IMPA1_ARATH
ID IMPA1_ARATH Reviewed; 532 AA.
AC Q96321; O49599; O81520; Q940R6; Q9C841; Q9ZRI5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Importin subunit alpha-1 {ECO:0000305};
DE Short=IMPa-1 {ECO:0000303|PubMed:18836040};
DE AltName: Full=Karyopherin subunit alpha-1;
DE Short=KAP-alpha-1;
GN Name=IMPA1 {ECO:0000303|PubMed:18836040}; Synonyms=KAP1;
GN OrderedLocusNames=At3g06720 {ECO:0000312|Araport:AT3G06720};
GN ORFNames=F3E22.14, T8E24.1;
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], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RA Smith H.M., Raikhel N.V.;
RT "A cDNA encoding an importin alpha homologue from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR96-104(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8776900; DOI=10.2307/3870305;
RA Hicks G.R., Smith H.M., Lobreaux S., Raikhel N.V.;
RT "Nuclear import in permeabilized protoplasts from higher plants has unique
RT features.";
RL Plant Cell 8:1337-1352(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9193081; DOI=10.1104/pp.114.2.411;
RA Smith H.M., Hicks G.R., Raikhel N.V.;
RT "Importin alpha from Arabidopsis thaliana is a nuclear import receptor that
RT recognizes three classes of import signals.";
RL Plant Physiol. 114:411-417(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ballas N., Citovsky V.;
RT "AtKAPalpha gene from Arabidopsis encodes a protein that mediates nuclear
RT import of Agrobacterium VirD2 protein.";
RL (er) Plant Gene Register PGR97-129(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9380702; DOI=10.1073/pnas.94.20.10723;
RA Ballas N., Citovsky V.;
RT "Nuclear localization signal binding protein from Arabidopsis mediates
RT nuclear import of Agrobacterium VirD2 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:10723-10728(1997).
RN [6]
RP SEQUENCE REVISION.
RA Ballas N., Citovsky V.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Raikhel N.V., Smith H.M.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Schledz M., Leclerc D., Neuhaus G., Merkle T.;
RT "Characterization of four cDNAs encoding different importin alpha
RT homologues from Arabidopsis thaliana, designated AtIMPa1-4.";
RL (er) Plant Gene Register PGR98-022(1998).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [10]
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 [11]
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 [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [13]
RP FUNCTION, AND INTERACTION WITH IMPORTIN SUBUNIT BETA-1 KPNB1.
RX PubMed=10428841; DOI=10.1074/jbc.274.32.22610;
RA Hubner S., Smith H.M., Hu W., Chan C.K., Rihs H.P., Paschal B.M.,
RA Raikhel N.V., Jans D.A.;
RT "Plant importin alpha binds nuclear localization sequences with high
RT affinity and can mediate nuclear import independent of importin beta.";
RL J. Biol. Chem. 274:22610-22617(1999).
RN [14]
RP FUNCTION, AND INTERACTION WITH VIP1.
RX PubMed=12124400; DOI=10.1073/pnas.162304099;
RA Tzfira T., Vaidya M., Citovsky V.;
RT "Increasing plant susceptibility to Agrobacterium infection by
RT overexpression of the Arabidopsis nuclear protein VIP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10435-10440(2002).
RN [15]
RP FUNCTION, INTERACTION WITH AGROBACTERIUM VIRD2 AND VIRE2, AND GENE FAMILY.
RX PubMed=18836040; DOI=10.1105/tpc.108.060467;
RA Bhattacharjee S., Lee L.Y., Oltmanns H., Cao H., Gupta V., Cuperus J.,
RA Gelvin S.B.;
RT "IMPa-4, an Arabidopsis importin alpha isoform, is preferentially involved
RT in agrobacterium-mediated plant transformation.";
RL Plant Cell 20:2661-2680(2008).
RN [16]
RP INTERACTION WITH KPNB1.
RX PubMed=23582042; DOI=10.1111/tpj.12207;
RA Luo Y., Wang Z., Ji H., Fang H., Wang S., Tian L., Li X.;
RT "An Arabidopsis homolog of importin beta1 is required for ABA response and
RT drought tolerance.";
RL Plant J. 75:377-389(2013).
CC -!- FUNCTION: Binds to conventional NLS motifs with high affinity in the
CC absence of an importin beta subunit. Mediates nuclear protein import
CC across the nuclear envelope in vitro in the absence of exogenously
CC added importin beta subunit (PubMed:10428841). Acts as cellular
CC receptor for the nuclear import of the virD2 protein of Agrobacterium,
CC but is not essential for Agrobacterium-mediated root transformation
CC (PubMed:18836040). {ECO:0000269|PubMed:10428841,
CC ECO:0000269|PubMed:18836040}.
CC -!- SUBUNIT: Forms a complex with the importin subunit beta-1 KPNB1
CC (PubMed:10428841, PubMed:23582042). Interacts with VIP1 and promotes
CC its nuclear import (PubMed:12124400). Interacts with A.tumefaciens
CC VirD2 and VirE2 (PubMed:18836040). {ECO:0000269|PubMed:10428841,
CC ECO:0000269|PubMed:12124400, ECO:0000269|PubMed:18836040,
CC ECO:0000269|PubMed:23582042}.
