KA122_YEAST
ID KA122_YEAST Reviewed; 1081 AA.
AC P32767; D6VUC1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Importin beta-like protein KAP122;
DE AltName: Full=Karyopherin-122;
DE AltName: Full=Pleiotropic drug resistance regulatory protein 6;
GN Name=KAP122; Synonyms=PDR6; OrderedLocusNames=YGL016W;
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], AND FUNCTION.
RC STRAIN=ATCC 46191 / IL125-2B;
RX PubMed=1882553; DOI=10.1002/yea.320070311;
RA Chen W., Balzi E., Capieaux E., Choder M., Goffeau A.;
RT "The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1 and
RT ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals the PDR6
RT gene, a new member of the genetic network controlling pleiotropic drug
RT resistance.";
RL Yeast 7:287-299(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 SUBCELLULAR LOCATION, INTERACTION WITH NUP1; NUP2; TOA1 AND TOA2, AND
RP FUNCTION.
RX PubMed=10525531; DOI=10.1083/jcb.147.2.235;
RA Titov A.A., Blobel G.;
RT "The karyopherin Kap122p/Pdr6p imports both subunits of the transcription
RT factor IIA into the nucleus.";
RL J. Cell Biol. 147:235-246(1999).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GSP2.
RX PubMed=10617640; DOI=10.1074/jbc.275.1.467;
RA Lau D., Kunzler M., Braunwarth A., Hellmuth K., Podtelejnikov A., Mann M.,
RA Hurt E.;
RT "Purification of protein A-tagged yeast ran reveals association with a
RT novel karyopherin beta family member, Pdr6p.";
RL J. Biol. Chem. 275:467-471(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ASSOCIATION WITH THE NUCLEAR PORE
RP COMPLEX.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [7]
RP FUNCTION, AND INTERACTION WITH WTM1.
RX PubMed=16432237; DOI=10.1073/pnas.0510516103;
RA Zhang Z., An X., Yang K., Perlstein D.L., Hicks L., Kelleher N., Stubbe J.,
RA Huang M.;
RT "Nuclear localization of the Saccharomyces cerevisiae ribonucleotide
RT reductase small subunit requires a karyopherin and a WD40 repeat protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:1422-1427(2006).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=18838542; DOI=10.1128/mcb.01388-08;
RA Wu X., Huang M.;
RT "Dif1 controls subcellular localization of ribonucleotide reductase by
RT mediating nuclear import of the R2 subunit.";
RL Mol. Cell. Biol. 28:7156-7167(2008).
CC -!- FUNCTION: Nuclear transport factor (karyopherin) involved in protein
CC transport between the cytoplasm and nucleoplasm. Required for the
CC nuclear import of the complex composed the large subunit (TOA1) and the
CC small subunit (TOA2) of the general transcription factor IIA (TFIIA).
CC Required for the nuclear import of the RNR2-RNR4 heterodimer, also
CC called beta-beta' subunit, which corresponds to the small subunit of
CC the ribonucleotide reductase (RNR). May play a role in regulation of
CC pleiotropic drug resistance. {ECO:0000269|PubMed:10525531,
CC ECO:0000269|PubMed:16432237, ECO:0000269|PubMed:1882553,
CC ECO:0000269|PubMed:18838542}.
CC -!- SUBUNIT: Associates with the nuclear pore complex (NPC). Interacts with
CC GSP2, NUP1, NUP2, TOA1, TOA2 and WTM1. {ECO:0000269|PubMed:10525531,
CC ECO:0000269|PubMed:10617640, ECO:0000269|PubMed:16432237}.
CC -!- INTERACTION:
CC P32767; Q12363: WTM1; NbExp=2; IntAct=EBI-13044, EBI-20563;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:10525531,
CC ECO:0000269|PubMed:10617640}.
CC -!- MISCELLANEOUS: Present with 9760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
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DR EMBL; S58126; AAD13901.1; -; Genomic_DNA.
DR EMBL; S57895; AAB19613.1; -; Genomic_DNA.
DR EMBL; Z72538; CAA96716.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08082.1; -; Genomic_DNA.
DR PIR; S15040; S15040.
DR RefSeq; NP_011499.1; NM_001180881.1.
DR PDB; 6Q82; X-ray; 2.99 A; A=2-1081.
DR PDB; 6Q83; X-ray; 4.53 A; A=2-1081.
DR PDB; 6Q84; X-ray; 3.70 A; A/D=2-1081.
DR PDBsum; 6Q82; -.
DR PDBsum; 6Q83; -.
DR PDBsum; 6Q84; -.
DR AlphaFoldDB; P32767; -.
DR SMR; P32767; -.
DR BioGRID; 33230; 272.
DR DIP; DIP-2449N; -.
DR IntAct; P32767; 17.
DR MINT; P32767; -.
DR STRING; 4932.YGL016W; -.
DR iPTMnet; P32767; -.
DR MaxQB; P32767; -.
DR PaxDb; P32767; -.
