ID   NU157_YEAST             Reviewed;        1391 AA.
AC   P40064; D3DM12;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Nucleoporin NUP157;
DE   AltName: Full=Nuclear pore protein NUP157;
GN   Name=NUP157; OrderedLocusNames=YER105C;
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=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
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   CHARACTERIZATION, AND PROTEIN SEQUENCE OF 1016-1030 AND 1349-1367.
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   [4]
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   [5]
RP   FUNCTION, AND INTERACTION WITH NUP170 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   [6]
RP   INTERACTION WITH MAD2 AND NUP53.
RX   PubMed=10688190; DOI=10.1038/35001009;
RA   Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R.,
RA   Lockshon D., Narayan V., Srinivasan M., Pochart P., Qureshi-Emili A.,
RA   Li Y., Godwin B., Conover D., Kalbfleisch T., Vijayadamodar G., Yang M.,
RA   Johnston M., Fields S., Rothberg J.M.;
RT   "A comprehensive analysis of protein-protein interactions in Saccharomyces
RT   cerevisiae.";
RL   Nature 403:623-627(2000).
RN   [7]
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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, 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   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(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. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:12473689}.
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       NUP157 may be part of a NPC subcomplex containing NUP53, NUP170, and
CC       NUP59. In addition it may bind to MAD2. {ECO:0000269|PubMed:10684247}.
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   -!- MISCELLANEOUS: Present with 4420 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; U18839; AAB64660.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07766.1; -; Genomic_DNA.
DR   PIR; S50608; S50608.
DR   RefSeq; NP_011031.1; NM_001178996.1.
DR   PDB; 4MHC; X-ray; 2.40 A; A=70-893.
DR   PDB; 7N85; EM; 7.60 A; 1/Z=1-1391.
DR   PDB; 7N9F; EM; 37.00 A; 1/Z=1-1391.
DR   PDB; 7WOO; EM; 3.71 A; C=1-1391.
DR   PDB; 7WOT; EM; 3.73 A; C/O=1-1391.
DR   PDB; 8TJ5; EM; 6.60 A; 1/Z=1-1391.
DR   PDBsum; 4MHC; -.
DR   PDBsum; 7N85; -.
DR   PDBsum; 7N9F; -.
DR   PDBsum; 7WOO; -.
DR   PDBsum; 7WOT; -.
DR   PDBsum; 8TJ5; -.
DR   AlphaFoldDB; P40064; -.
DR   EMDB; EMD-24232; -.
DR   EMDB; EMD-24258; -.
DR   EMDB; EMD-32653; -.
DR   EMDB; EMD-32658; -.
DR   EMDB; EMD-41300; -.
DR   SMR; P40064; -.
DR   BioGRID; 36851; 93.
DR   ComplexPortal; CPX-824; Nuclear pore complex.
DR   DIP; DIP-846N; -.
DR   IntAct; P40064; 16.
DR   MINT; P40064; -.
DR   STRING; 4932.YER105C; -.
DR   TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR   iPTMnet; P40064; -.
DR   MaxQB; P40064; -.
DR   PaxDb; 4932-YER105C; -.
DR   PeptideAtlas; P40064; -.
DR   TopDownProteomics; P40064; -.
DR   DNASU; 856842; -.
DR   EnsemblFungi; YER105C_mRNA; YER105C; YER105C.
DR   GeneID; 856842; -.
DR   KEGG; sce:YER105C; -.
DR   AGR; SGD:S000000907; -.
DR   SGD; S000000907; NUP157.
DR   VEuPathDB; FungiDB:YER105C; -.
DR   eggNOG; KOG1900; Eukaryota.
DR   GeneTree; ENSGT00390000016532; -.
DR   HOGENOM; CLU_000429_0_1_1; -.
DR   InParanoid; P40064; -.
DR   OMA; SELFACY; -.
DR   OrthoDB; 52774at2759; -.
DR   BioCyc; YEAST:G3O-30270-MONOMER; -.
DR   BioGRID-ORCS; 856842; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40064; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40064; Protein.
DR   GO; GO:0005635; C:nuclear envelope; NAS: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:0003677; F:DNA binding; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IDA:SGD.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IGI: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; NAS:ComplexPortal.
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; IBA:GO_Central.
DR   GO; GO:0036228; P:protein localization to nuclear inner membrane; IBA:GO_Central.
DR   GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR   Gene3D; 1.10.167.20; -; 1.
DR   Gene3D; 1.20.120.1050; -; 1.
DR   Gene3D; 1.20.58.1780; -; 1.
DR   Gene3D; 1.25.40.440; Nucleoporin, helical domain, central subdomain; 1.
DR   Gene3D; 1.25.40.450; Nucleoporin, helical domain, N-terminal subdomain; 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; NUCLEAR PORE COMPLEX PROTEIN NUP155; 1.
DR   PANTHER; PTHR10350:SF6; NUCLEAR PORE COMPLEX PROTEIN NUP155; 1.
DR   Pfam; PF03177; Nucleoporin_C; 1.
