NUP96_ARATH
ID NUP96_ARATH Reviewed; 1046 AA.
AC Q8LLD0; Q38941; Q8LLD1;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Nuclear pore complex protein NUP96 {ECO:0000303|PubMed:21189294};
DE Short=AtNUP96;
DE AltName: Full=Nucleoporin 96 {ECO:0000303|PubMed:21189294};
DE AltName: Full=Nucleoporin PRECOCIOUS;
DE AltName: Full=Nucleoporin PRECOZ;
DE AltName: Full=Protein MODIFIER OF SNC1 3 {ECO:0000303|PubMed:15772285};
DE AltName: Full=Protein SUPPRESSOR OF AUXIN RESISTANCE 3 {ECO:0000303|PubMed:16751346};
GN Name=NUP96 {ECO:0000303|PubMed:21189294};
GN Synonyms=MOS3 {ECO:0000303|PubMed:15772285}, PRE,
GN SAR3 {ECO:0000303|PubMed:16751346};
GN OrderedLocusNames=At1g80680 {ECO:0000312|Araport:AT1G80680};
GN ORFNames=F23A5.3 {ECO:0000312|EMBL:AAF14656.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15772285; DOI=10.1105/tpc.104.029926;
RA Zhang Y., Li X.;
RT "A putative nucleoporin 96 is required for both basal defense and
RT constitutive resistance responses mediated by suppressor of npr1-
RT 1,constitutive 1.";
RL Plant Cell 17:1306-1316(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RA Alonso Blanco C., Martinez-Zapater J.M.;
RT "A mutation in PRECOZ (PRE) causes early flowering and supresses late
RT flowering mutant phenotypes in Arabidopsis.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Goodman H.M., Gallant P., Keifer-Higgins S., Rubenfield M., Church G.M.;
RT "A 37.5 Kb sequence from Arabidopsis thaliana chromosome I.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16751346; DOI=10.1105/tpc.106.041566;
RA Parry G., Ward S., Cernac A., Dharmasiri S., Estelle M.;
RT "The Arabidopsis SUPPRESSOR OF AUXIN RESISTANCE proteins are nucleoporins
RT with an important role in hormone signaling and development.";
RL Plant Cell 18:1590-1603(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, 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).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21203492; DOI=10.1371/journal.pgen.1001250;
RA Germain H., Qu N., Cheng Y.T., Lee E., Huang Y., Dong O.X., Gannon P.,
RA Huang S., Ding P., Li Y., Sack F., Zhang Y., Li X.;
RT "MOS11: a new component in the mRNA export pathway.";
RL PLoS Genet. 6:E1001250-E1001250(2010).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22288649; DOI=10.1111/j.1365-313x.2012.04928.x;
RA Wiermer M., Cheng Y.T., Imkampe J., Li M., Wang D., Lipka V., Li X.;
RT "Putative members of the Arabidopsis Nup107-160 nuclear pore sub-complex
RT contribute to pathogen defense.";
RL Plant J. 70:796-808(2012).
CC -!- FUNCTION: Contributes to the transfer of mature mRNA from the nucleus
CC to the cytosol. Required for both R gene-mediated and basal disease
CC resistance. RNA export seems to play a critical role in stress
CC responses and regulation of plant growth and development.
CC {ECO:0000269|PubMed:15772285, ECO:0000269|PubMed:16751346,
CC ECO:0000269|PubMed:21203492, ECO:0000269|PubMed:22288649}.
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 membrane {ECO:0000269|PubMed:16751346};
CC Peripheral membrane protein {ECO:0000269|PubMed:16751346};
CC Nucleoplasmic side {ECO:0000269|PubMed:16751346}. Nucleus, nuclear pore
CC complex {ECO:0000269|PubMed:15772285, ECO:0000269|PubMed:21203492}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:16751346}.
CC -!- DISRUPTION PHENOTYPE: Pleiotropic phenotype with diverse growth defects
CC and early flowering. {ECO:0000269|PubMed:15772285,
CC ECO:0000269|PubMed:16751346, ECO:0000269|PubMed:21203492,
CC ECO:0000269|PubMed:22288649}.
CC -!- MISCELLANEOUS: Unlike in mammals and yeast, NUP96 and NUP98 are not
CC translated as a polyprotein. {ECO:0000305|PubMed:15772285}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA98914.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF14656.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY942798; AAX44044.1; -; mRNA.
DR EMBL; AF411838; AAN03675.1; -; Genomic_DNA.
DR EMBL; AF411839; AAN03676.1; -; mRNA.
DR EMBL; U53501; AAA98914.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011713; AAF14656.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36436.1; -; Genomic_DNA.
DR PIR; B96839; B96839.
DR RefSeq; NP_178183.2; NM_106716.4.
DR AlphaFoldDB; Q8LLD0; -.
