IMPA3_ARATH
ID IMPA3_ARATH Reviewed; 531 AA.
AC O04294; O04255; O49601; Q4JHM3; Q94F55;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Importin subunit alpha-3 {ECO:0000305};
DE Short=IMPa-3 {ECO:0000303|PubMed:18836040};
DE AltName: Full=Karyopherin subunit alpha-2;
DE Short=KAP-alpha-2;
DE AltName: Full=Protein MODIFIER OF SNC1 6 {ECO:0000303|PubMed:15964279};
GN Name=IMPA3 {ECO:0000303|PubMed:18836040};
GN Synonyms=KAP2, MOS6 {ECO:0000303|PubMed:15964279};
GN OrderedLocusNames=At4g02150 {ECO:0000312|Araport:AT4G02150};
GN ORFNames=T10M13.16;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15964279; DOI=10.1016/j.cub.2005.05.022;
RA Palma K., Zhang Y., Li X.;
RT "An importin alpha homolog, MOS6, plays an important role in plant innate
RT immunity.";
RL Curr. Biol. 15:1129-1135(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Salchert K.D.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
RP INTERACTION WITH PRL1.
RX PubMed=9765207; DOI=10.1101/gad.12.19.3059;
RA Nemeth K., Salchert K., Putnoky P., Bhalerao R., Koncz-Kalman Z.,
RA Stankovic-Stangeland B., Bako L., Mathur J., Oekresz L., Stabel S.,
RA Geigenberger P., Stitt M., Redei G.P., Schell J., Koncz C.;
RT "Pleiotropic control of glucose and hormone responses by PRL1, a nuclear WD
RT protein, in Arabidopsis.";
RL Genes Dev. 12:3059-3073(1998).
RN [8]
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).
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). May be involved in the regulation of pathogen-
CC induced salicylic acid accumulation (PubMed:15964279).
CC {ECO:0000250|UniProtKB:Q96321, ECO:0000269|PubMed:15964279,
CC ECO:0000269|PubMed:18836040}.
CC -!- SUBUNIT: Forms a complex with importin subunit beta-1 (By similarity).
CC Interacts with PRL1 (PubMed:9765207). Interacts with A.tumefaciens
CC VirD2 and VirE2 (PubMed:18836040). {ECO:0000250|UniProtKB:Q96321,
CC ECO:0000269|PubMed:18836040, ECO:0000269|PubMed:9765207}.
CC -!- INTERACTION:
CC O04294; O80837: DBP; NbExp=4; IntAct=EBI-1644689, EBI-1788073;
CC O04294; Q39101: FER1; NbExp=3; IntAct=EBI-1644689, EBI-25513208;
CC O04294; Q9MAA7: GID1A; NbExp=3; IntAct=EBI-1644689, EBI-963597;
CC O04294; P93830: IAA17; NbExp=3; IntAct=EBI-1644689, EBI-632243;
CC O04294; Q38822: IAA3; NbExp=3; IntAct=EBI-1644689, EBI-307174;
CC O04294; O23160: MYB73; NbExp=3; IntAct=EBI-1644689, EBI-25506855;
CC O04294; Q42384: PRL1; NbExp=3; IntAct=EBI-1644689, EBI-1382964;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15964279}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show enhanced disease susceptibility to
CC the virulent pathogen H.arabidopsidis isolate NOCO2.
CC {ECO:0000269|PubMed:15964279}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; Y15225; CAA75514.1; -; mRNA.
DR EMBL; DQ087970; AAY87936.1; -; mRNA.
DR EMBL; Y09511; CAA70703.1; -; mRNA.
DR EMBL; AF001308; AAC78706.1; -; Genomic_DNA.
DR EMBL; AL161493; CAB80708.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82131.1; -; Genomic_DNA.
DR EMBL; AF385693; AAK60286.1; -; mRNA.
DR EMBL; AY081725; AAL87378.1; -; mRNA.
