KAPA_EMENI
ID KAPA_EMENI Reviewed; 553 AA.
AC G5EB89; C8VM76; Q5BBD8; Q8X175;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Importin subunit alpha {ECO:0000305};
DE AltName: Full=Karyopherin alpha {ECO:0000305};
GN Name=kapA {ECO:0000303|PubMed:19318129}; Synonyms=srp1; ORFNames=AN2142;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH HSP70; HSP90; NAPB;
RP NKUA; NUDK; AN1413 AND NIME.
RX PubMed=17890114; DOI=10.1016/j.fgb.2007.08.003;
RA Araujo-Bazan L., Fernandez-Martinez J., Rios V.M., Etxebeste O.,
RA Albar J.P., Penalva M.A., Espeso E.A.;
RT "NapA and NapB are the Aspergillus nidulans Nap/SET family members and NapB
RT is a nuclear protein specifically interacting with importin alpha.";
RL Fungal Genet. Biol. 45:278-291(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP FUNCTION.
RX PubMed=12684370; DOI=10.1128/ec.2.2.209-221.2003;
RA Nikolaev I., Cochet M.-F., Felenbok B.;
RT "Nuclear import of zinc binuclear cluster proteins proceeds through
RT multiple, overlapping transport pathways.";
RL Eukaryot. Cell 2:209-221(2003).
RN [5]
RP FUNCTION.
RX PubMed=17163983; DOI=10.1111/j.1365-2958.2006.05506.x;
RA Stinnett S.M., Espeso E.A., Cobeno L., Araujo-Bazan L., Calvo A.M.;
RT "Aspergillus nidulans VeA subcellular localization is dependent on the
RT importin alpha carrier and on light.";
RL Mol. Microbiol. 63:242-255(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-111.
RX PubMed=19318129; DOI=10.1016/j.fgb.2009.03.006;
RA Araujo-Bazan L., Dhingra S., Chu J., Fernandez-Martinez J., Calvo A.M.,
RA Espeso E.A.;
RT "Importin alpha is an essential nuclear import carrier adaptor required for
RT proper sexual and asexual development and secondary metabolism in
RT Aspergillus nidulans.";
RL Fungal Genet. Biol. 46:506-515(2009).
CC -!- FUNCTION: Import of proteins with classical NLS composed of one or two
CC clusters of basic residues is initiated by binding to the importin
CC alpha/beta heterodimer, where importin alpha acts as an adapter subunit
CC to bridge NLS cargos to importin beta, which transports the whole
CC complex through the nuclear envelope (PubMed:12684370). Involved in the
CC nuclear accumulation of the light-dependent developmental regulator veA
CC (PubMed:17163983, PubMed:19318129). Participates at different
CC regulatory stages of asexual and sexual development, being required for
CC the completion of both reproductive cycles with the formation of
CC conidiospores and ascospores, respectively (PubMed:19318129). Mediates
CC secondary metabolite gene expression with positive regulation of
CC penicillin production and negative regulation of mycotoxin biosynthesis
CC (PubMed:19318129). {ECO:0000269|PubMed:12684370,
CC ECO:0000269|PubMed:17163983, ECO:0000269|PubMed:19318129}.
CC -!- SUBUNIT: Forms a complex with an importin beta subunit (By similarity).
CC Interacts with hsp70, hsp90, napB, nkuA, nudK, AN1413 and nimE
CC (PubMed:17890114). {ECO:0000250|UniProtKB:Q02821,
CC ECO:0000269|PubMed:17890114}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B6HJ92}.
CC -!- DISRUPTION PHENOTYPE: Leads to lethality (PubMed:19318129).
CC {ECO:0000269|PubMed:19318129}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; AF465210; AAL69976.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF86262.1; -; Genomic_DNA.
DR EMBL; AACD01000034; EAA64186.1; -; Genomic_DNA.
DR RefSeq; XP_659746.1; XM_654654.1.
DR AlphaFoldDB; G5EB89; -.
DR SMR; G5EB89; -.
DR STRING; 162425.CADANIAP00008820; -.
DR EnsemblFungi; CBF86262; CBF86262; ANIA_02142.
DR EnsemblFungi; EAA64186; EAA64186; AN2142.2.
DR GeneID; 2875733; -.
DR KEGG; ani:AN2142.2; -.
DR VEuPathDB; FungiDB:AN2142; -.
DR eggNOG; KOG0166; Eukaryota.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; G5EB89; -.
DR OMA; EMIQMLY; -.
DR OrthoDB; 1111872at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IDA:AspGD.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
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 GO; GO:0006606; P:protein import into nucleus; IMP:AspGD.
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; 3.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Nucleus; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..553
FT /note="Importin subunit alpha"
FT /id="PRO_0000435924"
FT DOMAIN 1..58
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 115..154
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 157..196
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 199..239
FT /note="ARM 3"
FT /evidence="ECO:0000255"
FT REPEAT 242..281
FT /note="ARM 4"
FT /evidence="ECO:0000255"
FT REPEAT 284..323
FT /note="ARM 5"
FT /evidence="ECO:0000255"
FT REPEAT 326..365
FT /note="ARM 6"
FT /evidence="ECO:0000255"
FT REPEAT 368..407
FT /note="ARM 7"
FT /evidence="ECO:0000255"
FT REPEAT 413..452
FT /note="ARM 8"
FT /evidence="ECO:0000255"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 111
FT /note="S->F: Leads to thermosensitivity and affects nuclear
FT import at the restrictive temperature."
FT /evidence="ECO:0000269|PubMed:19318129"
SQ SEQUENCE 553 AA; 60627 MW; FEA035D324290A2A CRC64;
MAERYIPEHR RTQYKARNQF RPDELRRRRE EQQVEIRKQK REENLAKRRG IQTRDGGIGV
GGGMAAAESD DEASAIESEL NVELPEMVKG VFSDQIEAQI QATTKFRKLL SKERNPPIER
VIETGVVSRF VEFLRSPHTL VQFEAAWALT NIASGSAQQT QVVIEAGAVP IFVELLSSPE
PDVREQAVWA LGNIAGDSPQ CRDFVLNAGA LRPLLTLIND GRKISMLRNA TWTLSNFCRG
KTPQPDWNTI APALPVLAKL IYMLDDEVLI DACWAISYLS DGPNEKIQAV IEAGIPRRLV
ELLMHASTSV QTPALRSVGN IVTGDDVQTQ VIINCGALPA LLSLLSSTKD GIRKEACWTI
SNITAGNSSQ IQSVIDAGII PPLVHLLANG DFKTRKEACW AISNATSGGL QKPDQIRYLV
TQGCIKPLCD LLACPDNKII QVALDGLENI LKVGEMDKEA GQGDAHVNRY ALFIEEAGGM
EKIHDCQNNA NEEIYMKAYN IIEKYFSDED EAAGDIDELA PQQTQTGFTL GATQQQPGGF
SFGGANGGDS MDM
