NTF2A_ARATH
ID NTF2A_ARATH Reviewed; 122 AA.
AC Q9FZK4;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Nuclear transport factor 2A {ECO:0000303|PubMed:16428596};
DE Short=AtNTF2a {ECO:0000303|PubMed:16428596};
DE Contains:
DE RecName: Full=Nuclear transport factor 2A, N-terminally processed;
GN Name=NTF2A {ECO:0000303|PubMed:16428596};
GN OrderedLocusNames=At1g27310 {ECO:0000312|Araport:AT1G27310};
GN ORFNames=F17L21.10 {ECO:0000312|EMBL:AAK68829.1};
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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 SUBCELLULAR LOCATION.
RX PubMed=15610358; DOI=10.1111/j.1365-313x.2004.02281.x;
RA Koroleva O.A., Tomlinson M.L., Leader D., Shaw P., Doonan J.H.;
RT "High-throughput protein localization in Arabidopsis using Agrobacterium-
RT mediated transient expression of GFP-ORF fusions.";
RL Plant J. 41:162-174(2005).
RN [5]
RP FUNCTION, MUTAGENESIS OF GLU-38 AND GLU-91, TISSUE SPECIFICITY, INTERACTION
RP WITH RAN1, SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=16428596; DOI=10.1104/pp.105.075499;
RA Zhao Q., Leung S., Corbett A.H., Meier I.;
RT "Identification and characterization of the Arabidopsis orthologs of
RT nuclear transport factor 2, the nuclear import factor of ran.";
RL Plant Physiol. 140:869-878(2006).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Facilitates protein transport into the nucleus. Interacts
CC with various nucleoporins and with Ran-GDP. Could be part of a
CC multicomponent system of cytosolic factors that assemble at the pore
CC complex during nuclear import. {ECO:0000269|PubMed:16428596}.
CC -!- SUBUNIT: Interacts with RAN1. {ECO:0000269|PubMed:16428596}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15610358,
CC ECO:0000269|PubMed:16428596}. Nucleus {ECO:0000269|PubMed:15610358,
CC ECO:0000269|PubMed:16428596}. Nucleus envelope
CC {ECO:0000269|PubMed:16428596}. Note=Accumulates at the nuclear rim.
CC Excluded from the nucleolus. {ECO:0000269|PubMed:16428596}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers, and,
CC at low levels, in siliques. {ECO:0000269|PubMed:16428596}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004557; AAF99749.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30805.1; -; Genomic_DNA.
DR EMBL; AY042889; AAK68829.1; -; mRNA.
DR EMBL; AY072473; AAL66888.1; -; mRNA.
DR PIR; H86398; H86398.
DR RefSeq; NP_174051.1; NM_102493.3.
DR AlphaFoldDB; Q9FZK4; -.
DR SMR; Q9FZK4; -.
DR STRING; 3702.AT1G27310.1; -.
DR iPTMnet; Q9FZK4; -.
DR PaxDb; Q9FZK4; -.
DR PRIDE; Q9FZK4; -.
DR ProteomicsDB; 248937; -.
DR EnsemblPlants; AT1G27310.1; AT1G27310.1; AT1G27310.
DR GeneID; 839620; -.
DR Gramene; AT1G27310.1; AT1G27310.1; AT1G27310.
DR KEGG; ath:AT1G27310; -.
DR Araport; AT1G27310; -.
DR TAIR; locus:2015914; AT1G27310.
DR eggNOG; KOG2104; Eukaryota.
DR HOGENOM; CLU_131642_0_0_1; -.
DR InParanoid; Q9FZK4; -.
DR OMA; LAICTFP; -.
DR OrthoDB; 1437819at2759; -.
DR PhylomeDB; Q9FZK4; -.
DR PRO; PR:Q9FZK4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZK4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:TAIR.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR CDD; cd00780; NTF2; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR045875; NTF2/Mtr2.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR PANTHER; PTHR12612; PTHR12612; 1.
DR Pfam; PF02136; NTF2; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..122
FT /note="Nuclear transport factor 2A"
FT /id="PRO_0000441932"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..122
FT /note="Nuclear transport factor 2A, N-terminally processed"
FT /id="PRO_0000443352"
FT DOMAIN 6..119
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 38
FT /note="E->K: Loss of interaction with RAN1 leading to
FT impaired nuclear protein import activity."
FT /evidence="ECO:0000269|PubMed:16428596"
FT MUTAGEN 91
FT /note="E->K: Loss of interaction with RAN1 leading to
FT impaired nuclear protein import activity."
FT /evidence="ECO:0000269|PubMed:16428596"
SQ SEQUENCE 122 AA; 13527 MW; E7CDD9486631A1D2 CRC64;
MDPDAVAKAF VEHYYSTFDA NRPGLVSLYQ EGSMLTFEGQ KIQGSQNIVA KLTGLPFQQC
KHNITTVDCQ PSGPAGGMLV FVSGNLQLAG EQHALKFSQM FHLISNQGNY YVFNDIFRLN
YA
