NU157_YEAST
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 03-AUG-2022, entry version 173.
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 PDBsum; 4MHC; -.
DR PDBsum; 7N85; -.
DR PDBsum; 7N9F; -.
DR PDBsum; 7WOO; -.
DR PDBsum; 7WOT; -.
DR AlphaFoldDB; P40064; -.
DR SMR; P40064; -.
DR BioGRID; 36851; 87.
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; P40064; -.
DR PRIDE; P40064; -.
DR TopDownProteomics; P40064; -.
DR DNASU; 856842; -.
DR EnsemblFungi; YER105C_mRNA; YER105C; YER105C.
DR GeneID; 856842; -.
DR KEGG; sce:YER105C; -.
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; VACTNKG; -.
DR BioCyc; YEAST:G3O-30270-MON; -.
DR PRO; PR:P40064; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40064; 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: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; IC: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; 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; 1.25.40.440; -; 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; 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
