NUP49_YEAST
ID NUP49_YEAST Reviewed; 472 AA.
AC Q02199; D6VTY0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Nucleoporin NUP49/NSP49;
DE AltName: Full=Nuclear pore protein NUP49/NSP49;
GN Name=NUP49; Synonyms=NSP49; OrderedLocusNames=YGL172W; ORFNames=G1648;
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].
RX PubMed=1464327; DOI=10.1002/j.1460-2075.1992.tb05612.x;
RA Wimmer C., Doye V., Grandi P., Nehrbass U., Hurt E.C.;
RT "A new subclass of nucleoporins that functionally interact with nuclear
RT pore protein NSP1.";
RL EMBO J. 11:5051-5061(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1385442; DOI=10.1083/jcb.119.4.705;
RA Wente S.R., Rout M.P., Blobel G.;
RT "A new family of yeast nuclear pore complex proteins.";
RL J. Cell Biol. 119:705-723(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8619317; DOI=10.1002/yea.320111209;
RA Bertani I., Coglievina M., Zaccaria P., Klima R., Bruschi C.V.;
RT "The sequence of an 11.1 kb fragment on the left arm of Saccharomyces
RT cerevisiae chromosome VII reveals six open reading frames including NSP49,
RT KEM1 and four putative new genes.";
RL Yeast 11:1187-1194(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
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 [6]
RP FUNCTION IN MRNA EXPORT.
RX PubMed=7813444; DOI=10.1002/j.1460-2075.1994.tb06953.x;
RA Doye V., Wepf R., Hurt E.C.;
RT "A novel nuclear pore protein Nup133p with distinct roles in poly(A)+ RNA
RT transport and nuclear pore distribution.";
RL EMBO J. 13:6062-6075(1994).
RN [7]
RP FUNCTION IN TRNA EXPORT.
RX PubMed=8524308; DOI=10.1128/mcb.16.1.294;
RA Sharma K., Fabre E., Tekotte H., Hurt E.C., Tollervey D.;
RT "Yeast nucleoporin mutants are defective in pre-tRNA splicing.";
RL Mol. Cell. Biol. 16:294-301(1996).
RN [8]
RP FUNCTION, AND THE NUP57 SUBCOMPLEX.
RX PubMed=9017593; DOI=10.1091/mbc.8.1.33;
RA Schlaich N.L., Haener M., Lustig A., Aebi U., Hurt E.C.;
RT "In vitro reconstitution of a heterotrimeric nucleoporin complex consisting
RT of recombinant Nsp1p, Nup49p, and Nup57p.";
RL Mol. Biol. Cell 8:33-46(1997).
RN [9]
RP FUNCTION, AND PRE-RIBOSOME EXPORT.
RX PubMed=9971735; DOI=10.1083/jcb.144.3.389;
RA Hurt E.C., Hannus S., Schmelzl B., Lau D.M., Tollervey D., Simos G.;
RT "A novel in vivo assay reveals inhibition of ribosomal nuclear export in
RT ran-cycle and nucleoporin mutants.";
RL J. Cell Biol. 144:389-401(1999).
RN [10]
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 [11]
RP FUNCTION, AND NUCLEOPORIN INTERACTING PROTEINS.
RX PubMed=11387327; DOI=10.1074/jbc.m102629200;
RA Allen N.P., Huang L., Burlingame A., Rexach M.;
RT "Proteomic analysis of nucleoporin interacting proteins.";
RL J. Biol. Chem. 276:29268-29274(2001).
RN [12]
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 [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 FUNCTION, AND FG REPEAT STRUCTURE.
RX PubMed=12604785; DOI=10.1073/pnas.0437902100;
RA Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.;
RT "Disorder in the nuclear pore complex: the FG repeat regions of
RT nucleoporins are natively unfolded.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003).
RN [15]
RP FUNCTION, AND FG REPEATS IN NPC TRANSPORT.
RX PubMed=15039779; DOI=10.1038/ncb1097;
RA Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.;
RT "Minimal nuclear pore complexes define FG repeat domains essential for
RT transport.";
RL Nat. Cell Biol. 6:197-206(2004).
RN [16]
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).
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. Active directional transport is assured by both, a Phe-Gly
CC (FG) repeat affinity gradient for these transport factors across the
CC NPC and a transport cofactor concentration gradient across the nuclear
CC envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in
CC the nucleus, with GDP in the cytoplasm). NUP49 plays an important role
CC in several nuclear transport pathways including poly(A)+ RNA, tRNA, and
CC pre-ribosome transport. {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687,
CC ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779,
CC ECO:0000269|PubMed:7813444, ECO:0000269|PubMed:8524308,
CC ECO:0000269|PubMed:9017593, ECO:0000269|PubMed:9971735}.
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 NUP49 is part of the NUP57 subcomplex (NIC96, NSP1, NUP49, NUP57)
CC interacting with NUP57. Interacts through its FG repeats with
CC karyopherins. {ECO:0000269|PubMed:10684247}.
CC -!- INTERACTION:
CC Q02199; Q06142: KAP95; NbExp=2; IntAct=EBI-12315, EBI-9145;
CC Q02199; P34077: NIC96; NbExp=3; IntAct=EBI-12315, EBI-12056;
CC Q02199; Q02199: NUP49; NbExp=4; IntAct=EBI-12315, EBI-12315;
CC Q02199; P48837: NUP57; NbExp=9; IntAct=EBI-12315, EBI-12324;
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 -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC FG repeat types and their physico-chemical environment change across
CC the NPC from the nucleoplasmic to the cytoplasmic side: GLFG repeats
CC are especially abundant in NUPs in the central region (lacking a
CC charged environment but are enriched in Ser, Thr, Gln, and Asn).
