ID IMA1A_ORYSJ Reviewed; 526 AA. AC Q71VM4; O82783; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 2. DT 02-SEP-2026, entry version 122. DE RecName: Full=Importin subunit alpha-1a; GN OrderedLocusNames=Os01g0253300, LOC_Os01g14950; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND RP INDUCTION. RC STRAIN=cv. Nipponbare; TISSUE=Callus, and Leaf; RX PubMed=9678973; DOI=10.1016/s0378-1119(98)00175-9; RA Shoji K., Iwasaki T., Matsuki R., Miyao M., Yamamoto N.; RT "Cloning of a cDNA encoding an importin-alpha and down-regulation of the RT gene by light in rice leaves."; RL Gene 212:279-286(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Fischer R.; RT "Importin alpha-3, a novel variant of the small importin subunit RT evolutionarily conserved from hydrozoa to man."; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12447438; DOI=10.1038/nature01184; RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M., RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M., RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T., RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S., RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H., RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y., RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S., RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y., RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S., RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.; RT "The genome sequence and structure of rice chromosome 1."; RL Nature 420:312-316(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [5] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=9727027; DOI=10.1074/jbc.273.37.24083; RA Jiang C.-J., Imamoto N., Matsuki R., Yoneda Y., Yamamoto N.; RT "Functional characterization of a plant importin alpha homologue. Nuclear RT localization signal (NLS)-selective binding and mediation of nuclear import RT of nls proteins in vitro."; RL J. Biol. Chem. 273:24083-24087(1998). RN [7] RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND INTERACTION WITH IMPORTIN RP BETA-1. RX PubMed=11124253; DOI=10.1074/jbc.m006430200; RA Jiang C.-J., Shoji K., Matsuki R., Baba A., Inagaki N., Ban H., Iwasaki T., RA Imamoto N., Yoneda Y., Deng X.-W., Yamamoto N.; RT "Molecular cloning of a novel importin alpha homologue from rice, by which RT constitutive photomorphogenic 1 (COP1) nuclear localization signal (NLS)- RT protein is preferentially nuclear imported."; RL J. Biol. Chem. 276:9322-9329(2001). RN [8] RP INTERACTION WITH MUNGBEAN YELLOW MOSAIC VIRUS CAPSID PROTEIN. RX PubMed=15914861; DOI=10.1099/vir.0.80920-0; RA Guerra-Peraza O., Kirk D., Seltzer V., Veluthambi K., Schmit A.C., Hohn T., RA Herzog E.; RT "Coat proteins of Rice tungro bacilliform virus and Mungbean yellow mosaic RT virus contain multiple nuclear-localization signals and interact with RT importin alpha."; RL J. Gen. Virol. 86:1815-1826(2005). CC -!- FUNCTION: Functions in nuclear protein import. Binds specifically and CC directly to substrates containing either a simple or bipartite NLS CC motif. Promotes docking of import substrates to the nuclear envelope. CC {ECO:0000269|PubMed:11124253, ECO:0000269|PubMed:9727027}. CC -!- SUBUNIT: Forms a complex with importin subunit beta-1. The whole CC complex, most stable and composed of importin alpha, importin beta and CC NLS substrate, is referred to as PTAC or pore targeting complex. CC Interacts with mungbean yellow mosaic virus capsid protein. CC {ECO:0000269|PubMed:11124253, ECO:0000269|PubMed:15914861}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:9727027}. CC -!- TISSUE SPECIFICITY: Highly expressed in callus, followed by root and CC etiolated leaf. Low expression in green leaf. CC {ECO:0000269|PubMed:11124253, ECO:0000269|PubMed:9678973}. CC -!- INDUCTION: In both etiolated and green leaves, down-regulated by light. CC In green leaf, increased by dark treatment. CC {ECO:0000269|PubMed:11124253, ECO:0000269|PubMed:9678973}. CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB004660; BAA31165.1; -; mRNA. DR EMBL; AF005265; AAQ13406.1; -; mRNA. DR EMBL; AB004814; BAA31166.1; -; Genomic_DNA. DR EMBL; AP000816; BAA87855.1; -; Genomic_DNA. DR EMBL; AP014957; BAS71366.1; -; Genomic_DNA. DR PDB; 2YNS; X-ray; 2.10 A; A/B=73-526. DR PDB; 4B8J; X-ray; 2.00 A; A=1-526. DR PDB; 4B8O; X-ray; 2.08 A; A=73-526. DR PDB; 4B8P; X-ray; 2.30 A; A/B=73-526. DR PDB; 4BPL; X-ray; 2.30 A; A=73-526. DR PDB; 4BQK; X-ray; 2.00 A; A/B=73-526. DR AlphaFoldDB; Q71VM4; -. DR MDposit; Q71VM4; -. DR SMR; Q71VM4; -. DR FunCoup; Q71VM4; 2198. DR IntAct; Q71VM4; 2. DR MINT; Q71VM4; -. DR STRING; 39947.Q71VM4; -. DR PaxDb; 39947-Q71VM4; -. DR EnsemblPlants; Os01t0253300-01; Os01t0253300-01; Os01g0253300. DR EnsemblPlants; Os01t0253300-02; Os01t0253300-02; Os01g0253300. DR Gramene; Os01t0253300-01; Os01t0253300-01; Os01g0253300. DR Gramene; Os01t0253300-02; Os01t0253300-02; Os01g0253300. DR eggNOG; KOG0166; Eukaryota. DR HOGENOM; CLU_018084_5_0_1; -. DR InParanoid; Q71VM4; -. DR OMA; EMIQMLY; -. DR OrthoDB; 29145at2759; -. DR EvolutionaryTrace; Q71VM4; -. DR Proteomes; UP000059680; Chromosome 1. DR ExpressionAtlas; Q71VM4; baseline and differential. DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IBA:GO_Central. