NU160_ARATH
ID NU160_ARATH Reviewed; 1495 AA.
AC Q9C811; F4HR72; F4HR73;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Nuclear pore complex protein NUP160 {ECO:0000303|PubMed:21189294};
DE Short=AtNUP160;
DE AltName: Full=Nucleoporin 160;
DE AltName: Full=Protein SUPPRESSOR OF AUXIN RESISTANCE 1 {ECO:0000303|PubMed:16751346};
GN Name=NUP160 {ECO:0000303|PubMed:21189294};
GN Synonyms=SAR1 {ECO:0000303|PubMed:16751346}; OrderedLocusNames=At1g33410;
GN ORFNames=F10C21.8;
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 [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 [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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17030626; DOI=10.1128/mcb.01063-06;
RA Dong C.H., Hu X., Tang W., Zheng X., Kim Y.S., Lee B.H., Zhu J.K.;
RT "A putative Arabidopsis nucleoporin, AtNUP160, is critical for RNA export
RT and required for plant tolerance to cold stress.";
RL Mol. Cell. Biol. 26:9533-9543(2006).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION 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 [5]
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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20872268; DOI=10.1007/s00425-010-1278-7;
RA Muthuswamy S., Meier I.;
RT "Genetic and environmental changes in SUMO homeostasis lead to nuclear mRNA
RT retention in plants.";
RL Planta 233:201-208(2011).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22238449; DOI=10.1093/jxb/err424;
RA Robles L.M., Deslauriers S.D., Alvarez A.A., Larsen P.B.;
RT "A loss-of-function mutation in the nucleoporin AtNUP160 indicates that
RT normal auxin signalling is required for a proper ethylene response in
RT Arabidopsis.";
RL J. Exp. Bot. 63:2231-2241(2012).
RN [8]
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).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22902705; DOI=10.4161/psb.21426;
RA Roth C., Wiermer M.;
RT "Nucleoporins Nup160 and Seh1 are required for disease resistance in
RT Arabidopsis.";
RL Plant Signal. Behav. 7:1212-1214(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. Required for
CC proper expression of factors associated with auxin signaling.
CC {ECO:0000269|PubMed:16751346, ECO:0000269|PubMed:17030626,
CC ECO:0000269|PubMed:20872268, ECO:0000269|PubMed:22238449,
CC ECO:0000269|PubMed:22288649, ECO:0000269|PubMed:22902705}.
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:17030626,
CC ECO:0000269|PubMed:21189294, ECO:0000269|PubMed:22902705}; Peripheral
CC membrane protein {ECO:0000269|PubMed:17030626}; Nucleoplasmic side
CC {ECO:0000269|PubMed:17030626}. Nucleus, nuclear pore complex
CC {ECO:0000305|PubMed:17030626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C811-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C811-2; Sequence=VSP_057129;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, anthers, siliques and
CC vascular tissues of cotyledons, leaves and hypocotyls.
CC {ECO:0000269|PubMed:16751346, ECO:0000269|PubMed:17030626}.
CC -!- DISRUPTION PHENOTYPE: Pleiotropic phenotype with diverse growth defects
CC and early flowering. Enhanced ethylene response and sensitivity to cold
CC stress. Reduced EDS1 expression and enhanced susceptibility to virulent
CC Pseudomonas bacteria and oomycete pathogens. Accumulation of nuclear
CC poly(A)+ RNA and high-molecular weight SUMO conjugates.
CC {ECO:0000269|PubMed:16751346, ECO:0000269|PubMed:17030626,
CC ECO:0000269|PubMed:20872268, ECO:0000269|PubMed:22238449,
CC ECO:0000269|PubMed:22288649}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51224.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC051630; AAG51224.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31591.1; -; Genomic_DNA.
DR PIR; G86457; G86457.
DR RefSeq; NP_001185129.1; NM_001198200.2. [Q9C811-2]
DR AlphaFoldDB; Q9C811; -.
DR BioGRID; 25468; 13.
DR STRING; 3702.AT1G33410.1; -.
DR iPTMnet; Q9C811; -.
DR PaxDb; Q9C811; -.
DR PRIDE; Q9C811; -.
DR ProteomicsDB; 248978; -. [Q9C811-1]
DR EnsemblPlants; AT1G33410.2; AT1G33410.2; AT1G33410. [Q9C811-2]
DR GeneID; 840234; -.
DR Gramene; AT1G33410.2; AT1G33410.2; AT1G33410. [Q9C811-2]
DR KEGG; ath:AT1G33410; -.
DR Araport; AT1G33410; -.
DR TAIR; locus:2007023; AT1G33410.
