IMPA2_ARATH
ID IMPA2_ARATH Reviewed; 535 AA.
AC F4JL11; O49600; Q9ASV4;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Importin subunit alpha-2 {ECO:0000305};
DE Short=IMPa-2 {ECO:0000303|PubMed:18836040};
GN Name=IMPA2 {ECO:0000303|PubMed:18836040};
GN OrderedLocusNames=At4g16143 {ECO:0000312|Araport:AT4G16143};
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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].
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 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 [6]
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 and mediates nuclear protein
CC import across the nuclear envelope (By similarity). 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:0000250|UniProtKB:Q96321,
CC ECO:0000269|PubMed:18836040}.
CC -!- SUBUNIT: Forms a complex with the importin subunit beta-1 KPNB1
CC (PubMed:23582042). Interacts with A.tumefaciens VirD2 and VirE2
CC (PubMed:18836040). {ECO:0000269|PubMed:18836040,
CC ECO:0000269|PubMed:23582042}.
CC -!- INTERACTION:
CC F4JL11; Q8L9K1: ERF13; NbExp=3; IntAct=EBI-1253508, EBI-15204728;
CC F4JL11; Q39101: FER1; NbExp=3; IntAct=EBI-1253508, EBI-25513208;
CC F4JL11; Q9LRH6: GATA25; NbExp=3; IntAct=EBI-1253508, EBI-2460434;
CC F4JL11; P93830: IAA17; NbExp=3; IntAct=EBI-1253508, EBI-632243;
CC F4JL11; O23160: MYB73; NbExp=3; IntAct=EBI-1253508, EBI-25506855;
CC F4JL11; Q8GY55: TIFY4B; NbExp=3; IntAct=EBI-1253508, EBI-15206004;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; Y14615; CAA74965.1; -; mRNA.
DR EMBL; AL161543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE83699.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83700.1; -; Genomic_DNA.
DR EMBL; AF361811; AAK32824.1; -; mRNA.
DR EMBL; AY060529; AAL31160.1; -; mRNA.
DR PIR; T52098; T52098.
DR RefSeq; NP_001154239.1; NM_001160767.2.
DR RefSeq; NP_567485.4; NM_117708.6.
DR AlphaFoldDB; F4JL11; -.
DR SMR; F4JL11; -.
DR IntAct; F4JL11; 63.
DR STRING; 3702.AT4G16143.2; -.
DR iPTMnet; F4JL11; -.
DR PaxDb; F4JL11; -.
DR PRIDE; F4JL11; -.
DR ProteomicsDB; 248538; -.
DR EnsemblPlants; AT4G16143.1; AT4G16143.1; AT4G16143.
DR EnsemblPlants; AT4G16143.2; AT4G16143.2; AT4G16143.
DR GeneID; 827302; -.
DR Gramene; AT4G16143.1; AT4G16143.1; AT4G16143.
DR Gramene; AT4G16143.2; AT4G16143.2; AT4G16143.
DR KEGG; ath:AT4G16143; -.
DR Araport; AT4G16143; -.
DR TAIR; locus:505006475; AT4G16143.
DR eggNOG; KOG0166; Eukaryota.
DR HOGENOM; CLU_018084_5_0_1; -.
DR InParanoid; F4JL11; -.
DR OMA; SHDNHEI; -.
DR OrthoDB; 1111872at2759; -.
DR PRO; PR:F4JL11; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JL11; baseline and differential.
DR Genevisible; F4JL11; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; 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 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; 5.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Nucleus; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..535
FT /note="Importin subunit alpha-2"
FT /id="PRO_0000431569"
FT DOMAIN 1..58
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 110..150
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 153..192
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 195..235
FT /note="ARM 3"
FT /evidence="ECO:0000255"
FT REPEAT 237..276
FT /note="ARM 4"
FT /evidence="ECO:0000255"
FT REPEAT 279..318
FT /note="ARM 5"
FT /evidence="ECO:0000255"
FT REPEAT 321..361
FT /note="ARM 6"
FT /evidence="ECO:0000255"
FT REPEAT 364..403
FT /note="ARM 7"
FT /evidence="ECO:0000255"
FT REPEAT 407..446
FT /note="ARM 8"
FT /evidence="ECO:0000255"
FT REGION 20..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 65
FT /note="P -> S (in Ref. 1; CAA74965 and 4; AAK32824/
FT AAL31160)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="I -> V (in Ref. 1; CAA74965)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="I -> N (in Ref. 1; CAA74965)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..338
FT /note="SHGALLSLLS -> KSCAPPSLLG (in Ref. 1; CAA74965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 58907 MW; 113E9D397868E7F2 CRC64;
MSLRPNAKTE VRRNRYKVAV DAEEGRRRRE DNMVEIRKSK REESLQKKRR EGLQANQLPQ
FAPSPVPASS TVEKKLESLP AMVGGVWSDD RSLQLEATTQ FRKLLSIERS PPIEEVIDAG
VVPRFVEFLT REDYPQLQFE AAWALTNIAS GTSENTKVVI EHGAVPIFVQ LLASQSDDVR
EQAVWALGNV AGDSPRCRDL VLGQGALIPL LSQLNEHAKL SMLRNATWTL SNFCRGKPQP
PFDQVRPALP ALERLIHSTD EEVLTDACWA LSYLSDGTND KIQSVIEAGV VPRLVELLQH
QSPSVLIPAL RSIGNIVTGD DLQTQCVISH GALLSLLSLL THNHKKSIKK EACWTISNIT
AGNRDQIQAV CEAGLICPLV NLLQNAEFDI KKEAAWAISN ATSGGSPDQI KYMVEQGVVK
PLCDLLVCPD PRIITVCLEG LENILKVGEA EKVTGNTGDV NFYAQLIDDA EGLEKIENLQ
SHDNSEIYEK AVKILETYWL EEEDETLPPG DPSAQGFQFG GGNDAAVPPG GFNFQ
