IMA_DROME
ID IMA_DROME Reviewed; 522 AA.
AC P52295; Q24431; Q95R96; Q9VL45;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Importin subunit alpha;
DE AltName: Full=Karyopherin subunit alpha;
DE AltName: Full=Pendulin;
GN Name=Pen; ORFNames=CG4799;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R;
RX PubMed=7790350; DOI=10.1083/jcb.129.6.1491;
RA Kuessel P., Frasch M.;
RT "Pendulin, a Drosophila protein with cell cycle-dependent nuclear
RT localization, is required for normal cell proliferation.";
RL J. Cell Biol. 129:1491-1507(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=7790349; DOI=10.1083/jcb.129.6.1473;
RA Torok I., Strand D., Schmitt R., Tick G., Torok T., Kiss I., Mechler B.M.;
RT "The overgrown hematopoietic organs-31 tumor suppressor gene of Drosophila
RT encodes an importin-like protein accumulating in the nucleus at the onset
RT of mitosis.";
RL J. Cell Biol. 129:1473-1489(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo, Larva, and Pupae;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-56 AND SER-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Binds specifically and directly to substrates containing
CC either a simple or bipartite NLS motif. Promotes docking of import
CC substrates to the nuclear envelope. Seems to act as a cytosolic
CC receptor for both simple and bipartite NLS motifs (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: It is required for normal cell proliferation and may serve as
CC an adapter molecule to form complexes with other proteins. May act as a
CC tumor suppressor in hematopoietic cells. May play a role in the nuclear
CC import of karyophilic proteins and some of these may be required for
CC the normal transmission and function of proliferative signals in the
CC cells.
CC -!- SUBUNIT: Forms a complex with importin beta subunit.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
CC cytoplasm and nucleus in a cell cycle-dependent manner.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the neuroblast stem
CC cells.
CC -!- DEVELOPMENTAL STAGE: High levels are detected during the first half of
CC embryogenesis reaching a maximum between 4 and 8 hours of development.
CC Protein expression increases again from the third larval instar
CC onwards. It is expressed in a maternal/early embryonic phase, and again
CC during morphogenesis in late larval and pupal stages.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the overgrown hematopoietic
CC organs-31 protein (OHO-31). {ECO:0000305|PubMed:7790349}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL29091.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; U12269; AAA85260.1; -; mRNA.
DR EMBL; X85752; CAA59753.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52853.1; -; Genomic_DNA.
DR EMBL; AY061543; AAL29091.1; ALT_SEQ; mRNA.
DR EMBL; BT003258; AAO25015.1; -; mRNA.
DR PIR; A57319; A57319.
DR RefSeq; NP_477041.1; NM_057693.5.
DR AlphaFoldDB; P52295; -.
DR SMR; P52295; -.
DR BioGRID; 60430; 51.
DR DIP; DIP-17105N; -.
DR IntAct; P52295; 5.
DR MINT; P52295; -.
DR STRING; 7227.FBpp0079527; -.
DR iPTMnet; P52295; -.
DR PaxDb; P52295; -.
DR PRIDE; P52295; -.
DR DNASU; 34338; -.
DR EnsemblMetazoa; FBtr0079937; FBpp0079527; FBgn0267727.
DR GeneID; 34338; -.
DR KEGG; dme:Dmel_CG4799; -.
DR CTD; 34338; -.
DR FlyBase; FBgn0287720; Pen.
DR VEuPathDB; VectorBase:FBgn0267727; -.
DR eggNOG; KOG0166; Eukaryota.
DR GeneTree; ENSGT01050000244891; -.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; P52295; -.
DR OMA; DQTRCVI; -.
DR OrthoDB; 1111872at2759; -.
DR PhylomeDB; P52295; -.
DR Reactome; R-DME-5693548; Sensing of DNA Double Strand Breaks.
DR SignaLink; P52295; -.
DR BioGRID-ORCS; 34338; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Pen; fly.
DR GenomeRNAi; 34338; -.
DR PRO; PR:P52295; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0267727; Expressed in cleaving embryo and 20 other tissues.
DR Genevisible; P52295; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IEA:InterPro.
DR GO; GO:0007301; P:female germline ring canal formation; IMP:FlyBase.
DR GO; GO:0042332; P:gravitaxis; IMP:FlyBase.
DR GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
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; 7.
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; 3.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..522
FT /note="Importin subunit alpha"
FT /id="PRO_0000120733"
FT DOMAIN 1..56
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 64..105
FT /note="ARM 1"
FT REPEAT 106..148
FT /note="ARM 2"
FT REPEAT 149..190
FT /note="ARM 3"
FT REPEAT 191..233
FT /note="ARM 4"
FT REPEAT 234..275
FT /note="ARM 5"
FT REPEAT 276..317
FT /note="ARM 6"
FT REPEAT 318..359
FT /note="ARM 7"
FT REPEAT 360..400
FT /note="ARM 8"
FT REPEAT 401..447
FT /note="ARM 9"
FT REPEAT 448..489
FT /note="ARM 10"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 69
FT /note="L -> P (in Ref. 1; AAA85260)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 57822 MW; B02773EB76812AD1 CRC64;
MSKADSNSRQ GSYKANSINT QDSRMRRHEV TIELRKSKKE DQMFKRRNIN DEDLTSPLKE
LNGQSPVQLS VDEIVAAMNS EDQERQFLGM QSARKMLSRE RNPPIDLMIG HGIVPICIRF
LQNTNNSMLQ FEAAWALTNI ASGTSDQTRC VIEHNAVPHF VALLQSKSMN LAEQAVWALG
NIAGDGAAAR DIVIHHNVID GILPLINNET PLSFLRNIVW LMSNLCRNKN PSPPFDQVKR
LLPVLSQLLL SQDIQVLADA CWALSYVTDD DNTKIQAVVD SDAVPRLVKL LQMDEPSIIV
PALRSVGNIV TGTDQQTDVV IASGGLPRLG LLLQHNKSNI VKEAAWTVSN ITAGNQKQIQ
AVIQAGIFQQ LRTVLEKGDF KAQKEAAWAV TNTTTSGTPE QIVDLIEKYK ILKPFIDLLD
TKDPRTIKVV QTGLSNLFAL AEKLGGTENL CLMVEEMGGL DKLETLQQHE NEEVYKKAYA
IIDTYFSNGD DEAEQELAPQ EVNGALEFNA TQPKAPEGGY TF