CC -!- INTERACTION:
CC Q96321; F8RP38; Xeno; NbExp=3; IntAct=EBI-2131458, EBI-6368424;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:8776900}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD09923.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L81172; AAD09923.1; ALT_FRAME; mRNA.
DR EMBL; AF077528; AAC27644.1; -; mRNA.
DR EMBL; U69533; AAB72116.2; -; mRNA.
DR EMBL; Y15224; CAA75513.1; -; mRNA.
DR EMBL; AC023912; AAF63826.1; -; Genomic_DNA.
DR EMBL; AC036106; AAG50999.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74447.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74448.1; -; Genomic_DNA.
DR EMBL; AY094390; AAM19769.1; -; mRNA.
DR EMBL; AY054164; AAL06825.1; -; mRNA.
DR EMBL; AY088732; AAM67050.1; -; mRNA.
DR EMBL; AY125529; AAM78039.1; -; mRNA.
DR PIR; T52102; T52102.
DR PIR; T52268; T52268.
DR RefSeq; NP_187328.1; NM_111552.3.
DR RefSeq; NP_850524.1; NM_180193.3.
DR AlphaFoldDB; Q96321; -.
DR SMR; Q96321; -.
DR BioGRID; 5192; 70.
DR IntAct; Q96321; 49.
DR STRING; 3702.AT3G06720.1; -.
DR iPTMnet; Q96321; -.
DR MetOSite; Q96321; -.
DR PaxDb; Q96321; -.
DR PRIDE; Q96321; -.
DR ProteomicsDB; 247012; -.
DR EnsemblPlants; AT3G06720.1; AT3G06720.1; AT3G06720.
DR EnsemblPlants; AT3G06720.2; AT3G06720.2; AT3G06720.
DR GeneID; 819857; -.
DR Gramene; AT3G06720.1; AT3G06720.1; AT3G06720.
DR Gramene; AT3G06720.2; AT3G06720.2; AT3G06720.
DR KEGG; ath:AT3G06720; -.
DR Araport; AT3G06720; -.
DR TAIR; locus:2083313; AT3G06720.
DR eggNOG; KOG0166; Eukaryota.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; Q96321; -.
DR OMA; ANIAYFK; -.
DR OrthoDB; 1111872at2759; -.
DR PhylomeDB; Q96321; -.
DR PRO; PR:Q96321; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q96321; baseline and differential.
DR Genevisible; Q96321; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA: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:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR Gene3D; 1.20.5.690; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032413; Arm_3.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR036975; Importin-a_IBB_sf.
DR InterPro; IPR024931; Importin_alpha.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF16186; Arm_3; 1.
DR Pfam; PF01749; IBB; 1.
DR PIRSF; PIRSF005673; Importin_alpha; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 4.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Nucleus; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..532
FT /note="Importin subunit alpha-1"
FT /id="PRO_0000120737"
FT DOMAIN 1..58
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 108..150
FT /note="ARM 1"
FT REPEAT 151..195
FT /note="ARM 2"
FT REPEAT 196..233
FT /note="ARM 3"
FT REPEAT 234..278
FT /note="ARM 4"
FT REPEAT 279..318
FT /note="ARM 5"
FT REPEAT 319..361
FT /note="ARM 6"
FT REPEAT 362..402
FT /note="ARM 7"
FT REPEAT 403..444
FT /note="ARM 8"
FT REGION 497..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 150
FT /note="H -> Y (in Ref. 8; CAA75513)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="L -> F (in Ref. 11; AAL06825)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="G -> P (in Ref. 6; AAB72116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 58645 MW; 9425EACB98D585C7 CRC64;
MSLRPNAKTE VRRNRYKVAV DAEEGRRRRE DNMVEIRKSK REESLMKKRR EGMQALQGFP
SASAASVDKK LDSLKDMVAG VWSDDPALQL ESTTQFRKLL SIERSPPIEE VISAGVVPRF
VEFLKKEDYP AIQFEAAWAL TNIASGTSDH TKVVIDHNAV PIFVQLLASP SDDVREQAVW
ALGNVAGDSP RCRDLVLGCG ALLPLLNQLN EHAKLSMLRN ATWTLSNFCR GKPQPHFDQV
KPALPALERL IHSDDEEVLT DACWALSYLS DGTNDKIQTV IQAGVVPKLV ELLLHHSPSV
LIPALRTVGN IVTGDDIQTQ CVINSGALPC LANLLTQNHK KSIKKEACWT ISNITAGNKD
QIQTVVEANL ISPLVSLLQN AEFDIKKEAA WAISNATSGG SHDQIKYLVE QGCIKPLCDL
LVCPDPRIIT VCLEGLENIL KVGEAEKNLG HTGDMNYYAQ LIDDAEGLEK IENLQSHDNN
EIYEKAVKIL ETYWLEEEDD ETQQPPGVDG SQAGFQFGGN QAPVPSGGFN FS
