NU145_YEAST
ID NU145_YEAST Reviewed; 1317 AA.
AC P49687; D6VU53;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Nucleoporin NUP145;
DE EC=3.4.21.-;
DE AltName: Full=Nuclear pore protein NUP145;
DE Contains:
DE RecName: Full=Nucleoporin NUP145N;
DE Short=N-NUP145;
DE Contains:
DE RecName: Full=Nucleoporin NUP145C;
DE Short=C-NUP145;
DE Flags: Precursor;
GN Name=NUP145; Synonyms=RAT10; OrderedLocusNames=YGL092W;
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], AND FUNCTION IN NUCLEAR MRNA EXPORT.
RX PubMed=8044840; DOI=10.1016/0092-8674(94)90297-6;
RA Fabre E., Boelens W.C., Wimmer C., Mattaj I.W., Hurt E.C.;
RT "Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA
RT in vitro via a novel conserved motif.";
RL Cell 78:275-289(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN NPC ASSEMBLY AND
RP DISTRIBUTION.
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=8195299; DOI=10.1083/jcb.125.5.955;
RA Wente S.R., Blobel G.;
RT "NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG)
RT nucleoporin required for nuclear envelope structure.";
RL J. Cell Biol. 125:955-969(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
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, AND NUCLEAR 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 [7]
RP FUNCTION, CLEAVAGE, AND MUTAGENESIS OF HIS-604; PHE-605 AND TRP-608.
RX PubMed=9305650; DOI=10.1093/emboj/16.16.5086;
RA Teixeira M.T., Siniossoglou S., Podtelejnikov S., Benichou J.C., Mann M.,
RA Dujon B., Hurt E.C., Fabre E.;
RT "Two functionally distinct domains generated by in vivo cleavage of
RT Nup145p: a novel biogenesis pathway for nucleoporins.";
RL EMBO J. 16:5086-5097(1997).
RN [8]
RP FUNCTION, AUTOCATALYTIC CLEAVAGE, AND MUTAGENESIS OF SER-606.
RX PubMed=10542288; DOI=10.1074/jbc.274.45.32439;
RA Teixeira M.T., Fabre E., Dujon B.;
RT "Self-catalyzed cleavage of the yeast nucleoporin Nup145p precursor.";
RL J. Biol. Chem. 274:32439-32444(1999).
RN [9]
RP FUNCTION, AND INTERACTION WITH MLP1 AND MLP2.
RX PubMed=10638763; DOI=10.1038/47528;
RA Galy V., Olivo-Marin J.-C., Scherthan H., Doye V., Rascalou N.,
RA Nehrbass U.;
RT "Nuclear pore complexes in the organization of silent telomeric
RT chromatin.";
RL Nature 403:108-112(2000).
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 NUP84 NPC SUBCOMPLEX ASSEMBLY/STRUCTURE.
RX PubMed=11823431; DOI=10.1093/emboj/21.3.387;
RA Lutzmann M., Kunze R., Buerer A., Aebi U., Hurt E.C.;
RT "Modular self-assembly of a Y-shaped multiprotein complex from seven
RT nucleoporins.";
RL EMBO J. 21:387-397(2002).
RN [12]
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 [13]
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 [14]
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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-751, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-679; SER-689 AND
RP THR-751, AND IDENTIFICATION BY 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-403; SER-404;
RP SER-414; SER-667; SER-679 AND SER-689, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 731-1158 IN COMPLEX WITH HUMAN
RP SEC13.
RX PubMed=18160040; DOI=10.1016/j.cell.2007.11.038;
RA Hsia K.C., Stavropoulos P., Blobel G., Hoelz A.;
RT "Architecture of a coat for the nuclear pore membrane.";
RL Cell 131:1313-1326(2007).
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). NUP145 is autocatalytically
CC cleaved in vivo in 2 polypeptides which assume different functions in
CC the NPC. NUP145N as one of the FG repeat nucleoporins participates in
CC karyopherin interactions and contains part of the autocatalytic
CC cleavage activity. NUP145C as part of the NUP84 complex is involved in
CC nuclear poly(A)+ RNA and tRNA export. It is also required for normal
CC NPC distribution (probably through interactions with MLP1 and MLP2) and
CC NPC assembly, as well as for normal nuclear envelope organization.
CC {ECO:0000269|PubMed:10542288, ECO:0000269|PubMed:10638763,
CC ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11823431,
CC ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779,
CC ECO:0000269|PubMed:8044840, ECO:0000269|PubMed:8195299,
CC ECO:0000269|PubMed:8524308, ECO:0000269|PubMed:9305650}.
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 NUP145C is part of the heptameric 0.5 MDa autoassembling NUP84 NPC
CC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1).
CC NUP145N may bind homomeric RNA and interacts through its FG repeats
CC with karyopherins. Interacts with MLP1 and MLP2.