DR eggNOG; KOG4521; Eukaryota.
DR OMA; TAYHWKK; -.
DR PRO; PR:Q9C811; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C811; baseline and differential.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:TAIR.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0032502; P:developmental process; IMP:TAIR.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IGI:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR InterPro; IPR021717; Nucleoporin_Nup160.
DR InterPro; IPR035192; NUP160.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR21286; PTHR21286; 1.
DR Pfam; PF17238; DUF5311; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Plant defense; Protein transport; Reference proteome;
KW Stress response; Translocation; Transport.
FT CHAIN 1..1495
FT /note="Nuclear pore complex protein NUP160"
FT /id="PRO_0000425595"
FT VAR_SEQ 221
FT /note="L -> LWGFVRLQCR (in isoform 2)"
FT /id="VSP_057129"
SQ SEQUENCE 1495 AA; 168278 MW; 5E0EC7E5478325BF CRC64;
MEENRRNPSA GMEVPVAGGG NVVKWIEISV PSPSVSSSSI GANSSEDNEC VQLPLSEDYA
SSSVIGEPSI SFVWRINKTS PNALELLQLS AKSGFPITGL RFVFAQTLSP FAFVYADEGG
DSGRLVYFLY SLTPSGVVYV LKLSNTLAYK SGSVFPLDHL IHLDVRPYLN ESRVTSVAAS
PGFIFLGRSD GCVSCFQPIV YFQKSSGFHQ ELRDDTGFGR LGTVVAAVQD LFISEVHGRN
YLCVLHADGA LRVWDILTYS RVLCQSIAAK NLEGVMCVRL WLGKADYDSG IIPLAVLYRK
SMNDSMDVIT VYGLHFSSAE GIALSLDSGL QNIPLEEGEL RDVRFTSDKI WTLKANELTS
YMLCQKSSTM EAQSYTLQED YISEQLFLSS RSSSHDLLLT THSLFSSAKD QIMGFISSIF
LRRLLCPGIF HNVALRLTLL DHNKNWTDSE FQSLSLDELT SEILLLVEHE VTAETSISVF
HWWKNFCTSY LHHWCSNNEP RTLLVQSDVI GLVRNNSVSL FFRLENAEHS LGGSSSEHSN
LTSLDLGVSH SDHEILAEVL RCTSKISKQW GGAPYAMYYE SITGRPIISS DEIVPRLVNI
LESGYSTTIG QRTWSDLGAD RAWEKELEAH KNLRTFSIDM LLSLSALCQR AGSWEKVFTI
MEHYLQYLVP KKSMQKNDGE ALSDICSSIL VQATSQFVKV MFESAFDIFL LISYLLNIAG
QVNMSQQDIC KLRLELLPMI QDIVSEWLII LFFVTTPAES TSMEDFSLKL SSLQIDSSID
KRSWNAMLGK CGFSLAFILL FSDRSCIVDG RFNLRYLPSS QIITSLVQNF ISWIRYSKTG
DDSSSLLRRS TELSLRLIRN GQSDAVERIL VVVEASLRGE KTFGCSQDTS GDWCLLQHLR
GCCLLDQVQR GASGILRERK IIDAIRCFFR ASSGEGSWKA LHSLSKEAGF SPATTGPSIL
DGSTSSAAWK LHYYEWAMQI FERYNISEGA CQFAYAALEQ VDDAYNFIEM TEEFDPTKAA
TYTRGRLWAN VFKFTLDLNL LNDAYCAIIS NPDEEIKRIC LRRFIIVLFE CGKTKILSDG
HLPFIGLTEK ITQELFWKAG RSDIMMKPNP YKLLYAYEMR RHNWRMAASY MYQFSARLRS
EGACKDYKHM SLVLQERLNG LSAAMNALAL VHPGYAWIDP VPEETTRYPV KKARRAEEEQ
LRSNDQPKGE KSCIDIEKLQ NEFVFTTAEY MLSLKNFGWT YSGLEKPPSD LVDLLVQANL
YDMAFTVVLK FWRGSALKRE LEKIFENMAI KCCPAKGTLW SSPNLMLTSN DEEVTHSPDR
SPADQGSKLA GDWEILEVYL KRYIDIHARL PVSVASTLLQ ADSCIELPLW LIQMFKDGQK
EKALGMAGQE ASPASLFQLY VDYGRLTEAT NLLLEYMESF ASSKPAEVLK RKKVSGVWFP
YTTVERLWWE LEKTMNSGRM VEQCHKLKEQ LHHALLNHLK LLKVDSNDAV SSATG
