TNPO1_ARATH
ID TNPO1_ARATH Reviewed; 891 AA.
AC Q8H0U4; F4ILE2; Q8H2D6; Q9ZVW8;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Transportin-1;
DE Short=AtTRN1;
DE AltName: Full=Importin beta-2;
DE AltName: Full=Karyopherin beta-2;
GN Name=TRN1; OrderedLocusNames=At2g16950; ORFNames=F12A24.13;
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] (ISOFORM 2), INTERACTION WITH RBG7; RBG8; RAN1
RP AND RNP1, SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=14756317; DOI=10.1023/b:plan.0000009288.46713.1f;
RA Ziemienowicz A., Haasen D., Staiger D., Merkle T.;
RT "Arabidopsis transportin1 is the nuclear import receptor for the circadian
RT clock-regulated RNA-binding protein AtGRP7.";
RL Plant Mol. Biol. 53:201-212(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [5]
RP REVIEW.
RX PubMed=14523572; DOI=10.1007/s00294-003-0444-x;
RA Merkle T.;
RT "Nucleo-cytoplasmic partitioning of proteins in plants: implications for
RT the regulation of environmental and developmental signalling.";
RL Curr. Genet. 44:231-260(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP IDENTIFICATION BY 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 GENE FAMILY.
RX PubMed=21556326; DOI=10.1371/journal.pone.0019308;
RA O'Reilly A.J., Dacks J.B., Field M.C.;
RT "Evolution of the karyopherin-? family of nucleocytoplasmic transport
RT factors; ancient origins and continued specialization.";
RL PLoS ONE 6:E19308-E19308(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals (NLS) in
CC cargo substrates. Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) through
CC binding to nucleoporin and the complex is subsequently translocated
CC through the pore by an energy requiring, Ran-dependent mechanism. At
CC the nucleoplasmic side of the NPC, Ran binds to the importin, the
CC importin/substrate complex dissociates and importin is re-exported from
CC the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The
CC directionality of nuclear import is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran between
CC the cytoplasm and nucleus (By similarity). Involved in nuclear import
CC of M9-containing proteins. In vitro, binds directly to the M9 region of
CC the glycine-rich RNA-binding RBG7 and mediates its nuclear import.
CC {ECO:0000250, ECO:0000269|PubMed:14756317}.
CC -!- SUBUNIT: Interacts with RBG7, RBG8, RAN1 and RNP1.
CC {ECO:0000269|PubMed:14756317}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:14756317}. Note=Shuttles continuously between the
CC nucleus and the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H0U4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H0U4-2; Sequence=VSP_045998;
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC64225.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y18342; CAC80068.1; -; mRNA.
DR EMBL; AC005167; AAC64225.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06561.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06562.1; -; Genomic_DNA.
DR EMBL; BT002041; AAN72052.1; -; mRNA.
DR EMBL; BT008804; AAP68243.1; -; mRNA.
DR PIR; C84546; C84546.
DR RefSeq; NP_001031359.1; NM_001036282.2. [Q8H0U4-1]
DR RefSeq; NP_179287.3; NM_127248.4. [Q8H0U4-2]
DR AlphaFoldDB; Q8H0U4; -.
DR SMR; Q8H0U4; -.
DR BioGRID; 1555; 5.
DR IntAct; Q8H0U4; 6.
DR STRING; 3702.AT2G16950.1; -.
DR iPTMnet; Q8H0U4; -.
DR PaxDb; Q8H0U4; -.
DR PRIDE; Q8H0U4; -.
DR ProMEX; Q8H0U4; -.
DR ProteomicsDB; 232467; -. [Q8H0U4-1]
DR EnsemblPlants; AT2G16950.1; AT2G16950.1; AT2G16950. [Q8H0U4-2]
DR EnsemblPlants; AT2G16950.2; AT2G16950.2; AT2G16950. [Q8H0U4-1]
DR GeneID; 816198; -.
DR Gramene; AT2G16950.1; AT2G16950.1; AT2G16950. [Q8H0U4-2]
DR Gramene; AT2G16950.2; AT2G16950.2; AT2G16950. [Q8H0U4-1]
DR KEGG; ath:AT2G16950; -.
DR Araport; AT2G16950; -.
DR TAIR; locus:2039410; AT2G16950.
DR eggNOG; KOG2023; Eukaryota.
DR HOGENOM; CLU_008136_1_0_1; -.
DR OMA; MFPLLEC; -.
DR OrthoDB; 525700at2759; -.
DR PhylomeDB; Q8H0U4; -.
DR PRO; PR:Q8H0U4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8H0U4; baseline and differential.
DR Genevisible; Q8H0U4; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051170; P:import into nucleus; IDA:TAIR.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0070922; P:RISC complex assembly; IGI:TAIR.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nucleus; Protein transport;
KW Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..891
FT /note="Transportin-1"
FT /id="PRO_0000421800"
FT REPEAT 14..42
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT DOMAIN 37..105
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 47..85
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 94..127
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 133..170
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 180..210
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 223..250
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 262..289
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 305..382
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 390..421
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 433..460
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 478..511
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 519..552
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 560..598
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 606..654
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 665..696
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 704..741
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 749..785
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 793..826
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 835..867
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REGION 326..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 214
FT /note="A -> AVIWQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14756317"
FT /id="VSP_045998"
FT CONFLICT Q8H0U4-2:216..217
FT /note="IW -> R (in Ref. 1; CAC80068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 891 AA; 99109 MW; 91F5A6D6A66692D0 CRC64;
MAATAVVWQP RDDGLAEICS LLEQQISPSS VVDKSQIWKQ LQHFSQFPDF NNYLVFILVR
AEGKSVEVRQ AAGLLLKNNL RGAYPSMTQE NQKYIKSELL PCLGAADRNI RTTVGTIISV
IVNIEGVSGW HELLPALVTC LDSNDLNHMD GAMDALSKIC EDIPHVLDTE VPGLAERPIN
IFLPRLLQFF QSPHASLRKL ALGSVNQYII IMPAALYNSL DKYLQGLFVL ANDPVPEVRK
LVCAAFVHLT EVLPSSIEPH LRNVMEYMLQ VNRDPDEEVS LEACEFWSAY CDAQLPPENL
KEFLPRLIPV LLENMAYADD DESLLDAEED ESQPDRDQDL KPRFHTSRLH GSEDFDDDDD
DSFNVWNLRK CSAAAIDVLS NVFGDEILPA LMPLIQKNLS ASGDEAWKQR EAAVLALGAI
AEGCMNGLYP HLSEIVAFLL PLLDDKFPLI RSISCWTLSR FGKYLIQESG NPKGYEQFEK
VLMGLLRRLL DTNKRVQEAA CSAFATVEED AAEELVPHLG VILQHLMCAF GKYQRRNLRI
VYDAIGTLAD SVREELNKPA YLEILMPPLV AKWQQLSNSD KDLFPLLECF TSISQALGVG
FAPFAQPVFQ RCMDIIQLQQ LAKVNPASAG AQYDREFIVC SLDLLSGLAE GLGSGIESLV
QQSNLRDLLL NCCIDEAADV RQSAFALMGD LARVFPVYLQ PRLLDFLEIA SQQLSANLNR
ENLSVANNAC WAIGELAVKV RQEVSPIVAK VVSSLGLILQ HGEGVNKALV ENSAITLGRL
AWIRPDLVAP HMDHFMKPWC MALSMVRDDI EKEDAFRGLC AVVKVNPSGG VSSLVFICQA
IASWHEIRSE DVQTEVSQVL NGYKHMLGNS WAECLSALDP PVKERLARYQ V
