IMB1_ARATH
ID IMB1_ARATH Reviewed; 870 AA.
AC Q9FJD4; Q8GZ46;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Importin subunit beta-1 {ECO:0000305};
DE AltName: Full=Karyopherin subunit beta-1;
DE Short=ATKPNB1 {ECO:0000303|PubMed:23582042};
GN Name=KPNB1 {ECO:0000303|PubMed:23582042};
GN OrderedLocusNames=At5g53480 {ECO:0000312|Araport:AT5G53480};
GN ORFNames=MNC6.1 {ECO:0000312|EMBL:BAB09724.1};
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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).
RN [5]
RP FUNCTION, INTERACTION WITH IMPA1; IMPA2; NUP62; RAN1; RAN2 AND RAN3,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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: Acts as negative effector of drought tolerance. Involved in
CC the regulation of stomatal closure and in the abscisic acid (ABA)-
CC mediated pathway that lead to drought tolerance. Does not directly
CC mediate nuclear import of ABI1 and ABI2 which are key regulators of the
CC ABA signaling pathway. May be involved in nuclear translocation of
CC other type 2C protein phosphatases that mediate ABA signaling.
CC {ECO:0000269|PubMed:23582042}.
CC -!- SUBUNIT: Forms a complex with the importin subunits alpha IMPA1 or
CC IMPA2, the nucleoporin NUP62 and the Ran-GTP-binding proteins RAN1,
CC RAN2 or RAN3. {ECO:0000269|PubMed:23582042}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23582042}. Nucleus
CC {ECO:0000269|PubMed:23582042}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves, stems,
CC petals, stamen, stigma, siliques, embryos and guard cells.
CC {ECO:0000269|PubMed:23582042}.
CC -!- DISRUPTION PHENOTYPE: Delayed development and flowering, reduced length
CC of leaves, stems and siliques, increased sensitivity to abscisic acid
CC (ABA) and increased drought tolerance. {ECO:0000269|PubMed:23582042}.
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41893.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB015476; BAB09724.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96362.1; -; Genomic_DNA.
DR EMBL; AK117217; BAC41893.1; ALT_FRAME; mRNA.
DR RefSeq; NP_200160.1; NM_124727.3.
DR AlphaFoldDB; Q9FJD4; -.
DR SMR; Q9FJD4; -.
DR STRING; 3702.AT5G53480.1; -.
DR iPTMnet; Q9FJD4; -.
DR SwissPalm; Q9FJD4; -.
DR PaxDb; Q9FJD4; -.
DR PRIDE; Q9FJD4; -.
DR ProMEX; Q9FJD4; -.
DR ProteomicsDB; 248544; -.
DR EnsemblPlants; AT5G53480.1; AT5G53480.1; AT5G53480.
DR GeneID; 835429; -.
DR Gramene; AT5G53480.1; AT5G53480.1; AT5G53480.
DR KEGG; ath:AT5G53480; -.
DR Araport; AT5G53480; -.
DR TAIR; locus:2168586; AT5G53480.
DR eggNOG; KOG1241; Eukaryota.
DR HOGENOM; CLU_008296_0_0_1; -.
DR InParanoid; Q9FJD4; -.
DR OMA; GRICDII; -.
DR OrthoDB; 769199at2759; -.
DR PhylomeDB; Q9FJD4; -.
DR PRO; PR:Q9FJD4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJD4; baseline and differential.
DR Genevisible; Q9FJD4; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
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:0006606; P:protein import into nucleus; IDA: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 InterPro; IPR027140; KPNB1_plant.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR PANTHER; PTHR10527:SF68; PTHR10527:SF68; 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; Cytoplasm; Nucleus; Protein transport; Reference proteome;
KW Repeat; Stress response; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..870
FT /note="Importin subunit beta-1"
FT /id="PRO_0000431576"
FT REPEAT 4..33
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT DOMAIN 23..103
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 35..67
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 87..126
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 132..161
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 172..204
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 214..249
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 255..304
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 313..361
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 365..395
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 403..440
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 456..492
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 498..535
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 542..588
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 596..637
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 642..679
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 684..722
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 730..776
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 826..868
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 870 AA; 96259 MW; E09C2DFF6980889B CRC64;
MAMEVTQLLI NAQSIDGTVR KHAEESLKQF QEQNLAGFLL SLAGELANDE KPVDSRKLAG
LVLKNALDAK EQHRKYELVQ RWLALDMSTK SQIRAFLLKT LSAPVPDVRS TASQVIAKVA
GIELPQKQWP ELIVSLLSNI HQLPAHVKQA TLETLGYLCE EVSPDVVEQE HVNKILTAVV
QGMNAAEGNT DVRLAATRAL YMALGFAQAN FNNDMERDYI MRVVCEATLS PEVKIRQAAF
ECLVSIASTY YEKLAHYMQD IFNITAKAVR EDDESVALQA IEFWSSICDE EIDILEEYGG
EFAGDSDVPC FYFTKQALPG LVPLLLETLL KQEEDQDLDE GAWNIAMAGG TCLGLVARAV
GDDIVPHVMP FIEEKISKPD WREREAATYA FGSILEGPSA DKLMAIVNAA LTFMLNALTN
DPSNHVKDTT AWTLGRIFEF LHGSTIETPI INQANCQQII TVLIQSMNDA PNVAEKACGA
LYFLAQGYED IGPSSPLTPF FQEIIKSLLA VAHREDATES RLRTAAYEAL NEVVRCSTDE
TSTMVLQLVP VIMMELHNTL EGEKLSLDER EKQNELQGLL CGCLQVIIQK LGSEPTKSKF
MEYADQMMGL FLRVFGCRSA TAHEEAMLAI GALAYAAGPN FAKYMPEFYK YLEMGLQNFE
EYQVCAVTVG VVGDVCRALE DKILPYCDGI MTQLLKDLSS NQLHRSVKPP IFSCFGDIAL
AIGEDFDKYW RYSMPMLQSA AELSAHSAGA DDEMTEYTNS LRNGILEAYS GIFQGFKNSA
KTQLLIPFAP HILQFLDSIY MEKDMDEVVM KTAIGVLGDL ADTLGSHVGG LIQQSVSSKE
FLNECLSSED HTIKEAAEWA KHAITRAISV