DR   Pfam; PF08801; Nucleoporin_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Membrane;
KW   mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Translocation; Transport.
FT   CHAIN           1..1391
FT                   /note="Nucleoporin NUP157"
FT                   /id="PRO_0000204848"
FT   REGION          21..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1372..1391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         1034
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   HELIX           90..106
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          122..128
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            129..132
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          138..145
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           148..151
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            152..154
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          161..166
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            167..170
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          171..176
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          179..184
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            185..187
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          201..207
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            214..217
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          218..237
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          244..254
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            256..258
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          260..266
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            267..270
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          271..276
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          284..286
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          303..307
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          341..348
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            349..352
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          353..358
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          363..369
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          372..379
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           381..391
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           397..399
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            401..403
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          406..411
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            414..416
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          418..426
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          431..435
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          447..452
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           483..486
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          500..502
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            503..505
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          506..512
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          536..543
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           545..551
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          555..560
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          567..574
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          581..583
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            584..587
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           589..592
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            593..595
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          600..614
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           617..623
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            624..626
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           629..635
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           637..649
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           655..667
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            670..672
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           707..719
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   TURN            720..725
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          726..729
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   STRAND          745..747
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           749..768
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           770..772
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           787..815
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           816..818
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           819..829
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           838..845
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           849..853
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           857..872
FT                   /evidence="ECO:0007829|PDB:4MHC"
FT   HELIX           879..890
FT                   /evidence="ECO:0007829|PDB:4MHC"
SQ   SEQUENCE   1391 AA;  156649 MW;  CB47CEE27AB4FCE3 CRC64;
     MYSTPLKKRI DYDRETFTAS ASLGGNRLRN RPRDDQNNGK PNLSSRSFLS ERKTRKDVLN
     KYGEAGNTIE SELRDVTTHV KISGLTSSEP LQLASEFVQD LSFRDRNTPI LDNPDYYSKG
     LDYNFSDEVG GLGAFTPFQR QQVTNIPDEV LSQVSNTEIK SDMGIFLELN YCWITSDNKL
     ILWNINNSSE YHCIDEIEHT ILKVKLVKPS PNTFVSSVEN LLIVATLFDI YILTISFNDR
     THELNIFNTG LKVNVTGFNV SNIISYERTG QIFFTGATDG VNVWELQYNC SENLFNSKSN
     KICLTKSNLA NLLPTKLIPS IPGGKLIQKV LEGDAGTEEE TISQLEVDQS RGVLHTLSTK
     SIVRSYLITS NGLVGPVLID AAHIRRGMNA LGVKNSPLLS NRAFKIAKIV SISMCENNDL
     FLAVITTTGV RLYFKGSISR RSIGSLKLDS VKFPPTSISS SLEQNKSFII GHHPLNTHDT
     GPLSTQKASS TYINTTCAST IISPGIYFTC VRKRANSGEL SKGITNKALL ENKEEHKLYV
     SAPDYGILKN YGKYVENTAL LDTTDEIKEI VPLTRSFNYT STPQGYANVF ASQYSAEPLK
     VAVLTSNALE IYCYRTPDEV FESLIENPLP FIHSYGLSEA CSTALYLACK FNKSEHIKSS
     ALAFFSAGIP GVVEIKPKSS RESGSVPPIS QNLFDKSGEC DGIVLSPRFY GSALLITRLF
     SQIWEERVFV FKRASKTEKM DAFGISITRP QVEYYLSSIS VLADFFNIHR PSFVSFVPPK
     GSNAITASDA ESIAMNALIL LINSIKDALS LINVFYEDID AFKSLLNTLM GAGGVYDSKT
     REYFFDLKFH DLFTPNAKTK QLIKEILIEV VNANIASGTS ADYIVNVLKE RFGSFCHSAD
     ILCYRAGEHL EAAQKFEMID SKISRNHLDT AIDLYERCAE NIELCELRRV VDIMVKLNYQ
     PKTVGFLLRF ADKIDKGNQA QEYVSRGCNT ADPRKVFYDK RINVYTLIFE IVKSVDDYTS
     IEQSPSIANI SIFSPASSLK KRVYSVIMNS NNRFFHYCFY DWLVANKRQD YLLRLDSQFV
     LPYLKERAEK SLEISNLLWF YLFKEEHFLE AADVLYALAS SDFDLKLSER IECLARANGL
     CDSSTSFDQK PALVQLSENI HELFDIASIQ DDLLNLVRNE TRIDEDYRKQ LTLKLNGRVL
     PLSDLFNDCA DPLDYYEIKL RIFKVSQFKD EKVIQGEWNR LLDSMKNAPS PDVGSVGQES
     FLSSISNTLI RIGKTTRDTD VVFPVHFLMN KILESFIDKS SAADGSVCSM FLLAGVSHLK
     LYYILSRIIE NSEGNVELAK KEMVWLIKDW YQSDSDLRGS IAPEQIKKLE KYDPNTDPVQ
     DYVKDRHHGL K
//