CC {ECO:0000269|PubMed:10638763, ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:18160040}.
CC -!- INTERACTION:
CC P49687; P35729: NUP120; NbExp=23; IntAct=EBI-11730, EBI-11713;
CC P49687; P38181: NUP170; NbExp=3; IntAct=EBI-11730, EBI-11756;
CC P49687; P47054: NUP192; NbExp=2; IntAct=EBI-11730, EBI-25846;
CC P49687; P52891: NUP84; NbExp=17; IntAct=EBI-11730, EBI-12337;
CC P49687; P46673: NUP85; NbExp=12; IntAct=EBI-11730, EBI-12345;
CC P49687; Q04491: SEC13; NbExp=24; IntAct=EBI-11730, EBI-16529;
CC P49687; P55735: SEC13; Xeno; NbExp=15; IntAct=EBI-11730, EBI-1046596;
CC -!- SUBCELLULAR LOCATION: [Nucleoporin NUP145C]: Nucleus, nuclear pore
CC complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral
CC membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral
CC membrane protein; Nucleoplasmic side. Note=Symmetrically distributed on
CC the cytoplasmic and nucleoplasmic side of nuclear envelope.
CC -!- SUBCELLULAR LOCATION: [Nucleoporin NUP145N]: Nucleus, nuclear pore
CC complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral
CC membrane protein; Nucleoplasmic side. Note=Biased towards the
CC nucleoplasmic side, nuclear pore complex.
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 -!- PTM: NUP145 is autocatalytically cleaved in NUP145N and NUP145C.
CC {ECO:0000269|PubMed:9305650}.
CC -!- MISCELLANEOUS: Present with 4630 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; X76557; CAA54057.1; -; Genomic_DNA.
DR EMBL; Z32672; CAA83584.1; -; Genomic_DNA.
DR EMBL; Z72614; CAA96798.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08014.1; -; Genomic_DNA.
DR PIR; A54831; A54831.
DR RefSeq; NP_011423.1; NM_001180957.1.
DR PDB; 3BG0; X-ray; 3.15 A; B/C/F/G=731-1158.
DR PDB; 3BG1; X-ray; 3.00 A; B/C/F/G=731-1158.
DR PDB; 3IKO; X-ray; 3.20 A; B/E/H=731-1158.
DR PDB; 3JRO; X-ray; 4.00 A; A=714-1160.
DR PDB; 3JRP; X-ray; 2.60 A; A=714-784.
DR PDB; 3KEP; X-ray; 1.82 A; A/B=442-605.
DR PDB; 3KES; X-ray; 2.10 A; A/B=442-605.
DR PDB; 4XMM; X-ray; 7.38 A; B=680-1317.
DR PDB; 4XMN; X-ray; 7.60 A; B=680-1317.
DR PDB; 7N84; EM; 11.60 A; c/n=606-1317.
DR PDB; 7N9F; EM; 37.00 A; c/j=606-1317.
DR PDBsum; 3BG0; -.
DR PDBsum; 3BG1; -.
DR PDBsum; 3IKO; -.
DR PDBsum; 3JRO; -.
DR PDBsum; 3JRP; -.
DR PDBsum; 3KEP; -.
DR PDBsum; 3KES; -.
DR PDBsum; 4XMM; -.
DR PDBsum; 4XMN; -.
DR PDBsum; 7N84; -.
DR PDBsum; 7N9F; -.
DR AlphaFoldDB; P49687; -.
DR SMR; P49687; -.
DR BioGRID; 33159; 277.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2074N; -.
DR IntAct; P49687; 21.
DR MINT; P49687; -.
DR STRING; 4932.YGL092W; -.
DR MEROPS; S59.002; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P49687; -.
DR MaxQB; P49687; -.
DR PaxDb; P49687; -.
DR PRIDE; P49687; -.
DR DNASU; 852788; -.
DR EnsemblFungi; YGL092W_mRNA; YGL092W; YGL092W.
DR GeneID; 852788; -.
DR KEGG; sce:YGL092W; -.
DR SGD; S000003060; NUP145.
DR VEuPathDB; FungiDB:YGL092W; -.
DR eggNOG; KOG0845; Eukaryota.
DR HOGENOM; CLU_005908_0_0_1; -.
DR InParanoid; P49687; -.
DR OMA; KGFEWPY; -.
DR BioCyc; YEAST:G3O-30592-MON; -.
DR EvolutionaryTrace; P49687; -.
DR PRO; PR:P49687; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P49687; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
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:0044613; C:nuclear pore central transport channel; IDA:SGD.
DR GO; GO:0031080; C:nuclear pore outer ring; IDA:SGD.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IGI:SGD.
DR GO; GO:0051664; P:nuclear pore localization; IMP:SGD.
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:0045893; P:positive regulation of transcription, DNA-templated; IDA:SGD.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IGI:SGD.
