRSLLER HIPRLIPKQL
LDDEKIFSQT TNSTYNPASA TDNMSGRGLW NPSYPGMMST TGTARLNSMP NNVNEYSYTT
IVLSDQTQEF FLSSFDDVLQ TIITDCAFLL TKIKDAEEDS LLSGEDLTLD DISLKADLER
FFLSIYFFYA SRPEYSCTFW SDKESNAYGF IEWCSRCNDN LMRSCFYLMV SSLSFGPENA
LNVYHYFGEN SSISWKNIAQ CLSDYTKKIS NFNSSLHKRQ QFSESTHNDI DSTAVALEEG
LNEEAVIFLS SLLTLVGSVT YQVDEDVKSS LSKVFSDVLF EFTKINTPLV GAAFKVISNL
VPKLESSRTK FWSFLDSLIF KDSSLNYSSE SYRNAFTNVL TKYSDVLGFL QLFHNLISIH
SRENNSEYMV FGKLAFPTRL GQGYRKVGIW PYFDYIFNDI LAHVDQIVDI RNKRAVQLPI
LKIIYTGLCS FDYSVILNSI PAAANLDALV DCENFFNYVQ ECPAIPIFNY IFTEKIYKSI
FNVVDVGVDQ LSIELEGGKN QAELLQLAVK IINKVLDYQE TYVEELFPIV KKHGKTDYFL
PKNYSLHGLR SFYDAIFFNI PLVAHLGLYV GVDDQILATN SLRILAKLSE RSNGSVASLS
KRNKLLTIFD SVDESARIKD AFITQLESSI TDAGVLALKL ELLDFLTSNL SNYSRTMTIS
HLLLGFQVSN VISLGPNLAT FISSGTSLLD SLISVLEASL NSITKDNIDY APMRLATAAL
EIILKLCRNP LTSGLLYSYL IKENFFERIM ILDPQVTRFT TWNGSPFDNS TEEKCKNFIE
SESVGAFLSF LAYRNYWTQY LGLFIHKISF SGTKSEVLTY VNYLISNTMY SVRLFSFLDP
LNYGNICEPK ETLSIFTNVP LNLEQVTLNK YCSGNIYDFH KMENLMRLIK RVRAESLHSN
SFSLTVSKEQ FLKDADVECI KAKSHFTNII SRNKALELNL SVLHSWVQLV QIIVTDGKLE
PSTRSNFILE VFGTIIPKIS DYIEFNITFS EELVSLAVFL FDIYNRDRKL ITDKGTVDGR
LYQLFKTCIQ GINSPLSSVA LRSDFYILAN HYLSRVLSDQ VGSEKVLQDL RLGSKKLVEI
IWNDVVYGEG TSRVTGILLL DSLIQLANRS KENFILDSLM KTTRLLLIIR SLKNTDALLN
STTEHINIDD LLYELTAFKA TVFFLIRVAE TRGGASALIE NNLFRIIAEL SFLKVDPDLG
LDLMFDEVYV QNSKFLKVNV TLDNPLLVDK DANGVSLFEL IVPIFQLISA VLVSMGSSNK
AVVQTVKGLL NTYKRLVIGI FKRDLLREKE DKKNSSDPNN QSLNEMVKLI VMLCTLTGYQ
NND
