位置:首页 > 蛋白库 > IMA1A_ORYSJ
IMA1A_ORYSJ
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   03-AUG-2022, entry version 107.
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   RefSeq; XP_015621115.1; XM_015765629.1.
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   PDBsum; 2YNS; -.
DR   PDBsum; 4B8J; -.
DR   PDBsum; 4B8O; -.
DR   PDBsum; 4B8P; -.
DR   PDBsum; 4BPL; -.
DR   PDBsum; 4BQK; -.
DR   AlphaFoldDB; Q71VM4; -.
DR   SMR; Q71VM4; -.
DR   IntAct; Q71VM4; 2.
DR   MINT; Q71VM4; -.
DR   STRING; 4530.OS01T0253300-01; -.
DR   PaxDb; Q71VM4; -.
DR   PRIDE; Q71VM4; -.
DR   EnsemblPlants; Os01t0253300-01; Os01t0253300-01; Os01g0253300.
DR   EnsemblPlants; Os01t0253300-02; Os01t0253300-02; Os01g0253300.
DR   GeneID; 4327117; -.
DR   Gramene; Os01t0253300-01; Os01t0253300-01; Os01g0253300.
DR   Gramene; Os01t0253300-02; Os01t0253300-02; Os01g0253300.
DR   KEGG; osa:4327117; -.
DR   eggNOG; KOG0166; Eukaryota.
DR   HOGENOM; CLU_018084_5_0_1; -.
DR   InParanoid; Q71VM4; -.
DR   OMA; EMIQMLY; -.
DR   OrthoDB; 1111872at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; Q71VM4; baseline and differential.
DR   Genevisible; Q71VM4; OS.
DR   GO; GO:0005634; C:nucleus; 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; 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; 4.
DR   PROSITE; PS51214; IBB; 1.
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           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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024