DR GO; GO:0036228; P:protein localization to nuclear inner membrane; IGI:SGD.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0034398; P:telomere tethering at nuclear periphery; IMP:SGD.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR DisProt; DP02155; -.
DR Gene3D; 3.30.1610.10; -; 1.
DR InterPro; IPR025574; Nucleoporin_FG_rpt.
DR InterPro; IPR037665; Nucleoporin_S59-like.
DR InterPro; IPR037637; NUP98-NUP96.
DR InterPro; IPR007230; Nup98_auto-Pept-S59_dom.
DR InterPro; IPR036903; Nup98_auto-Pept-S59_dom_sf.
DR InterPro; IPR021967; Nup98_C.
DR PANTHER; PTHR23198; PTHR23198; 2.
DR PANTHER; PTHR23198:SF17; PTHR23198:SF17; 2.
DR Pfam; PF04096; Nucleoporin2; 1.
DR Pfam; PF13634; Nucleoporin_FG; 1.
DR Pfam; PF12110; Nup96; 1.
DR SUPFAM; SSF82215; SSF82215; 1.
DR PROSITE; PS51434; NUP_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Hydrolase; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; RNA-binding; Translocation; Transport.
FT CHAIN 1..605
FT /note="Nucleoporin NUP145N"
FT /id="PRO_0000019927"
FT CHAIN 606..1317
FT /note="Nucleoporin NUP145C"
FT /id="PRO_0000019928"
FT REPEAT 12..13
FT /note="FG 1"
FT REPEAT 39..42
FT /note="GLFG 1"
FT REPEAT 79..80
FT /note="FG 2"
FT REPEAT 89..92
FT /note="GLFG 2"
FT REPEAT 106..107
FT /note="FG 3"
FT REPEAT 136..139
FT /note="GLFG 3"
FT REPEAT 154..157
FT /note="GLFG 4"
FT REPEAT 168..171
FT /note="GLFG 5"
FT REPEAT 181..184
FT /note="GLFG 6"
FT REPEAT 193..196
FT /note="GLFG 7; approximate"
FT REPEAT 206..209
FT /note="GLFG 8"
FT DOMAIN 458..605
FT /note="Peptidase S59"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00765"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..523
FT /note="Required for autocatalytic cleavage"
FT REGION 460..604
FT /note="Nucleoporin RNA-binding motif (NRM)"
FT MOTIF 369..385
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 133..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 751
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MUTAGEN 604
FT /note="H->P: Loss of autocatalytic cleavage; when
FT associated with L-608."
FT /evidence="ECO:0000269|PubMed:9305650"
FT MUTAGEN 605
FT /note="F->S: Loss of autocatalytic cleavage; when
FT associated with R-608."
FT /evidence="ECO:0000269|PubMed:9305650"
FT MUTAGEN 606
FT /note="S->A: Loss of autocatalytic cleavage."
FT /evidence="ECO:0000269|PubMed:10542288"
FT MUTAGEN 608
FT /note="W->L: Loss of autocatalytic cleavage; when
FT associated with P-604."
FT /evidence="ECO:0000269|PubMed:9305650"
FT MUTAGEN 608
FT /note="W->R: Loss of autocatalytic cleavage; when
FT associated with F-605."
FT /evidence="ECO:0000269|PubMed:9305650"
FT CONFLICT 281..282
FT /note="NA -> QR (in Ref. 2; CAA83584)"
FT /evidence="ECO:0000305"
FT CONFLICT 1142
FT /note="L -> S (in Ref. 2; CAA83584)"
FT /evidence="ECO:0000305"
FT CONFLICT 1310..1316
FT /note="LMKCTYK -> FEVYI (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 454..458
FT /evidence="ECO:0007829|PDB:3KES"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:3KEP"
FT HELIX 467..471
FT /evidence="ECO:0007829|PDB:3KEP"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:3KEP"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:3KEP"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:3KEP"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:3KEP"
FT STRAND 492..498
FT /evidence="ECO:0007829|PDB:3KEP"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:3KEP"
FT HELIX 509..513
FT /evidence="ECO:0007829|PDB:3KEP"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:3KEP"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:3KEP"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:3KEP"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:3KEP"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:3KEP"
FT STRAND 546..552
FT /evidence="ECO:0007829|PDB:3KEP"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:3KEP"
FT HELIX 570..582
FT /evidence="ECO:0007829|PDB:3KEP"
FT STRAND 584..592
FT /evidence="ECO:0007829|PDB:3KEP"
