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Importin subunit beta-2 (Importin-104) (Karyopherin subunit beta-2) (Karyopherin-104) (Transportin) (TRN)

 IMB2_YEAST              Reviewed;         918 AA.
P38217; D6VQ19;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
20-JUN-2018, entry version 152.
RecName: Full=Importin subunit beta-2 {ECO:0000250|UniProtKB:Q92973};
AltName: Full=Importin-104;
AltName: Full=Karyopherin subunit beta-2;
AltName: Full=Karyopherin-104 {ECO:0000303|PubMed:8849456};
AltName: Full=Transportin {ECO:0000250|UniProtKB:Q92973};
Short=TRN {ECO:0000250|UniProtKB:Q92973};
Name=KAP104 {ECO:0000303|PubMed:8849456};
OrderedLocusNames=YBR017C {ECO:0000312|SGD:S000000221};
ORFNames=YBR0224;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7762304; DOI=10.1002/yea.320110110;
Schaaff-Gerstenschlaeger I., Schindwolf T., Lehnert W., Rose M.,
Zimmermann F.K.;
"Sequence and functional analysis of a 7.2 kb fragment of
Saccharomyces cerevisiae chromosome II including GAL7 and GAL10 and a
new essential open reading frame.";
Yeast 11:79-83(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NAB2; HRP1; NUP1;
NUP100 AND NUP106.
PubMed=8849456; DOI=10.1126/science.274.5287.624;
Aitchison J.D., Blobel G., Rout M.P.;
"Kap104p: a karyopherin involved in the nuclear transport of messenger
RNA binding proteins.";
Science 274:624-627(1996).
[5]
INTERACTION WITH GSP1.
PubMed=9321403; DOI=10.1093/emboj/16.20.6237;
Schlenstedt G., Smirnova E., Deane R., Solsbacher J., Kutay U.,
Goerlich D., Ponstingl H., Bischoff F.R.;
"Yrb4p, a yeast ran-GTP-binding protein involved in import of
ribosomal protein L25 into the nucleus.";
EMBO J. 16:6237-6249(1997).
[6]
FUNCTION, AND INTERACTION WITH NAB2.
PubMed=9488461; DOI=10.1128/MCB.18.3.1449;
Truant R., Fridell R.A., Benson R.E., Bogerd H., Cullen B.R.;
"Identification and functional characterization of a novel nuclear
localization signal present in the yeast Nab2 poly(A)+ RNA binding
protein.";
Mol. Cell. Biol. 18:1449-1458(1998).
[7]
FUNCTION, AND INTERACTION WITH NAB2; HRP1 AND GSP1.
PubMed=10506153; DOI=10.1074/jbc.274.41.29031;
Lee D.C., Aitchison J.D.;
"Kap104p-mediated nuclear import. Nuclear localization signals in
mRNA-binding proteins and the role of Ran and RNA.";
J. Biol. Chem. 274:29031-29037(1999).
[8]
REVIEW.
PubMed=11423015; DOI=10.1186/gb-2001-2-6-reviews3008;
Stroem A.C., Weis K.;
"Importin-beta-like nuclear transport receptors.";
Genome Biol. 2:REVIEWS3008.1-REVIEWS3008.9(2001).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
FUNCTION, AND INTERACTION WITH TFG2.
PubMed=19366694; DOI=10.1074/jbc.M809384200;
Suel K.E., Chook Y.M.;
"Kap104p imports the PY-NLS-containing transcription factor Tfg2p into
the nucleus.";
J. Biol. Chem. 284:15416-15424(2009).
-!- FUNCTION: Functions in nuclear protein import as nuclear transport
receptor. Serves as receptor for arginine/glycine-rich nuclear
localization signals (rg-NLS) and PY-NLS in cargo substrates. Its
predominant cargo substrate seems to be mRNA-binding proteins.
Required for nuclear transport of NAB2, HRP1/NAB4 and TFG2.
Mediates docking of the importin/substrate complex to the nuclear
pore complex (NPC) through binding to repeat-containing
nucleoporins (PubMed:8849456, PubMed:9488461, PubMed:10506153,
PubMed:19366694). The complex is subsequently translocated through
the pore by an energy requiring, Ran-dependent mechanism
(PubMed:11423015). At the nucleoplasmic side of the NPC, GTP-Ran
binding leads to release of the cargo. Efficient GTP-Ran-mediated
substrate release requires RNA (PubMed:10506153). The importin is
re-exported from the nucleus to the cytoplasm where GTP hydrolysis
releases Ran from importin. The directionality of nuclear import
is thought to be conferred by an asymmetric distribution of the
GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus
(PubMed:11423015). {ECO:0000269|PubMed:10506153,
ECO:0000269|PubMed:19366694, ECO:0000269|PubMed:8849456,
ECO:0000269|PubMed:9488461, ECO:0000305|PubMed:11423015}.
