IMB2_YEAST
ID IMB2_YEAST Reviewed; 918 AA.
AC P38217; D6VQ19;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Importin subunit beta-2 {ECO:0000250|UniProtKB:Q92973};
DE AltName: Full=Importin-104;
DE AltName: Full=Karyopherin subunit beta-2;
DE AltName: Full=Karyopherin-104 {ECO:0000303|PubMed:8849456};
DE AltName: Full=Transportin {ECO:0000250|UniProtKB:Q92973};
DE Short=TRN {ECO:0000250|UniProtKB:Q92973};
GN Name=KAP104 {ECO:0000303|PubMed:8849456};
GN OrderedLocusNames=YBR017C {ECO:0000312|SGD:S000000221}; ORFNames=YBR0224;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762304; DOI=10.1002/yea.320110110;
RA Schaaff-Gerstenschlaeger I., Schindwolf T., Lehnert W., Rose M.,
RA Zimmermann F.K.;
RT "Sequence and functional analysis of a 7.2 kb fragment of Saccharomyces
RT cerevisiae chromosome II including GAL7 and GAL10 and a new essential open
RT reading frame.";
RL Yeast 11:79-83(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NAB2; HRP1; NUP1;
RP NUP100 AND NUP106.
RX PubMed=8849456; DOI=10.1126/science.274.5287.624;
RA Aitchison J.D., Blobel G., Rout M.P.;
RT "Kap104p: a karyopherin involved in the nuclear transport of messenger RNA
RT binding proteins.";
RL Science 274:624-627(1996).
RN [5]
RP INTERACTION WITH GSP1.
RX PubMed=9321403; DOI=10.1093/emboj/16.20.6237;
RA Schlenstedt G., Smirnova E., Deane R., Solsbacher J., Kutay U.,
RA Goerlich D., Ponstingl H., Bischoff F.R.;
RT "Yrb4p, a yeast ran-GTP-binding protein involved in import of ribosomal
RT protein L25 into the nucleus.";
RL EMBO J. 16:6237-6249(1997).
RN [6]
RP FUNCTION, AND INTERACTION WITH NAB2.
RX PubMed=9488461; DOI=10.1128/mcb.18.3.1449;
RA Truant R., Fridell R.A., Benson R.E., Bogerd H., Cullen B.R.;
RT "Identification and functional characterization of a novel nuclear
RT localization signal present in the yeast Nab2 poly(A)+ RNA binding
RT protein.";
RL Mol. Cell. Biol. 18:1449-1458(1998).
RN [7]
RP FUNCTION, AND INTERACTION WITH NAB2; HRP1 AND GSP1.
RX PubMed=10506153; DOI=10.1074/jbc.274.41.29031;
RA Lee D.C., Aitchison J.D.;
RT "Kap104p-mediated nuclear import. Nuclear localization signals in mRNA-
RT binding proteins and the role of Ran and RNA.";
RL J. Biol. Chem. 274:29031-29037(1999).
RN [8]
RP REVIEW.
RX PubMed=11423015; DOI=10.1186/gb-2001-2-6-reviews3008;
RA Stroem A.C., Weis K.;
RT "Importin-beta-like nuclear transport receptors.";
RL Genome Biol. 2:REVIEWS3008.1-REVIEWS3008.9(2001).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP FUNCTION, AND INTERACTION WITH TFG2.
RX PubMed=19366694; DOI=10.1074/jbc.m809384200;
RA Suel K.E., Chook Y.M.;
RT "Kap104p imports the PY-NLS-containing transcription factor Tfg2p into the
RT nucleus.";
RL J. Biol. Chem. 284:15416-15424(2009).
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for arginine/glycine-rich nuclear
CC localization signals (rg-NLS) and PY-NLS in cargo substrates. Its
CC predominant cargo substrate seems to be mRNA-binding proteins. Required
CC for nuclear transport of NAB2, HRP1/NAB4 and TFG2. Mediates docking of
CC the importin/substrate complex to the nuclear pore complex (NPC)
CC through binding to repeat-containing nucleoporins (PubMed:8849456,
CC PubMed:9488461, PubMed:10506153, PubMed:19366694). The complex is
CC subsequently translocated through the pore by an energy requiring, Ran-
CC dependent mechanism (PubMed:11423015). At the nucleoplasmic side of the
CC NPC, GTP-Ran binding leads to release of the cargo. Efficient GTP-Ran-
CC mediated substrate release requires RNA (PubMed:10506153). The importin
CC is re-exported from the nucleus to the cytoplasm where GTP hydrolysis
CC releases Ran from importin. The directionality of nuclear import is
CC thought to be conferred by an asymmetric distribution of the GTP- and
CC GDP-bound forms of Ran between the cytoplasm and nucleus
CC (PubMed:11423015). {ECO:0000269|PubMed:10506153,
CC ECO:0000269|PubMed:19366694, ECO:0000269|PubMed:8849456,
CC ECO:0000269|PubMed:9488461, ECO:0000305|PubMed:11423015}.
CC -!- SUBUNIT: Interacts with Ran (GSP1) (PubMed:9321403, PubMed:10506153);
CC interacts specifically with the GTP-bound form of Ran (GTP-Ran),
CC protecting it from GTP hydrolysis and nucleotide exchange
CC (PubMed:9321403). Interacts with nucleoporins NUP1, NUP100 and NUP116
CC (PubMed:8849456). Interacts with NAB2 and HRP1/NAB4; via their rg-NLS
CC (PubMed:9488461, PubMed:10506153). Interacts with TFG2; via its PY-NLS
CC (PubMed:19366694). {ECO:0000269|PubMed:10506153,
CC ECO:0000269|PubMed:19366694, ECO:0000269|PubMed:8849456,
CC ECO:0000269|PubMed:9321403, ECO:0000269|PubMed:9488461}.