FT TURN 593..596
FT /evidence="ECO:0007829|PDB:3KEP"
FT STRAND 597..603
FT /evidence="ECO:0007829|PDB:3KEP"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:3JRP"
FT TURN 731..733
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 741..747
FT /evidence="ECO:0007829|PDB:3JRP"
FT STRAND 757..760
FT /evidence="ECO:0007829|PDB:3JRP"
FT TURN 761..763
FT /evidence="ECO:0007829|PDB:3JRP"
FT STRAND 764..768
FT /evidence="ECO:0007829|PDB:3JRP"
FT STRAND 772..780
FT /evidence="ECO:0007829|PDB:3JRP"
FT HELIX 788..791
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 793..801
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 803..807
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 809..812
FT /evidence="ECO:0007829|PDB:3IKO"
FT STRAND 814..819
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 823..827
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 835..846
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 859..881
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 883..891
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 896..904
FT /evidence="ECO:0007829|PDB:3BG1"
FT TURN 905..907
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 909..918
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 922..931
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 936..948
FT /evidence="ECO:0007829|PDB:3BG1"
FT TURN 950..952
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 958..968
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 971..974
FT /evidence="ECO:0007829|PDB:3BG0"
FT HELIX 979..983
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 987..996
FT /evidence="ECO:0007829|PDB:3BG1"
FT TURN 997..1002
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 1005..1015
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 1023..1032
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 1034..1036
FT /evidence="ECO:0007829|PDB:3IKO"
FT HELIX 1037..1045
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 1053..1064
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 1073..1089
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 1093..1100
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 1106..1119
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 1122..1124
FT /evidence="ECO:0007829|PDB:3BG1"
FT TURN 1126..1129
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 1132..1135
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 1140..1157
FT /evidence="ECO:0007829|PDB:3BG1"
SQ SEQUENCE 1317 AA; 145661 MW; 59399D86BB553030 CRC64;
MFNKSVNSGF TFGNQNTSTP TSTPAQPSSS LQFPQKSTGL FGNVNVNANT STPSPSGGLF
NANSNANSIS QQPANNSLFG NKPAQPSGGL FGATNNTTSK SAGSLFGNNN ATANSTGSTG
LFSGSNNIAS STQNGGLFGN SNNNNITSTT QNGGLFGKPT TTPAGAGGLF GNSSSTNSTT
GLFGSNNTQS STGIFGQKPG ASTTGGLFGN NGASFPRSGE TTGTMSTNPY GINISNVPMA
VADMPRSITS SLSDVNGKSD AEPKPIENRR TYSFSSSVSG NAPLPLASQS SLVSRLSTRL
KATQKSTSPN EIFSPSYSKP WLNGAGSAPL VDDFFSSKMT SLAPNENSIF PQNGFNFLSS
QRADLTELRK LKIDSNRSAA KKLKLLSGTP AITKKHMQDE QDSSENEPIA NADSVTNIDR
KENRDNNLDN TYLNGKEQSN NLNKQDGENT LQHEKSSSFG YWCSPSPEQL ERLSLKQLAA
VSNFVIGRRG YGCITFQHDV DLTAFTKSFR EELFGKIVIF RSSKTVEVYP DEATKPMIGH
GLNVPAIITL ENVYPVDKKT KKPMKDTTKF AEFQVFDRKL RSMREMNYIS YNPFGGTWTF
KVNHFSIWGL VNEEDAEIDE DDLSKQEDGG EQPLRKVRTL AQSKPSDKEV ILKTDGTFGT
LSGKDDSIVE EKAYEPDLSD ADFEGIEASP KLDVSKDWVE QLILAGSSLR SVFATSKEFD
GPCQNEIDLL FSECNDEIDN AKLIMKERRF TASYTFAKFS TGSMLLTKDI VGKSGVSIKR
LPTELQRKFL FDDVYLDKEI EKVTIEARKS NPYPQISESS LLFKDALDYM EKTSSDYNLW
KLSSILFDPV SYPYKTDNDQ VKMALLKKER HCRLTSWIVS QIGPEIEEKI RNSSNEIEQI
FLYLLLNDVV RASKLAIESK NGHLSVLISY LGSNDPRIRD LAELQLQKWS TGGCSIDKNI
SKIYKLLSGS PFEGLFSLKE LESEFSWLCL LNLTLCYGQI DEYSLESLVQ SHLDKFSLPY
DDPIGVIFQL YAANENTEKL YKEVRQRTNA LDVQFCWYLI QTLRFNGTRV FSKETSDEAT
FAFAAQLEFA QLHGHSLFVS CFLNDDKAAE DTIKRLVMRE ITLLRASTND HILNRLKIPS
QLIFNAQALK DRYEGNYLSE VQNLLLGSSY DLAEMAIVTS LGPRLLLSNN PVQNNELKTL
REILNEFPDS ERDKWSVSIN VFEVYLKLVL DNVETQETID SLISGMKIFY DQYKHCREVA
ACCNVMSQEI VSKILEKNNP SIGDSKAKLL ELPLGQPEKA YLRGEFAQDL MKCTYKI