-!- SUBUNIT: Interacts with Ran (GSP1) (PubMed:9321403,
PubMed:10506153); interacts specifically with the GTP-bound form
of Ran (GTP-Ran), protecting it from GTP hydrolysis and nucleotide
exchange (PubMed:9321403). Interacts with nucleoporins NUP1,
NUP100 and NUP116 (PubMed:8849456). Interacts with NAB2 and
HRP1/NAB4; via their rg-NLS (PubMed:9488461, PubMed:10506153).
Interacts with TFG2; via its PY-NLS (PubMed:19366694).
{ECO:0000269|PubMed:10506153, ECO:0000269|PubMed:19366694,
ECO:0000269|PubMed:8849456, ECO:0000269|PubMed:9321403,
ECO:0000269|PubMed:9488461}.
-!- INTERACTION:
P38333:ENP1; NbExp=2; IntAct=EBI-9152, EBI-6482;
Q99383:HRP1; NbExp=4; IntAct=EBI-9152, EBI-11783;
P32505:NAB2; NbExp=4; IntAct=EBI-9152, EBI-11770;
P41896:TFG2; NbExp=2; IntAct=EBI-9152, EBI-18916;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8849456}.
Nucleus, nuclear pore complex {ECO:0000269|PubMed:8849456}.
Nucleus {ECO:0000269|PubMed:8849456}. Note=Predominantly
cytoplasmic. {ECO:0000269|PubMed:8849456}.
-!- MISCELLANEOUS: Binds to nucleoporin FxFG but not PSFG repeat
regions. {ECO:0000269|PubMed:8849456}.
-!- MISCELLANEOUS: Present with 2130 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the importin beta family. Importin beta-2
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X81324; CAA57104.1; -; Genomic_DNA.
EMBL; Z35886; CAA84959.1; -; Genomic_DNA.
EMBL; BK006936; DAA07139.1; -; Genomic_DNA.
PIR; S45872; S45872.
RefSeq; NP_009573.1; NM_001178365.1.
ProteinModelPortal; P38217; -.
BioGrid; 32720; 237.
DIP; DIP-1399N; -.
IntAct; P38217; 110.
MINT; P38217; -.
STRING; 4932.YBR017C; -.
MaxQB; P38217; -.
PaxDb; P38217; -.
PRIDE; P38217; -.
EnsemblFungi; YBR017C; YBR017C; YBR017C.
GeneID; 852305; -.
KEGG; sce:YBR017C; -.
EuPathDB; FungiDB:YBR017C; -.
SGD; S000000221; KAP104.
GeneTree; ENSGT00550000074720; -.
HOGENOM; HOG000203940; -.
InParanoid; P38217; -.
OMA; VRRHVCQ; -.
OrthoDB; EOG092C0UPN; -.
BioCyc; YEAST:G3O-29001-MONOMER; -.
Reactome; R-SCE-5620924; Intraflagellar transport.
PRO; PR:P38217; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0005934; C:cellular bud tip; IDA:SGD.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0031965; C:nuclear membrane; IBA:GO_Central.
GO; GO:0034399; C:nuclear periphery; IBA:GO_Central.
GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
GO; GO:0008139; F:nuclear localization sequence binding; IDA:SGD.
GO; GO:0008565; F:protein transporter activity; IBA:GO_Central.
GO; GO:0010458; P:exit from mitosis; IMP:SGD.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
GO; GO:0006606; P:protein import into nucleus; IDA:SGD.
GO; GO:0000060; P:protein import into nucleus, translocation; IBA:GO_Central.
GO; GO:0006610; P:ribosomal protein import into nucleus; IBA:GO_Central.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000357; HEAT.
Pfam; PF02985; HEAT; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; mRNA transport; Nuclear pore complex;
Nucleus; Protein transport; Reference proteome; Repeat; Translocation;
Transport.
CHAIN 1 918 Importin subunit beta-2.
/FTId=PRO_0000120770.
REPEAT 11 38 HEAT 1. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 43 92 HEAT 2. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 103 137 HEAT 3. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 145 181 HEAT 4. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 190 222 HEAT 5. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 235 263 HEAT 6. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 275 303 HEAT 7. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 320 413 HEAT 8. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 421 449 HEAT 9. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 461 488 HEAT 10. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 501 534 HEAT 11. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 542 577 HEAT 12. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 583 620 HEAT 13. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 628 678 HEAT 14. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 694 725 HEAT 15. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 777 814 HEAT 17. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 825 858 HEAT 18. {ECO:0000250|UniProtKB:Q92973}.
REPEAT 867 900 HEAT 19. {ECO:0000250|UniProtKB:Q92973}.
COMPBIAS 373 392 Asp/Glu-rich (acidic).
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


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