CC -!- MISCELLANEOUS: Present with 4760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X68109; CAA48229.1; -; Genomic_DNA.
DR EMBL; Z15040; CAA78758.1; -; Genomic_DNA.
DR EMBL; X84705; CAA59181.1; -; Genomic_DNA.
DR EMBL; Z72694; CAA96884.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07941.1; -; Genomic_DNA.
DR PIR; S28026; S28026.
DR RefSeq; NP_011343.1; NM_001181037.1.
DR PDB; 7N85; EM; 7.60 A; C/F/I/L=1-472.
DR PDB; 7N9F; EM; 37.00 A; C/F/I/L=1-472.
DR PDB; 7WOO; EM; 3.71 A; G/J=1-472.
DR PDB; 7WOT; EM; 3.73 A; G/J/S/V=1-472.
DR PDBsum; 7N85; -.
DR PDBsum; 7N9F; -.
DR PDBsum; 7WOO; -.
DR PDBsum; 7WOT; -.
DR AlphaFoldDB; Q02199; -.
DR SASBDB; Q02199; -.
DR SMR; Q02199; -.
DR BioGRID; 33081; 66.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-709N; -.
DR IntAct; Q02199; 25.
DR MINT; Q02199; -.
DR STRING; 4932.YGL172W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; Q02199; -.
DR MaxQB; Q02199; -.
DR PaxDb; Q02199; -.
DR PRIDE; Q02199; -.
DR DNASU; 852703; -.
DR EnsemblFungi; YGL172W_mRNA; YGL172W; YGL172W.
DR GeneID; 852703; -.
DR KEGG; sce:YGL172W; -.
DR SGD; S000003140; NUP49.
DR VEuPathDB; FungiDB:YGL172W; -.
DR eggNOG; KOG0845; Eukaryota.
DR HOGENOM; CLU_039862_0_0_1; -.
DR InParanoid; Q02199; -.
DR OMA; PVNLVDY; -.
DR BioCyc; YEAST:G3O-30660-MON; -.
DR PRO; PR:Q02199; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q02199; protein.
DR GO; GO:0005635; C:nuclear envelope; HDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0044613; C:nuclear pore central transport channel; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:SGD.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006999; P:nuclear pore organization; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0036228; P:protein localization to nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR DisProt; DP02122; -.
DR InterPro; IPR025574; Nucleoporin_FG_rpt.
DR InterPro; IPR039079; Nup49.
DR InterPro; IPR024864; Nup54/Nup57/Nup44.
DR PANTHER; PTHR13000; PTHR13000; 1.
DR PANTHER; PTHR13000:SF2; PTHR13000:SF2; 1.
DR Pfam; PF13634; Nucleoporin_FG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Repeat; Translocation;
KW Transport.
FT CHAIN 1..472
FT /note="Nucleoporin NUP49/NSP49"
FT /id="PRO_0000204867"
FT REPEAT 2..3
FT /note="FG 1"
FT REPEAT 14..17
FT /note="GLFG 1"
FT REPEAT 33..34
FT /note="FG 2"
FT REPEAT 48..51
FT /note="GLFG 2"
FT REPEAT 65..66
FT /note="FG 3"
FT REPEAT 77..78
FT /note="FG 4"
FT REPEAT 86..89
FT /note="GLFG 3"
FT REPEAT 101..104
FT /note="GLFG 4"
FT REPEAT 113..116
FT /note="SLFG 1"
FT REPEAT 125..128
FT /note="GLFG 5"
FT REPEAT 148..151
FT /note="GLFG 6"
FT REPEAT 159..162
FT /note="SLFG 2"
FT REPEAT 175..178
FT /note="GLFG 7; approximate"
FT REPEAT 185..188
FT /note="SLFG 3"
FT REPEAT 199..202
FT /note="GLFG 8"
FT REPEAT 210..213
FT /note="SLFG 4"
FT REPEAT 233..236
FT /note="GLFG 9"
FT REGION 28..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 49142 MW; 0CA7516FF5753CA3 CRC64;
MFGLNKASST PAGGLFGQAS GASTGNANTG FSFGGTQTGQ NTGPSTGGLF GAKPAGSTGG
LGASFGQQQQ QSQTNAFGGS ATTGGGLFGN KPNNTANTGG GLFGANSNSN SGSLFGSNNA
QTSRGLFGNN NTNNINNSSS GMNNASAGLF GSKPAGGTSL FGNTSTSSAP AQNQGMFGAK
PAGTSLFGNN AGNTTTGGGL FGSKPTGATS LFGSSNNNNN NNNSNNIMSA SGGLFGNQQQ
QLQQQPQMQC ALQNLSQLPI TPMTRISELP PQIRQEIEQL DQYIQKQVQI SHHLKADTID
HDELIDSIPR DVAYLLKSES ATSQYLKQDL KKISSFKSLI DEDLLDTQTF SVLLQQLLTP
GSKISSNDLD KFFQKKIHLY EKKLEDYCRI LSDIETAVNG IDTDLFGAPN NPNSTAITAD
LGSSEAENLL QLKTGLAAIV STVIEEFTLF MDIAERIAVL HQKTKTLASL SI