CC -!- INTERACTION:
CC P38217; P38333: ENP1; NbExp=2; IntAct=EBI-9152, EBI-6482;
CC P38217; Q99383: HRP1; NbExp=4; IntAct=EBI-9152, EBI-11783;
CC P38217; P32505: NAB2; NbExp=4; IntAct=EBI-9152, EBI-11770;
CC P38217; P41896: TFG2; NbExp=2; IntAct=EBI-9152, EBI-18916;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8849456}. Nucleus,
CC nuclear pore complex {ECO:0000269|PubMed:8849456}. Nucleus
CC {ECO:0000269|PubMed:8849456}. Note=Predominantly cytoplasmic.
CC {ECO:0000269|PubMed:8849456}.
CC -!- MISCELLANEOUS: Binds to nucleoporin FxFG but not PSFG repeat regions.
CC {ECO:0000269|PubMed:8849456}.
CC -!- MISCELLANEOUS: Present with 2130 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-2
CC subfamily. {ECO:0000305}.
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DR EMBL; X81324; CAA57104.1; -; Genomic_DNA.
DR EMBL; Z35886; CAA84959.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07139.1; -; Genomic_DNA.
DR PIR; S45872; S45872.
DR RefSeq; NP_009573.1; NM_001178365.1.
DR AlphaFoldDB; P38217; -.
DR SMR; P38217; -.
DR BioGRID; 32720; 254.
DR DIP; DIP-1399N; -.
DR IntAct; P38217; 111.
DR MINT; P38217; -.
DR STRING; 4932.YBR017C; -.
DR MaxQB; P38217; -.
DR PaxDb; P38217; -.
DR PRIDE; P38217; -.
DR EnsemblFungi; YBR017C_mRNA; YBR017C; YBR017C.
DR GeneID; 852305; -.
DR KEGG; sce:YBR017C; -.
DR SGD; S000000221; KAP104.
DR VEuPathDB; FungiDB:YBR017C; -.
DR eggNOG; KOG2023; Eukaryota.
DR GeneTree; ENSGT00940000174661; -.
DR HOGENOM; CLU_008136_1_1_1; -.
DR InParanoid; P38217; -.
DR OMA; MFPLLEC; -.
DR BioCyc; YEAST:G3O-29001-MON; -.
DR Reactome; R-SCE-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR PRO; PR:P38217; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38217; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:SGD.
DR GO; GO:0010458; P:exit from mitosis; IMP:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006606; P:protein import into nucleus; IDA:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR040122; Importin_beta.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF02985; HEAT; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..918
FT /note="Importin subunit beta-2"
FT /id="PRO_0000120770"
FT REPEAT 11..38
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 43..92
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 103..137
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 145..181
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 190..222
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 235..263
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 275..303
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 320..413
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 421..449
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 461..488
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 501..534
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 542..577
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 583..620
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 628..678
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 694..725
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 777..814
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 825..858
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 867..900
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REGION 361..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..393
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 103681 MW; E8010A477D1FC0B5 CRC64;
MASTWKPAED YVLQLATLLQ NCMSPNPEIR NNAMEAMENF QLQPEFLNYL CYILIEGESD
DVLKQHYSLQ DLQNNRATAG MLLKNSMLGG NNLIKSNSHD LGYVKSNIIH GLYNSNNNLV
SNVTGIVITT LFSTYYRQHR DDPTGLQMLY QLLELTSNGN EPSIKALSKI MEDSAQFFQL
EWSGNTKPME ALLDSFFRFI SNPNFSPVIR SESVKCINTV IPLQTQSFIV RLDKFLEIIF
QLAQNDENDL VRAQICISFS FLLEFRPDKL VSHLDGIVQF MLHLITTVNE EKVAIEACEF
LHAFATSPNI PEHILQPYVK DIVPILLSKM VYNEESIVLL EASNDDDAFL EDKDEDIKPI
APRIVKKKEA GNGEDADDNE DDDDDDDDED GDVDTQWNLR KCSAATLDVM TNILPHQVMD
IAFPFLREHL GSDRWFIREA TILALGAMAE GGMKYFNDGL PALIPFLVEQ LNDKWAPVRK
MTCWTLSRFS PWILQDHTEF LIPVLEPIIN TLMDKKKDVQ EAAISSVAVF IENADSELVE
TLFYSQLLTS FDKCLKYYKK KNLIILYDAI GRFAEKCALD ETAMQIILPP LIEKWALLSD
SDKELWPLLE CLSCVASSLG ERFMPMAPEV YNRAFRILCH CVELEAKSHQ DPTIVVPEKD
FIITSLDLID GLVQGLGAHS QDLLFPQGTK DLTILKIMLE CLQDPVHEVR QSCFALLGDI
VYFFNSELVI GNLEDFLKLI GTEIMHNDDS DGTPAVINAI WALGLISERI DLNTYIIDMS
RIILDLFTTN TQIVDSSVME NLSVTIGKMG LTHPEVFSSG AFANDSNWNK WCLSVNALDD
VEEKSSAYMG FLKIINLTST EVTMSNDTIH KIVTGLSSNV EANVFAQEIY TFLMNHSAQI
SAINFTPDEI SFLQQFTS