DR SMR; Q8LLD0; -.
DR STRING; 3702.AT1G80680.1; -.
DR MEROPS; S59.A01; -.
DR iPTMnet; Q8LLD0; -.
DR PaxDb; Q8LLD0; -.
DR PRIDE; Q8LLD0; -.
DR ProteomicsDB; 249356; -.
DR EnsemblPlants; AT1G80680.1; AT1G80680.1; AT1G80680.
DR GeneID; 844407; -.
DR Gramene; AT1G80680.1; AT1G80680.1; AT1G80680.
DR KEGG; ath:AT1G80680; -.
DR Araport; AT1G80680; -.
DR TAIR; locus:2025737; AT1G80680.
DR eggNOG; KOG0845; Eukaryota.
DR HOGENOM; CLU_012427_0_0_1; -.
DR InParanoid; Q8LLD0; -.
DR OMA; RWKFEVD; -.
DR OrthoDB; 93359at2759; -.
DR PhylomeDB; Q8LLD0; -.
DR PRO; PR:Q8LLD0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LLD0; baseline and differential.
DR Genevisible; Q8LLD0; AT.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0031965; C:nuclear membrane; IDA:TAIR.
DR GO; GO:0005643; C:nuclear pore; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0015288; F:porin activity; ISS:TAIR.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IPI:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0002758; P:innate immune response-activating signal transduction; IMP:TAIR.
DR GO; GO:0048574; P:long-day photoperiodism, flowering; IEP:TAIR.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009733; P:response to auxin; IGI:UniProtKB.
DR Gene3D; 3.30.1610.10; -; 1.
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; PF12110; Nup96; 1.
DR SUPFAM; SSF82215; SSF82215; 1.
DR PROSITE; PS51434; NUP_C; 1.
PE 1: Evidence at protein level;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Plant defense; Protein transport; Reference proteome; Stress response;
KW Translocation; Transport.
FT CHAIN 1..1046
FT /note="Nuclear pore complex protein NUP96"
FT /id="PRO_0000425594"
FT DOMAIN 51..187
FT /note="Peptidase S59"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00765"
FT REGION 283..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT CONFLICT 279
FT /note="S -> A (in Ref. 2; AAN03675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1046 AA; 119154 MW; DCA81819C7A0845E CRC64;
MTSLSIQPFP EISRMARDLD SRKKRRISLD GIAALCEHSK EIIDSLPMLN SPDYFLKPCI
NELVEREIES PDYCSRVPDF TIGRIGYGYI RFLGNTDVRR LDLDHIVKFH RHEVIVYDDE
SSKPVVGEGL NKAAEVTLVV NIPDLTWGKQ QVNHIAYKLK QSTERQGATF ISFDPDNGLW
KFFVPHFSRF GLSDDEAEDI AMDDAPGLGD PVGLDGKKVA DIDEEDQMET SELELSHSLP
AHLGLDPEKM KEMRMLMFPN EDEDESEDFR EQTSHLMTSL TKRNVRPSQK IAQRNSHQDP
PPVVRKTPLA LLEYNPGNDK SSPGSILMVQ QNKNLAVRKS KTGGFELDIS HVTPLTDNYS
RNVVDAALFM GRSFRAGWGP NGVLFHTGKP ICSSSSQMVL SSVINKEKIA IDKVVWDRKG
KVQKELIDSA FEAPLSLHKE LNHVEEEVRF GSFSLKLQNV VTDRVVLSDI CRSYIGIIEK
QLEVAGLSTS AKLFLMHQVM VWELIKVLFS ERQSTERLMY AASDNEEDVM QDVKEDSAKI
DTEALPLIRR AEFSCWLQES VSHRVQEDVS DLNGSSYLEH LFFLLTGREL DSAVELAISK
GDVRLACLLS QAGGSTVNRN DILQQLHLWR RNGLDFNFIE KERIKLYELL AGNIHDALQD
FTIDWKRFLG LLMWHHLPPD SSLPIIFRSY QLLLNQAKAP WPVPIYIDEG PADGFVSDNK
HSDILYYLML LHSKEEEEFG FLQTMFSAFS STDDPLDYHM IWHHRGILEA VGAFTSDDLH
TLDMGFVAQL LSQGLCHWAI YVVLHIPFRE DHPYLHVTVI REILFQYCET WSSMESQRQF
IKDLGIPSEW MHEALAVYYN YHGDFVKALD QFIECANWQR AHSIFMTSVA HSLFLSANHS
EIWRIATSMD DRKSEIENWD LGAGIYMSFY LLKSSLQEDA DTMVELEPLD STNESCRNFV
GRLNESLAVW GDRLPVEARV AYSKMAEEIC DLLLSDLSKN PSRETQLTCF ETAFDAPLPE
DVRSTHLQDA VSLFSLYLSE TGQISA