DR PIR; T01516; T01516.
DR PIR; T52099; T52099.
DR RefSeq; NP_192124.1; NM_116447.3.
DR PDB; 4TNM; X-ray; 2.90 A; A=1-531.
DR PDBsum; 4TNM; -.
DR AlphaFoldDB; O04294; -.
DR SMR; O04294; -.
DR BioGRID; 12765; 38.
DR IntAct; O04294; 49.
DR STRING; 3702.AT4G02150.1; -.
DR PaxDb; O04294; -.
DR PRIDE; O04294; -.
DR ProteomicsDB; 248539; -.
DR EnsemblPlants; AT4G02150.1; AT4G02150.1; AT4G02150.
DR GeneID; 827472; -.
DR Gramene; AT4G02150.1; AT4G02150.1; AT4G02150.
DR KEGG; ath:AT4G02150; -.
DR Araport; AT4G02150; -.
DR TAIR; locus:2132238; AT4G02150.
DR eggNOG; KOG0166; Eukaryota.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; O04294; -.
DR OMA; DQTRCVI; -.
DR OrthoDB; 1111872at2759; -.
DR PhylomeDB; O04294; -.
DR PRO; PR:O04294; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O04294; baseline and differential.
DR Genevisible; O04294; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0006952; P:defense response; IMP:TAIR.
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; 4.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..531
FT /note="Importin subunit alpha-3"
FT /id="PRO_0000120738"
FT DOMAIN 1..58
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 111..153
FT /note="ARM 1"
FT REPEAT 154..198
FT /note="ARM 2"
FT REPEAT 199..236
FT /note="ARM 3"
FT REPEAT 237..281
FT /note="ARM 4"
FT REPEAT 282..321
FT /note="ARM 5"
FT REPEAT 322..364
FT /note="ARM 6"
FT REPEAT 365..405
FT /note="ARM 7"
FT REPEAT 406..447
FT /note="ARM 8"
FT REGION 500..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 207
FT /note="P -> L (in Ref. 3; CAA70703)"
FT /evidence="ECO:0000305"
FT CONFLICT 330..331
FT /note="AL -> VQ (in Ref. 1; CAA75514)"
FT /evidence="ECO:0000305"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:4TNM"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 175..191
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:4TNM"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 301..315
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 319..326
FT /evidence="ECO:0007829|PDB:4TNM"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 344..357
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 386..401
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 406..413
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 429..450
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 460..467
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 470..476
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:4TNM"
FT HELIX 483..496
FT /evidence="ECO:0007829|PDB:4TNM"
SQ SEQUENCE 531 AA; 58616 MW; 55B8979D205FCAA3 CRC64;
MSLRPSAKTE VRRNRYKVAV DAEEGRRRRE DNLVEIRKNK REENLQKKRF TSSMAFGSAT
GQTEQDLSSA NQLKDNLPAM VAGIWSEDSN SQLEATNLLR KLLSIEQNPP INEVVQSGVV
PRVVKFLSRD DFPKLQFEAA WALTNIASGT SENTNVIIES GAVPIFIQLL SSASEDVREQ
AVWALGNVAG DSPKCRDLVL SYGAMTPLLS QFNENTKLSM LRNATWTLSN FCRGKPPPAF
EQTQPALPVL ERLVQSMDEE VLTDACWALS YLSDNSNDKI QAVIEAGVVP RLIQLLGHSS
PSVLIPALRT IGNIVTGDDL QTQMVLDQQA LPCLLNLLKN NYKKSIKKEA CWTISNITAG
NADQIQAVID AGIIQSLVWV LQSAEFEVKK EAAWGISNAT SGGTHDQIKF MVSQGCIKPL
CDLLTCPDLK VVTVCLEALE NILVVGEAEK NLGHTGEDNL YAQMIDEAEG LEKIENLQSH
DNNDIYDKAV KILETFWTED NEEEGNDENH APQSGFQFGS TNVPPGQFNF I
