NUP88_ARATH
ID NUP88_ARATH Reviewed; 810 AA.
AC Q9FFK6; Q0WPM6;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Nuclear pore complex protein NUP88 {ECO:0000303|PubMed:21189294};
DE AltName: Full=Nucleoporin 88;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2789;
DE AltName: Full=Protein MODIFIER OF SNC1,7 {ECO:0000303|PubMed:19700630};
GN Name=NUP88 {ECO:0000303|PubMed:21189294};
GN Synonyms=EMB2789, MOS7 {ECO:0000303|PubMed:19700630};
GN OrderedLocusNames=At5g05680 {ECO:0000312|Araport:AT5G05680};
GN ORFNames=MJJ3.8 {ECO:0000312|EMBL:BAB09662.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, MUTAGENESIS OF 190-PHE--SER-193, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19700630; DOI=10.1105/tpc.108.064519;
RA Cheng Y.T., Germain H., Wiermer M., Bi D., Xu F., Garcia A.V.,
RA Wirthmueller L., Despres C., Parker J.E., Zhang Y., Li X.;
RT "Nuclear pore complex component MOS7/Nup88 is required for innate immunity
RT and nuclear accumulation of defense regulators in Arabidopsis.";
RL Plant Cell 21:2503-2516(2009).
RN [5]
RP FUNCTION.
RX PubMed=21327081; DOI=10.4161/nucl.1.4.12109;
RA Wiermer M., Germain H., Cheng Y.T., Garcia A.V., Parker J.E., Li X.;
RT "Nucleoporin MOS7/Nup88 contributes to plant immunity and nuclear
RT accumulation of defense regulators.";
RL Nucleus 1:332-336(2010).
RN [6]
RP IDENTIFICATION IN THE NUCLEAR PORE COMPLEX BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND NOMENCLATURE.
RX PubMed=21189294; DOI=10.1105/tpc.110.079947;
RA Tamura K., Fukao Y., Iwamoto M., Haraguchi T., Hara-Nishimura I.;
RT "Identification and characterization of nuclear pore complex components in
RT Arabidopsis thaliana.";
RL Plant Cell 22:4084-4097(2010).
CC -!- FUNCTION: Involved in the regulation of exportin-mediated nuclear
CC protein export. Required for resistance mediated by multiple R proteins
CC and for the appropriate nuclear accumulation of SNC1 and of the
CC downstream defense signaling components EDS1 and NPR1. Not involved in
CC salt tolerance, ethylene and auxin responses, but required for systemic
CC acquired resistance. {ECO:0000269|PubMed:19700630,
CC ECO:0000269|PubMed:21327081}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC). The NPC has an eight-
CC fold symmetrical structure comprising a central transport channel and
CC two rings, the cytoplasmic and nuclear rings, to which eight filaments
CC are attached. The cytoplasmic filaments have loose ends, while the
CC nuclear filaments are joined in a distal ring, forming a nuclear
CC basket. NPCs are highly dynamic in configuration and composition, and
CC can be devided in 3 subcomplexes, the NUP62 subcomplex, the NUP107-160
CC subcomplex and the NUP93 subcomplex, containing approximately 30
CC different nucleoporin proteins. {ECO:0000305|PubMed:21189294}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:19700630,
CC ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex
CC {ECO:0000305|PubMed:19700630, ECO:0000305|PubMed:21189294}.
CC -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000269|PubMed:19700630}.
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DR EMBL; AB005237; BAB09662.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90908.1; -; Genomic_DNA.
DR EMBL; AK229039; BAF00923.1; -; mRNA.
DR RefSeq; NP_196187.1; NM_120650.4.
DR AlphaFoldDB; Q9FFK6; -.
DR SMR; Q9FFK6; -.
DR BioGRID; 15731; 8.
DR STRING; 3702.AT5G05680.1; -.
DR iPTMnet; Q9FFK6; -.
DR PaxDb; Q9FFK6; -.
DR PRIDE; Q9FFK6; -.
DR ProteomicsDB; 248752; -.
DR EnsemblPlants; AT5G05680.1; AT5G05680.1; AT5G05680.
DR GeneID; 830452; -.
DR Gramene; AT5G05680.1; AT5G05680.1; AT5G05680.
DR KEGG; ath:AT5G05680; -.
DR Araport; AT5G05680; -.
DR TAIR; locus:2166424; AT5G05680.
DR eggNOG; KOG4460; Eukaryota.
DR HOGENOM; CLU_023826_0_0_1; -.
DR InParanoid; Q9FFK6; -.
DR OMA; VFILFTD; -.
DR OrthoDB; 1149034at2759; -.
DR PhylomeDB; Q9FFK6; -.
DR PRO; PR:Q9FFK6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFK6; baseline and differential.
DR Genevisible; Q9FFK6; AT.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0005643; C:nuclear pore; IDA:TAIR.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006611; P:protein export from nucleus; IMP:TAIR.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0009627; P:systemic acquired resistance; IMP:TAIR.
DR InterPro; IPR019321; Nucleoporin_Nup88.
DR InterPro; IPR037700; NUP88/NUP82.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13257; PTHR13257; 1.
DR Pfam; PF10168; Nup88; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Coiled coil; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..810
FT /note="Nuclear pore complex protein NUP88"
FT /id="PRO_0000431085"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 646..748
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 190..193
FT /note="Missing: In mos7-1; enhanced disease
FT susceptibility."
FT /evidence="ECO:0000269|PubMed:19700630"
FT CONFLICT 244
FT /note="G -> D (in Ref. 3; BAF00923)"
SQ SEQUENCE 810 AA; 89731 MW; 79E20A5E4B8DF069 CRC64;
MKFNFNETED APDSRRSPTP KEPVRWVPLQ SHPVFASLPS SQDEPAVSQL FPRNFMAWDG
DSRVYYWDSR RYLLHRLSLR LGEPEPSSVL AAVPSKVMQP DLQVTFSVSK ISINKSGSAV
LLAGSDGICV MYLFGRASVI EDNVICRVVS IGSEIYTSSD SAITLLQASW HPDSDTHLGI
LSSDAVFRLF DLSSDTELPE QEYYLQPGEP GRSRTASSIY PADFSFGGDH LWDRFTVFIL
FTDGSIYILC PVVPFGSVYK WESVMEIYND ANMYGVKSSN SLAVSNSSLA IEWLEATFPD
LTEQGTRGEN ILVVKAQPYA LLDASLALQG PLYKASSGDG DEDFAVREAE CKGRAVSLLY
NLVSKDSILV TAWSAGQLQV DALVDEIQPV WISGNSSRLR MNSHNKIQGV AMICESNISE
LPVATSNLPL DHTVWLGHPP PLLRLAMVDL ALPKMREGGS LVTLFADSLL PERIYSLHDG
GIDSTVLHSL PFTSQASGKD EALKTPSVHT VLSTCQEESA VSPLLGFVPL SDSFGYSWIV
AVLSSGECIV AEMKTWDLLL PIHVSTDKTV SSSAIEKKEQ ENSCIISKEL LAGPKIRIAP
HALPNQRSTP ANSVEGRSIL LDYVKLFHEN YIEYAHKVHF ELQHHAPNLK RIIDDQHQRL
AEANEKISKV EKNQSFLEKR IDKAIERHDS LEQCLQRLRS LPGTHKKPLT RAELDFKSEL
DQYAGVEVDA LQSSIETLRA RVKKSTQKSH KGTVVAASQK KQYSKKNLIQ DTQMSQLQST
LAKLSLMNSD NSKKVKIVES ALKSQESSFM
