NTF2_ARATH
ID NTF2_ARATH Reviewed; 460 AA.
AC Q9FME2; F4K1Y4; Q8LEI7;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Nuclear transport factor 2 {ECO:0000303|PubMed:28229965};
DE Short=AtNTF2 {ECO:0000303|PubMed:28229965};
GN Name=NTF2 {ECO:0000303|PubMed:28229965};
GN OrderedLocusNames=At5g60980 {ECO:0000312|Araport:AT5G60980};
GN ORFNames=MSL3.12 {ECO:0000312|EMBL:AED97407.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP REGULATION BY MAV8.
RX PubMed=17189346; DOI=10.1105/tpc.106.044420;
RA Arteaga-Vazquez M., Caballero-Perez J., Vielle-Calzada J.-P.;
RT "A family of microRNAs present in plants and animals.";
RL Plant Cell 18:3355-3369(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MBD6, AND SUBCELLULAR
RP LOCATION.
RX PubMed=28229965; DOI=10.1007/s12038-016-9658-1;
RA Parida A.P., Sharma A., Sharma A.K.;
RT "AtMBD6, a methyl CpG binding domain protein, maintains gene silencing in
RT Arabidopsis by interacting with RNA binding proteins.";
RL J. Biosci. 42:57-68(2017).
CC -!- FUNCTION: Involved in RNA-directed DNA methylation (RdDM).
CC {ECO:0000269|PubMed:28229965}.
CC -!- SUBUNIT: Interacts with MBD6. {ECO:0000269|PubMed:28229965}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28229965}. Nucleus
CC {ECO:0000269|PubMed:28229965}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FME2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FME2-2; Sequence=VSP_060196;
CC -!- INDUCTION: Probably regulated by the microRNA MAV8.
CC {ECO:0000269|PubMed:17189346}.
CC -!- DISRUPTION PHENOTYPE: Reduced DNA methylation in some of the targets of
CC RNA-directed DNA methylation (RdDM). {ECO:0000269|PubMed:28229965}.
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DR EMBL; AB008269; BAB10647.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97406.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97407.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69708.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69709.1; -; Genomic_DNA.
DR EMBL; AY062108; AAL32982.1; -; mRNA.
DR EMBL; BT003010; AAO23575.1; -; mRNA.
DR EMBL; AY085400; AAM62628.1; -; mRNA.
DR RefSeq; NP_001331368.1; NM_001345438.1. [Q9FME2-1]
DR RefSeq; NP_001331369.1; NM_001345439.1. [Q9FME2-2]
DR RefSeq; NP_200906.2; NM_125491.3. [Q9FME2-1]
DR RefSeq; NP_851235.1; NM_180904.2. [Q9FME2-2]
DR AlphaFoldDB; Q9FME2; -.
DR SMR; Q9FME2; -.
DR IntAct; Q9FME2; 1.
DR STRING; 3702.AT5G60980.2; -.
DR PaxDb; Q9FME2; -.
DR PRIDE; Q9FME2; -.
DR ProteomicsDB; 185183; -.
DR ProteomicsDB; 189446; -. [Q9FME2-1]
DR EnsemblPlants; AT5G60980.1; AT5G60980.1; AT5G60980. [Q9FME2-2]
DR EnsemblPlants; AT5G60980.2; AT5G60980.2; AT5G60980. [Q9FME2-1]
DR EnsemblPlants; AT5G60980.3; AT5G60980.3; AT5G60980. [Q9FME2-1]
DR EnsemblPlants; AT5G60980.4; AT5G60980.4; AT5G60980. [Q9FME2-2]
DR GeneID; 836219; -.
DR Gramene; AT5G60980.1; AT5G60980.1; AT5G60980. [Q9FME2-2]
DR Gramene; AT5G60980.2; AT5G60980.2; AT5G60980. [Q9FME2-1]
DR Gramene; AT5G60980.3; AT5G60980.3; AT5G60980. [Q9FME2-1]
DR Gramene; AT5G60980.4; AT5G60980.4; AT5G60980. [Q9FME2-2]
DR KEGG; ath:AT5G60980; -.
DR Araport; AT5G60980; -.
DR TAIR; locus:2173567; AT5G60980.
DR eggNOG; KOG0116; Eukaryota.
DR HOGENOM; CLU_026954_3_0_1; -.
DR InParanoid; Q9FME2; -.
DR OMA; LKYEEYT; -.
DR OrthoDB; 1526879at2759; -.
DR PhylomeDB; Q9FME2; -.
DR PRO; PR:Q9FME2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FME2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR CDD; cd00780; NTF2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR039539; Ras_GTPase_bind_prot.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10693; PTHR10693; 1.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..460
FT /note="Nuclear transport factor 2"
FT /id="PRO_0000447464"
FT DOMAIN 15..131
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 293..370
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 207..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 331
FT /note="Missing (in isoform 2)"
FT /id="VSP_060196"
FT CONFLICT 94
FT /note="L -> P (in Ref. 4; AAM62628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 49543 MW; DA7D826834DB0580 CRC64;
MAQQEASPSP GAEVVGRAFV EQYYHILHQS PGLVHRFYQD SSFLTRPDVT GAVTTVTTMQ
AINDKILSLK YEDYTAEIET ADAQESHERG VIVLVTGRLT GNDNVRKKFS QSFFLAPQDK
GYFVLNDVFR FLEEKEVTAQ ARSVPINGTT RDVQAPIEPE RVVVSHEPEV EPEPVASIEE
EDLDNVAEVY DPSDKDEGVV VDVEPIEPPT QISHNEILSV PQGDAPKHSY ASILKQMKSS
PAPTTHVARN KPRPAPVNQK LTAPPAEPAA RPEASAHENV PNSSHVDVED DGHSIYVRNL
PFDSTPTQLE EVFKNFGAIK HEGIQVRSNK QQGFCFGFVE FETSSGKQSA LEASPVTIGD
RQAVVEEKKT NSRGGGNNGG SRGRYFSGRG SFRNESFKGG RGGGGRGGYG RGGGEFSGRP
KSSNPRNGGE GYQRVPQNGG GGRGGRGEGG RGGARGGGSS