DR PRIDE; P32767; -.
DR EnsemblFungi; YGL016W_mRNA; YGL016W; YGL016W.
DR GeneID; 852868; -.
DR KEGG; sce:YGL016W; -.
DR SGD; S000002984; KAP122.
DR VEuPathDB; FungiDB:YGL016W; -.
DR eggNOG; KOG2022; Eukaryota.
DR GeneTree; ENSGT00530000063347; -.
DR HOGENOM; CLU_284018_0_0_1; -.
DR InParanoid; P32767; -.
DR OMA; CFEKLKY; -.
DR BioCyc; YEAST:G3O-30537-MON; -.
DR PRO; PR:P32767; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32767; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IDA:SGD.
DR GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Transport.
FT CHAIN 1..1081
FT /note="Importin beta-like protein KAP122"
FT /id="PRO_0000058276"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:6Q82"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 81..98
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 109..125
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 187..210
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 217..223
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 246..261
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 316..327
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 359..373
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 377..385
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 398..412
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 429..440
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 451..469
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 472..482
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 486..509
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 510..514
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 515..523
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 538..556
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 565..571
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 576..588
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 595..621
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 626..642
FT /evidence="ECO:0007829|PDB:6Q82"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 651..671
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 673..676
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 677..679
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 680..690
FT /evidence="ECO:0007829|PDB:6Q82"
FT STRAND 691..697
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 699..714
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 721..745
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 750..769
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 782..795
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 800..812
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 815..818
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 821..832
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 833..836
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 849..859
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 860..862
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 865..882
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 883..886
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 889..899
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 901..903
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 904..907
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 908..910
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 912..928
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 930..934
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 937..942
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 943..949
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 950..952
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 956..971
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 977..989
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 991..1004
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 1011..1023
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 1025..1035
FT /evidence="ECO:0007829|PDB:6Q82"
FT TURN 1036..1038
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 1045..1057
FT /evidence="ECO:0007829|PDB:6Q82"
FT STRAND 1059..1061
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 1064..1070
FT /evidence="ECO:0007829|PDB:6Q82"
FT HELIX 1072..1075
FT /evidence="ECO:0007829|PDB:6Q82"
SQ SEQUENCE 1081 AA; 123531 MW; EEBC5ADD4E16D9D3 CRC64;
MSSIHEVVAL IEELYSPHPK HDVNQIQQSL QSIQKSEQGF HLANELLSDD KYSANVKYFG
ALTLTVQLNT RGENDYETLW NVFRSNLLYL TKFSTLYVSN PNMYGQSLII IKKLMSNLSL
IFTKINDPQL NNAGNENMIK QWNNPINTFI QLMSVQNQNI NADQLLLDSI NCSLTYEQLS
QFVSLSQKHN ELALTFTEVI VEDLTKFQTK RHSMSQIHEV VHEHLYISTM ALINLNLTAQ
AVFNPTVFDC ITAWINYISL TRSVSSSGRM DLSEIFQNLI DLMYQSTEGS DGYENAEKIL
TIFGNVFAND PLLMSYDLRQ QIECIFLGVV RPDSGITDIS NKNSWMLQYM NYLVTNDFFS
ELKELAICIV DFLQINTLSV CNKLFTNIQA ADNGQVQDEY IQEYIKVLLQ MTNFPLTPVL
QEFFSVRMVD FWLDLSDAYT NLASETLRPN SIELSTQIFQ QLINIYLPKI SLSVKQRIIE
EEGESTSVNE FEDFRNAVSD LAQSLWSILG NDNLTNVLID GMGQMPAASD ETLIIKDTDV
LFRIETMCFV LNTILVDMTL SESPWIKNIV DANKFFNQNV ISVFQTGFQT SASTKVSQIL
KLDFVRTSTT LIGTLAGYFK QEPFQLNPYV EALFQGLHTC TNFTSKNEQE KISNDKLEVM
VIKTVSTLCE TCREELTPYL MHFISFLNTV IMPDSNVSHF TRTKLVRSIG YVVQCQVSNG
PEEQAKYILQ LTNLLSGSIE HCLASSVQLQ EQQDYINCLL YCISELATSL IQPTEIIEND
ALLQRLSEFQ SFWSSDPLQI RSKIMCTIDK VLDNSIYCKN SAFVEIGCLI VGKGLNLPDG
EPYFLKYNMS EVMNFVLRHV PNCELATCLP YFVYLLEKLI SEFRKELTPQ EFDFMFEKIL
LVYYDAYIIN DPDLLQMTIG FVNNVLDVKP GLAIGSKHWT SFILPQFLKL IPSREKFTIV
AVAKFWTKLI NNKKYNQEEL TTVRQQVSSI GGDLVYQIMY GLFHTQRSDL NSYTDLLRAL
VAKFPIEARE WLVAVLPQIC NNPAGHEKFI NKLLITRGSR AAGNVILQWW LDCTTLPNYQ
G