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0061608; F:nuclear import signal receptor activity; IEA:InterPro. DR GO; GO:0006606; P:protein import into nucleus; IEA:InterPro. DR FunFam; 1.20.5.690:FF:000002; Importin subunit alpha; 1. DR FunFam; 1.25.10.10:FF:000040; Importin subunit alpha; 1. DR Gene3D; 1.20.5.690; Importin-alpha, importin-beta-binding domain; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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 PANTHER; PTHR23316; IMPORTIN ALPHA; 1. 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; ARM repeat; 1. DR PROSITE; PS50176; ARM_REPEAT; 4. DR PROSITE; PS51214; IBB; 1. DR PDBsum; 2YNS; -. DR PDBsum; 4B8J; -. DR PDBsum; 4B8O; -. DR PDBsum; 4B8P; -. DR PDBsum; 4BPL; -. DR PDBsum; 4BQK; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Host-virus interaction; Protein transport; KW Reference proteome; Repeat; Transport. FT CHAIN 1..526 FT /note="Importin subunit alpha-1a" FT /id="PRO_0000120740" FT DOMAIN 1..58 FT /note="IBB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561" FT REPEAT 105..145 FT /note="ARM 1" FT REPEAT 148..187 FT /note="ARM 2" FT REPEAT 190..230 FT /note="ARM 3" FT REPEAT 232..271 FT /note="ARM 4" FT REPEAT 274..313 FT /note="ARM 5" FT REPEAT 316..356 FT /note="ARM 6" FT REPEAT 359..398 FT /note="ARM 7" FT REPEAT 402..441 FT /note="ARM 8" FT CONFLICT 473..474 FT /note="LQ -> FE (in Ref. 2; AAQ13406)" FT /evidence="ECO:0000305" FT HELIX 74..82 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 86..100 FT /evidence="ECO:0007829|PDB:4BQK" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 108..113 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 117..123 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 130..144 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 148..156 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 159..166 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 172..186 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 190..198 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 202..207 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 215..229 FT /evidence="ECO:0007829|PDB:4BQK" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 234..236 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 237..240 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 243..250 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 256..269 FT /evidence="ECO:0007829|PDB:4BQK" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 274..282 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 286..292 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 298..311 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 316..323 FT /evidence="ECO:0007829|PDB:4BQK" FT TURN 324..326 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 327..336 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 341..355 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 359..368 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 371..380 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 383..399 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 402..410 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 414..419 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 420..422 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 426..449 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 456..463 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 466..473 FT /evidence="ECO:0007829|PDB:4BQK" FT HELIX 479..492 FT /evidence="ECO:0007829|PDB:4BQK" SQ SEQUENCE 526 AA; 57571 MW; 7A7DA264968FC983 CRC64; MSLRPSERVE VRRNRYKVAV DAEEGRRRRE DNMVEIRKSR REESLLKKRR EGLQAQAPVP ASAATGVDKK LESLPAMIGG VYSDDNNLQL EATTQFRKLL SIERSPPIEE VIQSGVVPRF VQFLTREDFP QLQFEAAWAL TNIASGTSEN TKVVIDHGAV PIFVKLLGSS SDDVREQAVW ALGNVAGDSP KCRDLVLANG ALLPLLAQLN EHTKLSMLRN ATWTLSNFCR GKPQPSFEQT RPALPALARL IHSNDEEVLT DACWALSYLS DGTNDKIQAV IEAGVCPRLV ELLLHPSPSV LIPALRTVGN IVTGDDAQTQ CIIDHQALPC LLSLLTQNLK KSIKKEACWT ISNITAGNKD QIQAVINAGI IGPLVNLLQT AEFDIKKEAA WAISNATSGG SHDQIKYLVS EGCIKPLCDL LICPDIRIVT VCLEGLENIL KVGETDKTLA AGDVNVFSQM IDEAEGLEKI ENLQSHDNNE IYEKAVKILE AYWMDEEDDT MGATTVAAPQ GATFDFGQGG GAAQFK //